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8-azaATP + alpha-D-glucose 1-phosphate
diphosphate + 8-azaADP-glucose
-
the photoaffinity labeling agent is used as a site specific probe of enzyme
reverse reaction is biphasic
r
8-N3-ATP + alpha-D-glucose 1-phosphate
8-N3-ADP-D-glucose + diphosphate
-
both the large and small subunit in the heterotetrameric form are labeled at equivalent rates with 8-N3-ATP, an analog which can readily substitute for ATP in catalysis
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
ATP + alpha-D-glucose-1-phosphate
ADP-D-glucose + diphosphate
ATP + alpha-D-glucose-1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-mannose 1-phosphate
diphosphate + ADP-mannose
the catalytic efficiency with glucose 1-phosphate is at least one order of magnitude higher than that with mannose 1-phosphate
-
-
r
diphosphate + ADP
ATP + alpha-D-glucose
diphosphate + ADP-glucose
ATP + alpha-D-glucose 1-phosphate
GTP + alpha-D-glucose 1-phosphate
diphosphate + GDP-glucose
-
can somewhat replace ATP
-
-
?
additional information
?
-
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
key step in glucan synthesis, the ADPGlc PPases are highly regulated by allosteric activators and inhibitors in accord with the carbon metabolism pathways of the organism
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
first committed step of starch biosynthesis in higher plants, identification of identify AGP isoforms essential for this biosynthetic process in sink and source tissues of rice plants
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
substrate binding structure and kinetics, regulation of wild-type and mutant enzymes, mapping the polymorphic sites important in altered allosteric properties, overview
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
the small subunit displays both catalytic and regulatory properties, the large subunit possesses catalytic and regulatory properties only when assembled with small subunit, the net properties of the heterotetrameric enzyme is a product of subunit synergy, overview
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
Sorghum sp.
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
AGPase, a key regulatory enzyme in starch biosynthesis, is highly regulated, effects of substrates, detailed overview
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
the enzyme is required for starch biosynthesis, while Tdy1 is not required, although tdy1-R mutant leaves retain large amounts of starch on prolonged dark treatment, consistent with a defect in starch catabolism, overview
-
-
?
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
substrate binding structure and kinetics, regulation of wild-type and mutant enzymes, mapping the polymorphic sites important in altered allosteric properties, overview
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: ITP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate are GTP, dATP, CTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: dTTP, XTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate are alpha-D-mannose 1-phosphate or alpha-D-galactose 1-phosphate
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
different large subunit isoforms allow the enzyme to be efficiently regulated according to the metabolic situation and the starch necessities of a tissue. In source tissues, ADP-glucose diphosphorylase would be finely regulated by the 3-phosphoglycerate/phosphate ratio, whereas in sink tissues, the enzyme would be dependent on the availability of substrates for starch synthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Escherichia aurescens
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Escherichia aurescens
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Escherichia aurescens
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Escherichia aurescens
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Escherichia aurescens
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
substrate binding studies: 1 mol glucose 1-phosphate per mol subunit, 4 mol ADP-glucose per mol tetrameric enzyme
-
?, r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
substrate binding studies: 1 mol glucose 1-phosphate per mol subunit, 4 mol ADP-glucose per mol tetrameric enzyme
-
?, r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
substrate binding studies: 1 mol glucose 1-phosphate per mol subunit, 4 mol ADP-glucose per mol tetrameric enzyme
-
?, r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: ITP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate are GTP, dATP, CTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: dTTP, XTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
first step of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ADP-glucose in the reverse direction
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate is UTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
the catalytic efficiency for ATP is not dependent upon the divalent metal ion
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first step of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
the reduction of cytosolic ADP-glucose pyrophosphorylase activity in shrunken endosperm did not inhibit granule initiation but severely restrained the subsequent enlargement of granules
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Rhodobacter gelatinosa
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Rhodobacter gelatinosa
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Rhodobacter globiformis
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Rhodobacter globiformis
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: ITP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: ITP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate are GTP, dATP, CTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate are GTP, dATP, CTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: dTTP, XTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: dTTP, XTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
ADP-glucose synthesis at 50%, strain 274 or 75%, strain 15365 the rate of pyrophosphorolysis
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
ADP-glucose pyrophosphorylase catalyzes the first committed and rate-limiting step in starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch synthesis, both subunits are involved in the allosteric regulation of AGPase
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
enzyme consists of two regulatory large subunits and two catalytic small subunits. Allosterism and catalysis are the products of an interplay between the regulatory large subunits and the catalytic small subunits that result in a synergistic response to the allosteric effectors and substrates
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Sorghum sp.
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Sorghum sp.
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Sorghum sp.
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Sorghum sp.
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
enzyme is specific for ATP and reaches similar activities in the directions of ADP-glucose synthesis or diphosphorolysis
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
enzyme is specific for ATP and reaches similar activities in the directions of ADP-glucose synthesis or diphosphorolysis
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: ITP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate are GTP, dATP, CTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate is UTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: ITP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate are GTP, dATP, CTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate is UTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: TTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate is UTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose-1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose-1-phosphate
ADP-D-glucose + diphosphate
-
AGP plays a crucial role in the morphogenesis of petal limbs in Xanthi through the synthesis of starch, which is the main carbohydrate source for expansion growth of petal limbs, in sepal tisues, overview
-
-
r
diphosphate + ADP
ATP + alpha-D-glucose
-
-
-
-
r
diphosphate + ADP
ATP + alpha-D-glucose
-
-
-
-
r
diphosphate + ADP
ATP + alpha-D-glucose
-
-
-
r
diphosphate + ADP-glucose
ATP + alpha-D-glucose 1-phosphate
-
-
-
r
diphosphate + ADP-glucose
ATP + alpha-D-glucose 1-phosphate
enzyme reaches similar activities in the directions of ADP-glucose synthesis or diphosphorolysis
-
-
r
diphosphate + ADP-glucose
ATP + alpha-D-glucose 1-phosphate
enzyme reaches similar activities in the directions of ADP-glucose synthesis or diphosphorolysis
-
-
r
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
identification of regions critically affecting kinetics and allosteric regulation of the ADP-glucose pyrophosphorylase, structure-function analysis, homology modelling, overview
-
-
?
additional information
?
-
-
enzyme displays a regulatory mechanism where the interaction with the allosteric activator triggers conformational changes at the level of loops containing residues Trp113 and Gln74
-
-
?
additional information
?
-
-
AGPase plays a key role in regulating starch biosynthesis in cereal seeds and is likely the most important determinant of seed strength
-
-
?
additional information
?
-
-
AGPase plays a key role in regulating starch biosynthesis in cereal seeds and is likely the most important determinant of seed strength
-
-
?
additional information
?
-
-
a key enzyme in starch biosynthesis, its expression is regulated at both the transcriptional and post-transcriptional levels during fruit ripening, overview
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
enzyme is able to accept UTP, CTP, dTTP and GTP with catalytic efficiencies below 1% of that with ATP
-
-
?
additional information
?
-
-
enzyme is able to accept UTP, CTP, dTTP and GTP with catalytic efficiencies below 1% of that with ATP
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
the large subunit is required for AGPase activity in leaf blades
-
-
?
additional information
?
-
-
elevated CO2 and increasing growth temperatures significantly increase activity of adenosine-5'-diphosphoglucose pyrophosphorylase. The upregulation of leaf carbohydrate metabolism enzymes under elevated CO2 plus temperature would be beneficial for growth and productivity of kidney bean in future climates
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
presence of 3-phosphoglycerate increases the velocity and the affinity for glucose 1-phosphate for the potato enzymes. Redox state does not affect kcat of the two potato isoforms. Without 3-phosphoglycerate the oxidized potato enzyme exhibits a rapid equilibrium random bi-bi mechanism with a dead end ternary complex
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis. The heat lability of maize endosperm AGPase contributes to yield loss caused by heat stress, overview
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in seed starch biosynthesis
-
-
?
additional information
?
-
in presence of 3-phosphoglycerate, enzyme follows a Theorell-Chance bi-bi mechanism with ATP binding first and ADP-Glc releasing last. 3-Phosphoglycerate increases the binding affinity for both substrates with little effect on velocity for the maize and chimeric maize/potato isoforms
-
-
?
additional information
?
-
-
in presence of 3-phosphoglycerate, enzyme follows a Theorell-Chance bi-bi mechanism with ATP binding first and ADP-Glc releasing last. 3-Phosphoglycerate increases the binding affinity for both substrates with little effect on velocity for the maize and chimeric maize/potato isoforms
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
ATP + alpha-D-glucose-1-phosphate
ADP-D-glucose + diphosphate
-
AGP plays a crucial role in the morphogenesis of petal limbs in Xanthi through the synthesis of starch, which is the main carbohydrate source for expansion growth of petal limbs, in sepal tisues, overview
-
-
r
additional information
?
-
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
key step in glucan synthesis, the ADPGlc PPases are highly regulated by allosteric activators and inhibitors in accord with the carbon metabolism pathways of the organism
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
first committed step of starch biosynthesis in higher plants, identification of identify AGP isoforms essential for this biosynthetic process in sink and source tissues of rice plants
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
Sorghum sp.
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
AGPase, a key regulatory enzyme in starch biosynthesis, is highly regulated, effects of substrates, detailed overview
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
the enzyme is required for starch biosynthesis, while Tdy1 is not required, although tdy1-R mutant leaves retain large amounts of starch on prolonged dark treatment, consistent with a defect in starch catabolism, overview
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
different large subunit isoforms allow the enzyme to be efficiently regulated according to the metabolic situation and the starch necessities of a tissue. In source tissues, ADP-glucose diphosphorylase would be finely regulated by the 3-phosphoglycerate/phosphate ratio, whereas in sink tissues, the enzyme would be dependent on the availability of substrates for starch synthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Escherichia aurescens
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Escherichia aurescens
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Escherichia aurescens
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
first step of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first step of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
the reduction of cytosolic ADP-glucose pyrophosphorylase activity in shrunken endosperm did not inhibit granule initiation but severely restrained the subsequent enlargement of granules
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Rhodobacter gelatinosa
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Rhodobacter globiformis
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
ADP-glucose pyrophosphorylase catalyzes the first committed and rate-limiting step in starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch synthesis, both subunits are involved in the allosteric regulation of AGPase
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Sorghum sp.
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Sorghum sp.
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
Sorghum sp.
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
AGPase plays a key role in regulating starch biosynthesis in cereal seeds and is likely the most important determinant of seed strength
-
-
?
additional information
?
-
-
AGPase plays a key role in regulating starch biosynthesis in cereal seeds and is likely the most important determinant of seed strength
-
-
?
additional information
?
-
-
a key enzyme in starch biosynthesis, its expression is regulated at both the transcriptional and post-transcriptional levels during fruit ripening, overview
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
the large subunit is required for AGPase activity in leaf blades
-
-
?
additional information
?
-
-
elevated CO2 and increasing growth temperatures significantly increase activity of adenosine-5'-diphosphoglucose pyrophosphorylase. The upregulation of leaf carbohydrate metabolism enzymes under elevated CO2 plus temperature would be beneficial for growth and productivity of kidney bean in future climates
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis. The heat lability of maize endosperm AGPase contributes to yield loss caused by heat stress, overview
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in seed starch biosynthesis
-
-
?
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1,6-Hexanediol bisphosphate
2-deoxy-D-ribose 5-phosphate
2-keto-3-deoxy phosphogluconate
2-mercaptoethanol
-
activation, at high concentration
3-Phosphoglyceric acid
-
-
4-Pyridoxic acid 5-phosphate
-
activation
6-phosphogluconate
-
slight activation
ADP-D-glucose
-
activation of mutant Mos(1-198) is reduced compared to the wild-type enzyme, overview
ADP-glucose
-
in the absence of 3-phosphoglycerate, ADP-glucose stimulates catalytic acitvity, acting as a feedback product activator
cysteine
-
slight activation, at high concentration
D-arabinitol 1,5-diphosphate
-
activation
D-fructose
-
25 mM, 1.3fold stimulation, enzyme from maize endosperm
D-fructose 1,6-bisphosphate
D-fructose 1,6-diphosphate
D-Fructose 1-phosphate
-
activation, less effective than D-fructose 6-phosphate
D-Glucose 1,6-bisphosphate
D-ribose 5-phosphate-1-diphosphate
-
activation
dihydroxyacetone phosphate
dithiothreitol
-
in absence of 3-phosphoglycerate, increase of acitivity for enzyme from tuber, no effect on enzyme from leaf
fructose 1,6-bisphosphate
Fruf-beta-(2->1)-6-O-P-Glcp
-
-
glyceraldehyde 3-phosphate
Glycerol 1,3-diphosphate
-
activation
GSH
-
activation, at high concentration
Phenylglyoxal
-
activation at pH 7
Phosphoglycolate
-
slight activation, ADP-glucose synthesis
sedoheptulose 1,7-diphosphate
Sodium oxamate
-
activation, structural analog of pyruvate
sucrose
-
the activity of ibAGP1 promoter is sucrose inducible
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
Escherichia aurescens
-
activation
1,6-Hexanediol bisphosphate
-
-
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
D-fructose 1,6-bisphosphate analog, most effective
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
Sorghum sp.
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
1,6-Hexanediol bisphosphate
-
activation
2,3-diphosphoglycerate
-
no activation
2,3-diphosphoglycerate
-
activation
2,3-diphosphoglycerate
-
allosteric activator
2,3-diphosphoglycerate
-
no activation
2,3-diphosphoglycerate
-
activation
2,3-diphosphoglycerate
-
actvation of ADP-glucose synthesis
2,3-diphosphoglycerate
-
no activation
2,3-diphosphoglycerate
-
no activation
2-deoxy-D-ribose 5-phosphate
-
no activation
2-deoxy-D-ribose 5-phosphate
-
activation, pyrophosphorolysis
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
Escherichia aurescens
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
fructose 6-phosphate and pyruvate analog, less effective than fructose bisphosphate
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
Sorghum sp.
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-keto-3-deoxy phosphogluconate
-
activation
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
Escherichia aurescens
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
Sorghum sp.
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-oxobutyrate
-
slight activation, pyruvate analog
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
activation
2-phospho-D-glycerate
-
slight activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
activation
2-phospho-D-glycerate
-
slight activation
2-phospho-D-glycerate
-
pyrophosphorolysis
2-phospho-D-glycerate
-
activation
2-phospho-D-glycerate
-
no activation
2-phospho-D-glycerate
-
no activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
no activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
allosteric activation
3-phosphoglycerate
-
kinetics
3-phosphoglycerate
-
kinetic study at different temperatures
3-phosphoglycerate
-
the polyethylene glycerol induced molecular crowding increases the sensitivity of enzyme to the cross-talk between 3-phosphoglycerate and phosphate, the ultrasensitive behaviour is correlated with intramolecular conformational changes induced in the tertiary structure of the homotetrameric enzyme
3-phosphoglycerate
-
allosteric activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
kinetic study and comparison of activation of recombinant enzymes, the activation is more drastic for recombinant enzyme APS1/APL1
3-phosphoglycerate
-
generation of hybrid enzymes using Solanum tuberosum large subunit and Arabidopsis thaliana small subunit. Hybrid potato small subunit with Arabidopsis large subunit APL1 is extremely sensitive against 3-phosphoglycerate and phosphate, while hybrid potato small subunit with Arabidosis large subunit APL2 is rather insensitive to both
3-phosphoglycerate
-
wild-type, half-maximal activation at 0.016 mM, mutant A33K, at 0.0055 mM, mutant G96N, at 0.0064 mM, mutant A33K/G96N, at 0.0066 mM
3-phosphoglycerate
-
in leaves 2fold, DTT abolishes the activation at 5 mM
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
allosteric activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
no activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
Escherichia aurescens
-
activation
3-phosphoglycerate
Escherichia aurescens
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
in leaves 2-3fold, DTT highly decreases the activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
no activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
slight activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
strong
3-phosphoglycerate
endospermal enzyme
3-phosphoglycerate
-
activator follows hyberbolic kinetic
3-phosphoglycerate
-
recombinant enzyme is insensitive to 3-phosphoglycerate
3-phosphoglycerate
-
in leaves 2fold, DTT decreases the activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
no activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
half-maximal activation at 0.25 mM for long day photoperiod, at 0.33 mM at short day photoperiod
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
activation kinetics. 50% of the maximal velocity at 0.075 mM
3-phosphoglycerate
-
activation
3-phosphoglycerate
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
very little enzymatic activity in the absence of 3-phosphoglycerate, 40fold in catalytic activity, when assayed und near saturating 3-phosphoglycerate concentration
3-phosphoglycerate
-
strong
3-phosphoglycerate
-
activation kinetics. Wild-type tetramer, 50% of the maximal velocity at 0.54 mM. Tetramer carrying mutation D148A in small subunit, 50% of the maximal velocity at 0.003 mM. Tetramer carrying mutation D171A in large subunit, 50% of the maximal velocity at 0.067 mM
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
no activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
no activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
no activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
slight activation
3-phosphoglycerate
-
no activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
no activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
in leaves 2-3fold, DTT decreases the activation
3-phosphoglycerate
activation of the heterotetramer comprised of large subunit isoform L1 and small subunit S is almost completely dependent on 3-phosphoglycerate. The heterotetramer comprised of large subunit isoform L3 and small subunit S shows approx. 20% of its maximal activity even in the absence of 3-phosphoglycerate
3-phosphoglycerate
-
activates
3-phosphoglycerate
-
allosteric activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
the activities of recombinant maize and recombinant potato enzyme are comparable in the presence of 10 mM 3-phosphoglycerate, however in absence of 3-phosphoglycerate and phosphate the maize enzyme exhibits approximately 20fold more activity than does potato enzyme, in presence of both 3-phosphoglycerate and phosphate the maize enzyme is 47fold active than is the potato enzyme
3-phosphoglycerate
-
the homotetrameric small subunit has much lower affinity for activator than the heterotetrameric enzyme
3-phosphoglycerate
-
strong
3-phosphoglycerate
50% activation at 0.12 mM for wild-type, at 1.38 mM for mutant D157E, at 0.03 mM for mutant K41R of large subunit plus D143N of small subunit
3-phosphoglycerate
-
50% activation of wild-type at 0.04 mM, of mutation P52L, large subunit, at 0.27 mM, of mutation P52L, large subunit, plus mutation L46F, small subunit at 0.1 mM, of mutation P52L, large subunit, plus mutation P112L, small subunit at 0.14 mM, of mutation P52L, large subunit, plus mutation P308L, small subunit at 0.006 mM, of mutation P52L, large subunit, plus mutation R350K, small subunit at 0.01 mM
3-phosphoglycerate
-
50% of maximal activation for wild-type at 0.11 mM, for mutant P17L at 0.08 mM, for mutant P26L at 0.15 mM, for mutant P44L at 0.25 mM, for mutant P52L at 0.77 mM, for mutant P55L at 0.26 mM, for mutant P66L at 0.03 mM
3-phosphoglycerate
-
generation of hybrid enzymes using Solanum tuberosum large subunit and Arabidopsis thaliana small subunit. Hybrid potato small subunit with Arabidopsis large subunit APL1 is extremely sensitive against 3-phosphoglycerate and phosphate, while hybrid potato small subunit with Arabidosis large subunit APL2 is rather insensitive to both
3-phosphoglycerate
-
allosterin activator
3-phosphoglycerate
-
in leaves and tubers 1.4-3.8fold, DTT decreases the activation, overview
3-phosphoglycerate
-
activation kinetics. 50% of the maximal velocity at 0.054 mM
3-phosphoglycerate
A0.5 value for wild-type 0.28 mm, for large subunit E370G/small subunit wild-type 0.83 mM
3-phosphoglycerate
activation. A0.5 value and Hill coefficient for wild-type 0.076 mM and 1.0, large subunit mutant E38K 0.013 mM and 0.9, large subunit mutant G101N 0.023 mM and 1.0, large subunit mutant E38K/G101N 0.006 mM and 0.4
3-phosphoglycerate
-
presence of 3-phosphoglycerate increases the velocity and the affinity for glucose 1-phosphate for the potato enzymes. Redox state does not affect kcat of the two potato isoforms. Without 3-phosphoglycerate the oxidized potato enzyme exhibits a rapid equilibrium random bi-bi mechanism with a dead end ternary complex. Activation constant Ka is 0.52 for the oxidized and 0.20 for the reduced enzyme and 0.03 for the chimeric enzyme
3-phosphoglycerate
Sorghum sp.
-
activation
3-phosphoglycerate
Sorghum sp.
-
pH-dependent
3-phosphoglycerate
Sorghum sp.
-
slight activation, DTT abolishes the activation
3-phosphoglycerate
-
allosteric activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
strong
3-phosphoglycerate
-
in leaves 30fold, DTT abolishes the activation at 1-5 mM
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
kinetics
3-phosphoglycerate
-
allosteric activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
kinetics
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
minimal activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
activation of leaf enzyme, however endosperm enzyme only, when phosphate, ADP or fructose 1,6-bisphosphate are present
3-phosphoglycerate
-
only 2fold stimulation at 15 mM 3-phosphoglycerate
3-phosphoglycerate
-
in leaves 2fold, DTT abolishes the activation at 5 mM
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
allosteric activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
the activities of recombinant maize and recombinant potato enzyme are comparable in the presence of 10 mM 3-phosphoglycerate, however in absence of 3-phosphoglycerate and phosphate the maize enzyme exhibits approximately 20fold more activity than does potato enzyme, in presence of both 3-phosphoglycerate and phosphate the maize enzyme is 47fold active than is the potato enzyme
3-phosphoglycerate
-
pH-dependent, endosperm
3-phosphoglycerate
-
strong
3-phosphoglycerate
-
10 mM, 16fold stimulation, enzyme from maize endosperm
3-phosphoglycerate
-
activation of mutant Mos(1-198) is reduced compared to the wild-type enzyme, overview
3-phosphoglycerate
in presence of 3-phosphoglycerate, enzyme follows a Theorell-Chance bi-bi mechanism with ATP binding first and ADP-Glc releasing last. 3-Phosphoglycerate increases the binding affinity for both substrates with little effect on velocity for the maize and chimeric maize/potato isoforms. Activation constant Ka is 0.06 for maize enzyme and 0.03 for the chimeric enzyme
ADP
-
no activation
ADP
-
activation, less effective than 3-phosphoglycerate
ADP
-
activation, less effective than 3-phosphoglycerate
ADP
-
activation, less effective than 3-phosphoglycerate
ADP
-
activation, less effective than 3-phosphoglycerate
ADP
-
activation, less effective than 3-phosphoglycerate
ADP
-
activation, less effective than 3-phosphoglycerate
alpha-glycerol phosphate
-
-
alpha-glycerol phosphate
-
activation, pyrophosphorolysis, not
AMP
-
no activation
AMP
-
activation, less effective than 3-phosphoglycerate
AMP
-
activation, less effective than 3-phosphoglycerate
AMP
-
activation, less effective than 3-phosphoglycerate
AMP
-
activation, less effective than 3-phosphoglycerate
AMP
-
activation, less effective than 3-phosphoglycerate
AMP
-
activation, less effective than 3-phosphoglycerate
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
mainly Escherichia coli and chimeric enzyme AE containing the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme, not chimeric enzyme EA containing the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme, C-terminus of Escherichia coli is relavant for the selectivity
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
slight activation
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
in presence of fructose 1,6-diphosphate pH-optimum decreased, effects on Km
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
one of the most effective activators
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
Escherichia aurescens
-
-
D-fructose 1,6-bisphosphate
Escherichia aurescens
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
most important in vivo
D-fructose 1,6-bisphosphate
-
mainly Escherichia coli and chimeric enzyme AE containing the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme, not chimeric enzyme EA containing the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme, C-terminus of Escherichia coli is relavant for the selectivity
D-fructose 1,6-bisphosphate
-
50% activation at 0.0364 mM for wild-type, at 0.0523 mM for mutant lacking N-terminal 3 amino acids, at 0.0887 mM for mutant lacking N-terminal 7 amino acids
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
one of the most effective activators
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
one of the most effective activators
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
physiological modulator
D-fructose 1,6-bisphosphate
-
in presence of fructose 1,6-diphosphate pH-optimum decreased, effects on Km
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
slight activation
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
one of the most effective activators
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
slight activation
D-fructose 1,6-bisphosphate
-
activation of pyrophosphorolysis
D-fructose 1,6-bisphosphate
-
activation of ADP-glucose synthesis
D-fructose 1,6-bisphosphate
Sorghum sp.
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
kinetics
D-fructose 1,6-bisphosphate
-
activation of pyrophosphorolysis
D-fructose 1,6-bisphosphate
-
activation of ADP-glucose synthesis
D-fructose 1,6-bisphosphate
activates GlgC by twofold, but has no effect on GlgC/GlgD complex. In the presence of D-fructose 1,6-bisphosphate GlgC becomes sensitive to inhibitors phosphoenolpyruvate and inorganic salts
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
less effective than 3-phosphoglycerate
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
slight activation
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
the most effective activator
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
activation of leaf enzyme, inhibition of endosperm enzyme
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
no activation
D-fructose 1,6-diphosphate
-
-
D-fructose 1,6-diphosphate
-
-
D-fructose 1,6-diphosphate
50% of maximal activation at 0.059 for wild-type
D-fructose 1,6-diphosphate
Rhodobacter gelatinosa
-
-
D-fructose 1,6-diphosphate
Rhodobacter globiformis
-
-
D-fructose 1,6-diphosphate
-
-
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
most effective allosteric activator of aeromonad enzyme
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
mainly Agrobacterium tumefaciens and chimeric enzyme AE containing the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme, not chimeric enzyme EA containing the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
slight activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
slight activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
no activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
Escherichia aurescens
-
activation
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
mainly Agrobacterium tumefaciens and chimeric enzyme AE containing the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme, not chimeric enzyme EA containing the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
no activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
Rhodobacter gelatinosa
-
-
D-fructose 6-phosphate
Rhodobacter globiformis
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
A0.5 value 2.2 mM, Hill coefficient 1.7
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
no activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
slight activation
D-fructose 6-phosphate
-
no activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation of pyrophosphorolysis
D-fructose 6-phosphate
Sorghum sp.
-
activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
activation of ADPglucose synthesis
D-fructose 6-phosphate
2 mM, 21fold activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
less effective than 3-phosphoglycerate
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
slight activation
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
activation of leaf enzyme, no influence on endosperm enzyme
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
allosteric activator
D-fructose 6-phosphate
-
less effective than 3-phosphoglycerate
D-fructose 6-phosphate
-
25 mM, 15fold stimulation, enzyme from maize endosperm
D-Glucose 1,6-bisphosphate
-
no activation
D-Glucose 1,6-bisphosphate
-
slight activation
D-Glucose 1,6-bisphosphate
-
slight activation
D-Glucose 1,6-bisphosphate
-
no activation
D-Glucose 1,6-bisphosphate
-
no activation
D-Glucose 1,6-bisphosphate
-
no activation
D-glucose 6-phosphate
-
no activation
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
slight activation
D-glucose 6-phosphate
-
no activation
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
no activation
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
no activation
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
A0.5 value 0.09 mM, Hill coefficient 2.2
D-glucose 6-phosphate
-
no activation
D-glucose 6-phosphate
-
no activation
D-glucose 6-phosphate
-
no activation
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
2 mM, 33fold activation
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
allosteric activator
D-glucose 6-phosphate
-
less effective than 3-phosphoglycerate
D-glucose 6-phosphate
-
25 mM, 12fold stimulation, enzyme from maize endosperm
D-mannose 6-phosphate
-
activation, less effective than D-fructose 6-phosphate
D-mannose 6-phosphate
A0.5 value 0.06 mM, Hill coefficient 2.9
D-mannose 6-phosphate
2 mM, 12fold activation
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
Escherichia aurescens
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
A0.5 value 4.0 mM, Hill coefficient 1.8
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
no activation
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
activation of pyrophosphorolysis
D-ribose 5-phosphate
-
activation of ADP-glucose synthesis
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
Sorghum sp.
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
slight activation
D-ribose 5-phosphate
-
activation of ADP-glucose synthesis
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
2 mM, 7fold activation
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
less effective than 3-phosphoglycerate
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
Escherichia aurescens
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
Sorghum sp.
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
no activation
dihydroxyacetone phosphate
-
activation, less effective than 3-phosphoglycerate
DTT
-
activation
DTT
-
only slight activation in the presence of 3-phosphoglycerate
fructose 1,6-bisphosphate
activation kinetics. 50% of the maximal velocity at 0.30 mM
fructose 1,6-bisphosphate
-
activation kinetics. Wild-type tetramer, 50% of the maximal velocity at 1.1 mM. Tetramer carrying mutation D148A in small subunit, 50% of the maximal velocity at 8.2 mM. Tetramer carrying mutation D171A in large subunit, 50% of the maximal velocity at 1.5 mM
fructose 1,6-bisphosphate
-
activation kinetics. 50% of the maximal velocity at 0.84 mM
fructose 6-phosphate
is an allosteric activator, binds to the interface between the N- and C-terminal domains, binding structure, modelling
fructose 6-phosphate
-
wild-type enzyme is activated, mutant enzyme R33A is insensitive to activation
fructose 6-phosphate
activation kinetics. 50% of the maximal velocity at 1.6 mM
fructose 6-phosphate
-
activation kinetics. Wild-type tetramer, 50% of the maximal velocity at 15 mM. Tetramer carrying mutation D148A in small subunit, 50% of the maximal velocity at 0.74 mM. Tetramer carrying mutation D171A in large subunit, 50% of the maximal velocity at 2.9 mM
fructose 6-phosphate
-
activation kinetics. 50% of the maximal velocity at 1.5 mM
fructose 6-phosphate
-
activation constant Ka is 9.8 for the oxidized and 20 for the reduced enzyme and 0.15 for the chimeric enzyme, respectively
fructose 6-phosphate
activation constant Ka is 0.53 for maize enzyme and 0.15 for the chimeric enzyme
glucose 6-phosphate
activation kinetics. 50% of the maximal velocity at 0.40 mM
glucose 6-phosphate
-
activation kinetics. Wild-type tetramer, 50% of the maximal velocity at 75 mM. Tetramer carrying mutation D148A in small subunit, 50% of the maximal velocity at 65 mM. Tetramer carrying mutation D171A in large subunit, 50% of the maximal velocity at 3.1 mM
glucose 6-phosphate
-
activation kinetics. 50% of the maximal velocity at 1.8 mM
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
slight activation
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
Escherichia aurescens
-
-
glyceraldehyde 3-phosphate
-
less effective than fructose bisphosphate
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
slight activation
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
no activation
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
Sorghum sp.
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
slight activation
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
no activation
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
Escherichia aurescens
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
Sorghum sp.
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
Hydroxypyruvate
-
slight activation, pyruvate analog
NADP+
-
less effective than fructose bisphosphate
NADP+
-
slight activation
NADPH
-
no activation
NADPH
-
activation, slight
NADPH
-
one of the most effective activators
NADPH
Escherichia aurescens
-
activation
NADPH
-
one of the most effective activators
NADPH
-
one of the most effective activators
NADPH
-
one of the most effective activators
phosphate
-
-
phosphate
-
enhances AGPase activity al low substrate concentations
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
slight activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
Escherichia aurescens
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
less effective than fructose bisphosphate
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
most effective for Enterobacter hafniae
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
A0.5 value 0.3 mM, Hill coefficient 1.2
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
kinetics
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation of pyrophosphorolysis
phosphoenolpyruvate
-
ADPglucose synthesis
phosphoenolpyruvate
Sorghum sp.
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation of pyrophosphorolysis
phosphoenolpyruvate
-
ADPglucose synthesis
phosphoenolpyruvate
2 mM, 14fold activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
slight activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
less effective than 3-phosphoglycerate
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
no activation
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
no activation
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
influence on Km and pH-optimum
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
one of the most effective activators, less effective for Enterobacter hafniae
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
Escherichia aurescens
-
activation
pyridoxal 5'-phosphate
Escherichia aurescens
-
allosteric activator
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
wild-type enzyme and mutant SG14
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
one of the most effective activators, less effective for Enterobacter hafniae
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
one of the most effective activators, less effective for Enterobacter hafniae
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
one of the most effective activators, less effective for Enterobacter hafniae
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
influence on Km and pH-optimum
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
slight activation
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
one of the most effective activators, less effective for Enterobacter hafniae
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
Sorghum sp.
-
activation
pyridoxal 5'-phosphate
Sorghum sp.
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
pyruvate
-
-
pyruvate
-
activation, kinetics
pyruvate
-
activation of chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme with higher affinity than activation of chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
pyruvate
-
activation, kinetics
pyruvate
-
activation, kinetics
pyruvate
-
activation, kinetics
pyruvate
-
activation of chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme with higher affinity than activation of chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
pyruvate
-
pyruvate is a weak activator by itself, and synergically enhances the fructose-1,6-bisphosphate activation
pyruvate
-
activation, kinetics
pyruvate
-
activation, kinetics
pyruvate
-
activation, kinetics
pyruvate
Rhodobacter gelatinosa
-
-
pyruvate
Rhodobacter globiformis
-
-
pyruvate
-
activation, kinetics
pyruvate
-
activation, kinetics
pyruvate
-
activation, kinetics
pyruvate
-
activation, kinetics
pyruvate
-
activation, kinetics
pyruvate
2 mM, 3fold activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
Escherichia aurescens
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
isosteric analog of fructose bisphosphate
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
Sorghum sp.
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
sedoheptulose 1,7-diphosphate
-
activation
additional information
-
-
-
additional information
-
-
-
additional information
-
no activation of Enterobacter hafniae or Aeromonas hydrophila enzyme by NADH, pyruvate, NAD+, NADP+, phosphate, erythrose 4-phosphate, malate, cAMP
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
Enterobacteriaceae with a nonspecific activator site
-
additional information
Escherichia aurescens
-
-
-
additional information
-
activator/inhibitor interaction in vivo and in vitro
-
additional information
-
effector binding studies, structural requirements for an activator
-
additional information
-
ADP-glucose diphosphorylase comprises two domains with a strong interaction between them. That interaction is important for allosteric properties and structural stability
-
additional information
-
no activation of Enterobacter hafniae or Aeromonas hydrophila enzyme by NADH, pyruvate, NAD+, NADP+, phosphate, erythrose 4-phosphate, malate, cAMP
-
additional information
-
-
-
additional information
-
Enterobacteriaceae with a nonspecific activator site
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
the Sh2r6hs transgene increases enzyme activity in developing endosperm by 2.7fold in presence of phosphate and this increased enzyme activity influences the plant phenotype: both seed weight per plant and total plant biomass
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
genus Serratia: no significant activation by glycolytic metabolites
-
additional information
-
-
-
additional information
-
not: oxaloacetate, L-malate
-
additional information
-
genus Serratia: no significant activation by glycolytic metabolites
-
additional information
-
not: 2-oxoglutarate
-
additional information
-
not: NADH, fumarate, succinate, acetyl-CoA, Glu, Ala, Asp, riboflavin 5'-phosphate
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
not: L-lactate, citrate
-
additional information
-
not: L-lactate, citrate
-
additional information
-
no activation of pyrophosphorolysis
-
additional information
-
not: oxaloacetate, L-malate
-
additional information
-
not: oxaloacetate, L-malate
-
additional information
-
not: 2-oxoglutarate
-
additional information
-
mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator
-
additional information
-
redox-activation
-
additional information
Sorghum sp.
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
peak of activities at the 28th day post anthesis, higher activity in the cultivar with a high starch content
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
not: fructose 2,6-bisphosphate, Ca2+/calmodulin
-
additional information
-
mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator
-
additional information
-
no activation by D-6-phosphogluconic acid, ribose 1,5-diphosphate, erythrose 4-phosphate, or methyl phosphate at 20 mM
-
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0.76
8-azaATP
-
pH 8.5, 37°C, influence of activators on Km
0.07 - 0.48
ADP-D-glucose
0.017 - 30
alpha-D-glucose 1-phosphate
0.041 - 0.083
alpha-D-glucose-1-phosphate
additional information
additional information
-
0.07
ADP-D-glucose
-
pH 7.4, 37°C, mutant MP-TI
0.11
ADP-D-glucose
-
pH 7.4, 37°C, mutant MP
0.33
ADP-D-glucose
-
pH 7.4, 37°C, mutant BT2-TI
0.48
ADP-D-glucose
-
pH 7.4, 37°C, wild-type BT2
0.24
ADP-glucose
-
-
0.24
ADP-glucose
-
pH 8.0, 37°C
0.45
ADP-glucose
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S
0.62
ADP-glucose
-
pH 7.4, 37°C
0.72
ADP-glucose
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L3 and small subunit S
1.57
ADP-glucose
pH 7.8, 37°C, large subunit isoform L3
2.1
ADP-glucose
pH 8.0, 37°C
0.017
alpha-D-glucose 1-phosphate
wild-type, pH 8.0, 37°C
0.017
alpha-D-glucose 1-phosphate
-
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.017
alpha-D-glucose 1-phosphate
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.018
alpha-D-glucose 1-phosphate
-
pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes
0.019
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL1 in presence of 0.1 mM 3-phosphoglycerate
0.021
alpha-D-glucose 1-phosphate
pH 8, 37°C, in absence of fructose 6-phosphate
0.023
alpha-D-glucose 1-phosphate
-
wild-type, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.026
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C
0.031
alpha-D-glucose 1-phosphate
-
pH 7.3, 37°C, in presence of 1 mM 3-phosphoglycerate
0.038
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C
0.038
alpha-D-glucose 1-phosphate
large subunit mutant Q96G/D161G/A443R, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.039
alpha-D-glucose 1-phosphate
wild-type, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.04
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, recombinant enzyme
0.04
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, mutant BT2-TI
0.04
alpha-D-glucose 1-phosphate
-
wild-type, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.04
alpha-D-glucose 1-phosphate
wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.044
alpha-D-glucose 1-phosphate
wild-type, pH 7.4, 37°C
0.05
alpha-D-glucose 1-phosphate
mutant W274F, pH 8.0, 37°C
0.05
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, wild-type BT2
0.05
alpha-D-glucose 1-phosphate
mutant BT2/E438Q
0.05
alpha-D-glucose 1-phosphate
mutant BT2/P372A
0.05
alpha-D-glucose 1-phosphate
-
reduced wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.052
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL3 in presence of 2 mM 3-phosphoglycerate
0.056
alpha-D-glucose 1-phosphate
pH 8, 37°C, in presence of fructose 6-phosphate
0.06
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL4 in presence of 1 mM 3-phosphoglycerate
0.06
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, enzyme from Zea mays endosperm
0.06
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, mutant MP-TI
0.06
alpha-D-glucose 1-phosphate
mutant BT2/A508S
0.06
alpha-D-glucose 1-phosphate
mutant BT2/M172T
0.06
alpha-D-glucose 1-phosphate
mutant BT2/T361C
0.06
alpha-D-glucose 1-phosphate
mutant BT2/V227R
0.06
alpha-D-glucose 1-phosphate
mutant BT2/V502T
0.06
alpha-D-glucose 1-phosphate
large subunit mutant D161G, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.07
alpha-D-glucose 1-phosphate
mutant BT2/C114A
0.07
alpha-D-glucose 1-phosphate
mutant BT2/D368S
0.07
alpha-D-glucose 1-phosphate
mutant BT2/H149S
0.07
alpha-D-glucose 1-phosphate
mutant BT2/Q213H
0.07
alpha-D-glucose 1-phosphate
wild type BT2/SH2
0.07
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 1.3, presence of mannose 6-phosphate, pH 8.0, 37°C
0.07
alpha-D-glucose 1-phosphate
S0.5 value, Hill coefficient 1.2, GlgC/GlgD complex, pH 8.0, 37°C
0.071
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, long day photoperiod
0.074
alpha-D-glucose 1-phosphate
large subunit mutant G101N, pH 7.5, 37°C
0.076
alpha-D-glucose 1-phosphate
pH 7.9, homotetramer APS1 in presence of 20 mM 3-phosphoglycerate
0.08
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, mutant MP
0.08
alpha-D-glucose 1-phosphate
mutant BT2/C382F
0.081
alpha-D-glucose 1-phosphate
large subunit mutant E38K/G101N, pH 7.5, 37°C
0.085
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL2 in presence of 4 mM 3-phosphoglycerate
0.086
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, fruit enzyme, in presence of 3-phosphoglycerate
0.09
alpha-D-glucose 1-phosphate
-
mutant P26L, 37°C
0.09
alpha-D-glucose 1-phosphate
mutant S212Y, pH 8.0, 37°C
0.09
alpha-D-glucose 1-phosphate
mutant BT2/C424V
0.09
alpha-D-glucose 1-phosphate
mutant BT2/S163F
0.09
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 1.1, presence of glucose 6-phosphate, pH 8.0, 37°C
0.1
alpha-D-glucose 1-phosphate
wild-type
0.1
alpha-D-glucose 1-phosphate
-
oxidized wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.105
alpha-D-glucose 1-phosphate
-
pH 7.3, 37°C, in absence of 3-phosphoglycerate
0.11
alpha-D-glucose 1-phosphate
-
pH 8.0, in presence of 2.5 mM 3-phosphoglycerate
0.11
alpha-D-glucose 1-phosphate
pH 8.0, 37°C, presence of Mg2+
0.12
alpha-D-glucose 1-phosphate
-
wild-type, 37°C
0.12
alpha-D-glucose 1-phosphate
mutant D157N
0.12
alpha-D-glucose 1-phosphate
-
mutant Q106A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.12
alpha-D-glucose 1-phosphate
-
mutant R107A, S0.5 value, Hill coefficient 1.0, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.122
alpha-D-glucose 1-phosphate
mutant F240M, pH 8.0, 37°C
0.13
alpha-D-glucose 1-phosphate
-
pH 7.0, 37°C, kinetic study
0.13
alpha-D-glucose 1-phosphate
-
pH 8.4, 37°C, influence of activators on Km
0.13
alpha-D-glucose 1-phosphate
-
wild-type, 37°C, pH 7.0
0.13
alpha-D-glucose 1-phosphate
pH 8.0, 37°C, presence of Co2+
0.13
alpha-D-glucose 1-phosphate
pH 8.0, 37°C, presence of Mn2+
0.13
alpha-D-glucose 1-phosphate
large subunit E370G/small subunit wild-type, pH 7.4, 37°C
0.14
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C
0.14
alpha-D-glucose 1-phosphate
-
mutant P55L, 37°C
0.14
alpha-D-glucose 1-phosphate
-
mutant P66L, 37°C
0.143
alpha-D-glucose 1-phosphate
-
mutant R115A, S0.5 value, Hill coefficient 1.7, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.15
alpha-D-glucose 1-phosphate
wild-type, pH 7.5, 37°C
0.15
alpha-D-glucose 1-phosphate
mutant D157E
0.15
alpha-D-glucose 1-phosphate
-
mutant P52L, 37°C
0.15
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, short day photoperiod
0.158
alpha-D-glucose 1-phosphate
heterodimer of small/large subunit, presence of ATPgammaS, pH 7.4, 25°C
0.16
alpha-D-glucose 1-phosphate
mutant G267S
0.16
alpha-D-glucose 1-phosphate
-
mutant P17L, 37°C
0.16
alpha-D-glucose 1-phosphate
mutant Q127M
0.16
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 0.7, presence of fructose 6-phosphate, pH 8.0, 37°C
0.169
alpha-D-glucose 1-phosphate
mutant D239E, pH 8.0, 37°C
0.17
alpha-D-glucose 1-phosphate
-
pH 7.5, 30°C, kinetic study
0.17
alpha-D-glucose 1-phosphate
-
pH 8.0, in presence of 5 mM 3-phosphoglycerate
0.17
alpha-D-glucose 1-phosphate
mutation K41R/T51K, large subunit, plus D143N, small subunit
0.17
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 0.8, presence of phosphoenolpyruvate, pH 8.0, 37°C
0.17
alpha-D-glucose 1-phosphate
large subunit mutant E38K, pH 7.5, 37°C
0.17
alpha-D-glucose 1-phosphate
-
mutant P103A, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.18
alpha-D-glucose 1-phosphate
-
pH 7.0, 37°C, kinetic study
0.19
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C
0.194
alpha-D-glucose 1-phosphate
heterodimer of small/large subunit, pH 7.4, 25°C
0.2
alpha-D-glucose 1-phosphate
-
pH 7.0, 37°C, strain AC70R1, kinetic study
0.204
alpha-D-glucose 1-phosphate
mutant F240A, pH 8.0, 37°C
0.21
alpha-D-glucose 1-phosphate
-
pH 8.4, 37°C, influence of activators on Km
0.21
alpha-D-glucose 1-phosphate
-
wild-type, pH 8.0, 37°C
0.21
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation P112L, small subunit, 37°C, pH 7.0
0.22
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, leaf enzyme, in presence of 3-phosphoglycerate
0.22
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, kinetic study
0.22
alpha-D-glucose 1-phosphate
mutant D157L
0.22
alpha-D-glucose 1-phosphate
mutant K41R/T51K
0.22
alpha-D-glucose 1-phosphate
-
mutant P103A, S0.5 value, Hill coefficient 1.1, pH 8.0, 37°C
0.23
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.0, presence of 25 mM pyruvate and 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.24
alpha-D-glucose 1-phosphate
mutant K41R
0.24
alpha-D-glucose 1-phosphate
mutant S212A, pH 8.0, 37°C
0.25
alpha-D-glucose 1-phosphate
-
pH 7.0, 37°C, strain B, kinetic study
0.25
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, mutant TG-15, kinetic study
0.25
alpha-D-glucose 1-phosphate
mutant G37A
0.25
alpha-D-glucose 1-phosphate
-
mutant Q106A, S0.5 value, Hill coefficient 1.6, pH 8.0, 37°C
0.26
alpha-D-glucose 1-phosphate
-
mutant R107A, S0.5 value, Hill coefficient 0.9, pH 8.0, 37°C
0.264
alpha-D-glucose 1-phosphate
mutant D239N, pH 8.0, 37°C
0.27
alpha-D-glucose 1-phosphate
-
mutant Y114A, S0.5 value, Hill coefficient 0.2, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.28
alpha-D-glucose 1-phosphate
-
mutant R115A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C
0.29
alpha-D-glucose 1-phosphate
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S
0.32
alpha-D-glucose 1-phosphate
mutant T51K
0.33
alpha-D-glucose 1-phosphate
-
pH 8.0, in absence of 3-phosphoglycerate
0.33
alpha-D-glucose 1-phosphate
-
mutant W113A, pH 8.0, 37°C
0.34
alpha-D-glucose 1-phosphate
-
mutant W113A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.36
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation L46F, small subunit, 37°C, pH 7.0
0.367
alpha-D-glucose 1-phosphate
mutant W274A, pH 8.0, 37°C
0.37
alpha-D-glucose 1-phosphate
pH 8.0, 37°C
0.37
alpha-D-glucose 1-phosphate
-
wild-type, S0.5 value, Hill coefficient 1.5, pH 8.0, 37°C
0.38
alpha-D-glucose 1-phosphate
mutation K41R, large subunit, plus D143N, small subunit
0.39
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.39
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.39
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation P308L, small subunit, 37°C, pH 7.0
0.4
alpha-D-glucose 1-phosphate
mutant G36A
0.4
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 0.6, presence of ribose 5-phosphate, pH 8.0, 37°C
0.41
alpha-D-glucose 1-phosphate
mutant D276E, pH 8.0, 37°C
0.41
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation R350K, small subunit, 37°C, pH 7.0
0.41
alpha-D-glucose 1-phosphate
-
mutant Q74A, pH 8.0, 37°C
0.41
alpha-D-glucose 1-phosphate
-
mutant W113A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.41
alpha-D-glucose 1-phosphate
-
S0.5 value, wild-type, 37°C, pH 7.0
0.42
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, 37°C, pH 7.0
0.43
alpha-D-glucose 1-phosphate
-
mutant Y114A, S0.5 value, Hill coefficient 0.3, pH 8.0, 37°C
0.44
alpha-D-glucose 1-phosphate
mutant G128A
0.45
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, wild-type enzyme
0.46
alpha-D-glucose 1-phosphate
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L3 and small subunit S
0.46
alpha-D-glucose 1-phosphate
-
mutant W113A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C
0.47
alpha-D-glucose 1-phosphate
mutant G267L
0.47
alpha-D-glucose 1-phosphate
-
mutant Q74A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.524
alpha-D-glucose 1-phosphate
mutant D239A, pH 8.0, 37°C
0.525
alpha-D-glucose 1-phosphate
mutant W274L, pH 8.0, 37°C
0.54
alpha-D-glucose 1-phosphate
mutant T129V
0.55
alpha-D-glucose 1-phosphate
-
pH 7.5, 5°C, kinetic study
0.57
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.0, presence of 25 mM pyruvate, pH 8.0, 37°C
0.6
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, wild-type enzyme
0.63
alpha-D-glucose 1-phosphate
mutant A132N
0.64
alpha-D-glucose 1-phosphate
mutant A132D
0.71
alpha-D-glucose 1-phosphate
mutant G128L
0.72
alpha-D-glucose 1-phosphate
pH 8.0, 37°C, presence of Cd2+
0.72
alpha-D-glucose 1-phosphate
-
S0.5 value, large subunit mutant A171V with wild-type small subunit, 37°C, pH 7.0
0.77
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.0, presence of 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.785
alpha-D-glucose 1-phosphate
mutant Y216F, pH 8.0, 37°C
0.8
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C
0.81
alpha-D-glucose 1-phosphate
mutant A132V
0.83
alpha-D-glucose 1-phosphate
-
mutant P44L, 37°C
0.88
alpha-D-glucose 1-phosphate
mutant T129V/A132V
0.92
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.92
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.95
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.1, pH 8.0, 37°C
0.97
alpha-D-glucose 1-phosphate
mutant A132F
1.01
alpha-D-glucose 1-phosphate
mutation T51K, large subunit, plus D143N, small subunit
1.07
alpha-D-glucose 1-phosphate
-
reduced wild-type, pH 7.4, 37°C
1.32
alpha-D-glucose 1-phosphate
-
S0.5 value, wild-type small subunit alone, 37°C, pH 7.0
1.43
alpha-D-glucose 1-phosphate
-
S0.5 value, large subunit mutant T139I with wild-type small subunit, 37°C, pH 7.0
1.44
alpha-D-glucose 1-phosphate
mutant E194Q, pH 8.0, 37°C
1.45
alpha-D-glucose 1-phosphate
mutant D276N, pH 8.0, 37°C
1.63
alpha-D-glucose 1-phosphate
-
oxidzed wild-type, pH 7.4, 37°C
1.7
alpha-D-glucose 1-phosphate
mutant D276A, pH 8.0, 37°C
1.8
alpha-D-glucose 1-phosphate
hyperbolic behavior, Hill coefficient 0.9, pH 8.0, 37°C
1.81
alpha-D-glucose 1-phosphate
wild-type, pH 7.4, 37°C, presence of phosphate
2.04
alpha-D-glucose 1-phosphate
S0.5 value, Hill coefficient 1.7, subunit GlgC in presence of fructose 1,6-bisphosphate, pH 8.0, 37°C
2.1
alpha-D-glucose 1-phosphate
pH 7.8, 37°C, large subunit isoform L3
2.8
alpha-D-glucose 1-phosphate
wild-type, 37°C, pH 7.4
2.8
alpha-D-glucose 1-phosphate
wild-type, pH 7.4, 37°C
2.81
alpha-D-glucose 1-phosphate
mutant E194A, pH 8.0, 37°C
3.44
alpha-D-glucose 1-phosphate
S0.5 value, Hill coefficient 0.9, subunit GlgC, pH 8.0, 37°C
4.01
alpha-D-glucose 1-phosphate
-
oxidized wild-type, pH 7.4, 37°C, presence of phosphate
4.2
alpha-D-glucose 1-phosphate
-
pH 7.6, 75°C
4.66
alpha-D-glucose 1-phosphate
mutant S212T, pH 8.0, 37°C
5.18
alpha-D-glucose 1-phosphate
-
reduced wild-type, pH 7.4, 37°C, presence of phosphate
6.42
alpha-D-glucose 1-phosphate
mutant S212V, pH 8.0, 37°C
6.59
alpha-D-glucose 1-phosphate
mutant E194D, pH 8.0, 37°C
6.79
alpha-D-glucose 1-phosphate
-
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
6.79
alpha-D-glucose 1-phosphate
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
6.8
alpha-D-glucose 1-phosphate
large subunit mutant D161G, 37°C, pH 7.4
8.74
alpha-D-glucose 1-phosphate
large subunit mutant Q96G/D161G/A443R, 37°C, pH 7.4
11.9
alpha-D-glucose 1-phosphate
-
chimeric enzyme, pH 7.4, 37°C
11.9
alpha-D-glucose 1-phosphate
chimeric enzyme, pH 7.4, 37°C
16.7
alpha-D-glucose 1-phosphate
mutant K195Q, pH 8.0, 37°C
30
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C
0.041
alpha-D-glucose-1-phosphate
-
mutant A33K, pH 7.5
0.055
alpha-D-glucose-1-phosphate
-
mutant G96N, pH 7.5
0.063
alpha-D-glucose-1-phosphate
-
mutant A33K/G96N, pH 7.5
0.083
alpha-D-glucose-1-phosphate
-
wild-type, pH 7.5
0.018
ATP
-
pH 7.4, 37°C, mutant Mos(1-198), in absence of 3-phosphoglycerate
0.018
ATP
-
pH 7.4, 37°C, mutant Mos(1-198), in absence of 3-phosphoglycerate
0.039
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate
0.039
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate
0.04
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-429), in absence of 3-phosphoglycerate
0.04
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-429), in absence of 3-phosphoglycerate
0.04
ATP
-
pH 7.4, 37°C, mutant Mos(1-376), in absence of 3-phosphoglycerate
0.04
ATP
-
pH 7.4, 37°C, mutant Mos(1-376), in absence of 3-phosphoglycerate
0.043
ATP
large subunit mutant D161G, 37°C, pH 7.4
0.044
ATP
-
pH 7.4, 37°C, mutant Mos(1-277), in absence of 3-phosphoglycerate
0.044
ATP
-
pH 7.4, 37°C, mutant Mos(1-277), in absence of 3-phosphoglycerate
0.044
ATP
large subunit mutant D161G, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.045
ATP
-
pH 7.3, 37°C, in presence of 1 mM 3-phosphoglycerate
0.05
ATP
-
pH 7.4, 37°C, leaf enzyme, in presence of 3-phosphoglycerate
0.05
ATP
wild-type, pH 7.4, 37°C
0.051
ATP
-
pH 7.4, 37°C, mutant Mos(1-198), in presence of 3-phosphoglycerate
0.051
ATP
-
pH 7.4, 37°C, mutant Mos(1-198), in presence of 3-phosphoglycerate
0.052
ATP
-
mutant G96N, pH 7.5
0.053
ATP
-
chimeric enzyme, pH 7.4, 37°C, presence of 3-0.040 phosphoglycerate
0.053
ATP
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.055
ATP
-
mutant A33K/G96N, pH 7.5
0.056
ATP
-
mutant A33K, pH 7.5
0.056
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate
0.056
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate
0.057
ATP
large subunit mutant Q96G/D161G/A443R, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.067
ATP
pH 7.9, APS1/APL1 in presence of 0.1 mM 3-phosphoglycerate
0.069
ATP
wild-type, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.073
ATP
-
wild-type, pH 7.5
0.074
ATP
-
pH 7.4, 37°C, wild-type enzyme, in presence of 3-phosphoglycerate
0.074
ATP
-
pH 7.4, 37°C, wild-type enzyme, in presence of 3-phosphoglycerate
0.075
ATP
-
pH 7.4, 37°C, wild-type enzyme, in absence of 3-phosphoglycerate
0.075
ATP
-
pH 7.4, 37°C, wild-type enzyme, in absence of 3-phosphoglycerate
0.079
ATP
pH 8, 37°C, in presence of fructose 6-phosphate
0.08
ATP
-
pH 8.0, in presence of 2.5 mM 3-phosphoglycerate
0.086
ATP
-
pH 8.0, 37°C, wild-type enzyme
0.09
ATP
mutant BT2/A508S
0.09
ATP
mutant BT2/M172T
0.09
ATP
large subunit E370G/small subunit wild-type, pH 7.4, 37°C
0.094
ATP
pH 7.9, APS1/APL3 in presence of 2 mM 3-phosphoglycerate
0.1
ATP
large subunit mutant Q96G/D161G/A443R, 37°C, pH 7.4
0.11
ATP
-
pH 7.5, 5°C, kinetic study
0.11
ATP
-
pH 7.4, 37°C, wild-type BT2 and mutant MP-TI
0.11
ATP
mutant BT2/D368S
0.11
ATP
large subunit mutant E38K/G101N, pH 7.5, 37°C
0.11
ATP
wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.118
ATP
pH 7.9, APS1/APL4 in presence of 1 mM 3-phosphoglycerate
0.12
ATP
-
pH 7.4, 37°C, fruit enzyme, in presence of 3-phosphoglycerate
0.12
ATP
-
pH 7.4, 37°C, enzyme from Zea mays endosperm
0.12
ATP
wild type BT2/SH2
0.13
ATP
-
pH 7.4, 37°C, mutant MP
0.13
ATP
mutant BT2/E438Q
0.13
ATP
mutant BT2/T361C
0.13
ATP
-
small subunit mutant R107A
0.13
ATP
-
oxidized wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.14
ATP
wild-type, pH 7.5, 37°C
0.14
ATP
mutant BT2/C114A
0.14
ATP
mutant BT2/C424V
0.14
ATP
mutant BT2/V227R
0.15
ATP
-
pH 7.4, 37°C, mutant BT2-TI
0.15
ATP
mutant BT2/C382F
0.15
ATP
mutant BT2/V502T
0.15
ATP
hyperbolic behavior, Hill coefficient 1.3, presence of mannose 6-phosphate, pH 8.0, 37°C
0.155
ATP
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.155
ATP
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.16
ATP
mutant D239A, pH 8.0, 37°C
0.16
ATP
large subunit mutant E38K, pH 7.5, 37°C
0.162
ATP
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.162
ATP
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.17
ATP
-
wild-type, 37°C, pH 7.0
0.17
ATP
mutant E194Q, pH 8.0, 37°C
0.17
ATP
heterodimer of small/large subunit, pH 7.4, 25°C
0.17
ATP
large subunit mutant G101N, pH 7.5, 37°C
0.17
ATP
-
oxidized wild-type, pH 7.4, 37°C
0.17
ATP
-
oxidized wild-type, pH 7.4, 37°C, presence of phosphate
0.17
ATP
-
wild-type, S0.5 value, Hill coefficient 2.0, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.18
ATP
-
pH 8.0, in presence of 5 mM 3-phosphoglycerate
0.18
ATP
-
pH 7.4, 37°C, long day photoperiod
0.19
ATP
-
wild-type, 37°C
0.19
ATP
mutant K195Q, pH 8.0, 37°C
0.19
ATP
-
large subunit mutant R116A
0.19
ATP
mutant BT2/H149S
0.19
ATP
mutant BT2/P372A
0.19
ATP
-
reduced wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.2
ATP
-
mutant P66L, 37°C
0.2
ATP
small subunit, pH 7.4, 25°C
0.21
ATP
-
mutant P17L, 37°C
0.21
ATP
mutant BT2/Q213H
0.22
ATP
pH 8, 37°C, enzyme modified for 30 min with 5 mM 2,3-butanedione
0.22
ATP
-
mutation P52L, large subunit, plus mutation P112L, small subunit, 37°C, pH 7.0
0.24
ATP
-
mutation P52L, large subunit, plus mutation L46F, small subunit, 37°C, pH 7.0
0.24
ATP
-
mutation P52L, large subunit, plus mutation P308L, small subunit, 37°C, pH 7.0
0.24
ATP
hyperbolic behavior, Hill coefficient 1.6, presence of glucose 6-phosphate, pH 8.0, 37°C
0.25
ATP
-
mutation P52L, large subunit, 37°C, pH 7.0
0.26
ATP
-
pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes
0.26
ATP
-
large subunit mutant R381A
0.27
ATP
mutant K41R/T51K
0.27
ATP
-
mutant P52L, 37°C
0.28
ATP
mutant W274F, pH 8.0, 37°C
0.29
ATP
-
mutation P52L, large subunit, plus mutation R350K, small subunit, 37°C, pH 7.0
0.29
ATP
-
reduced wild-type, pH 7.4, 37°C, presence of phosphate
0.3
ATP
-
pH 8.0, 37°C, wild-type enzyme
0.3
ATP
-
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
0.3
ATP
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
0.31
ATP
mutant D143N, small subunit
0.31
ATP
-
pH 7.4, 37°C, short day photoperiod
0.31
ATP
-
reduced wild-type, pH 7.4, 37°C
0.32
ATP
-
pH 7.3, 37°C, in absence of 3-phosphoglycerate
0.32
ATP
-
wild-type, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.33
ATP
-
mutant P55L, 37°C
0.34
ATP
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S
0.35
ATP
mutant Y216F, pH 8.0, 37°C
0.35
ATP
mutation K41R/T51K, large subunit, plus D143N, small subunit
0.36
ATP
-
small subunit mutant R340A
0.37
ATP
S0.5 value, Hill coefficient 1.5, subunit GlgC in presence of fructose 1,6-bisphosphate, pH 8.0, 37°C
0.38
ATP
mutant S212V, pH 8.0, 37°C
0.4
ATP
pH 8, 37°C, in absence of fructose 6-phosphate
0.4
ATP
mutation K41R, large subunit, plus D143N, small subunit
0.4
ATP
hyperbolic behavior, Hill coefficient 1.4, presence of phosphoenolpyruvate, pH 8.0, 37°C
0.41
ATP
mutant S212T, pH 8.0, 37°C
0.42
ATP
pH 7.9, homotetramer APS1 in presence of 20 mM 3-phosphoglycerate
0.42
ATP
-
large subunit mutant R146A
0.42
ATP
mutant BT2/S163F
0.43
ATP
mutant S212Y, pH 8.0, 37°C
0.43
ATP
mutant T129V/A132V
0.43
ATP
mutation T51K, large subunit, plus D143N, small subunit
0.48
ATP
-
pH 8.0, 37°C, kinetic study
0.48
ATP
mutant W274L, pH 8.0, 37°C
0.49
ATP
mutant E194D, pH 8.0, 37°C
0.49
ATP
-
S0.5 value, large subunit mutant T139I with wild-type small subunit, 37°C, pH 7.0
0.5
ATP
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L3 and small subunit S
0.5
ATP
hyperbolic behavior, Hill coefficient 1.1, presence of fructose 6-phosphate, pH 8.0, 37°C
0.5
ATP
hyperbolic behavior, Hill coefficient 1.3, presence of ribose 5-phosphate, pH 8.0, 37°C
0.5
ATP
-
S0.5 value, wild-type small subunit alone, 37°C, pH 7.0
0.51
ATP
-
S0.5 value, large subunit mutant A171V with wild-type small subunit, 37°C, pH 7.0
0.56
ATP
mutant D239N, pH 8.0, 37°C
0.57
ATP
pH 7.9, APS1/APL2 in presence of 4 mM 3-phosphoglycerate
0.58
ATP
-
S0.5 value, wild-type, 37°C, pH 7.0
0.58
ATP
wild-type, pH 7.4, 37°C, presence of phosphate
0.59
ATP
wild-type, pH 8.0, 37°C
0.61
ATP
-
pH 7.5, 30°C, kinetic study
0.68
ATP
-
mutant P44L, 37°C
0.68
ATP
mutant S212A, pH 8.0, 37°C
0.72
ATP
-
pH 8.4, 37°C, influence of activators on Km
0.81
ATP
-
mutant P103A, S0.5 value, Hill coefficient 1.5, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.89
ATP
-
mutant P103A, S0.5 value, Hill coefficient 1.9, pH 8.0, 37°C
0.9
ATP
-
pH 8.0, in absence of 3-phosphoglycerate
0.9
ATP
-
chimeric enzyme, pH 7.4, 37°C
0.9
ATP
chimeric enzyme, pH 7.4, 37°C
0.96
ATP
mutant D239E, pH 8.0, 37°C
0.99
ATP
-
S0.5 value, Hill coefficient 3.6, presence of 25 mM pyruvate and 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.04
ATP
mutant W274A, pH 8.0, 37°C
1.1
ATP
-
small subunit mutant R77K
1.14
ATP
mutant F240A, pH 8.0, 37°C
1.18
ATP
S0.5 value, Hill coefficient 3.7, GlgC/GlgD complex, pH 8.0, 37°C
1.2
ATP
-
pH 7.0, 37°C, strain AC70R1, kinetic study
1.2
ATP
pH 7.5, 37°C, mutant TG-15, kinetic study
1.2
ATP
mutant E194A, pH 8.0, 37°C
1.2
ATP
hyperbolic behavior, Hill coefficient 1.2, pH 8.0, 37°C
1.3
ATP
-
pH 7.0, 37°C, strain B, kinetic study
1.3
ATP
-
mutant R115A, S0.5 value, Hill coefficient 1.7, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.4
ATP
-
large subunit mutant R104A
1.55
ATP
-
pH 7.0, 37°C, kinetic study
1.63
ATP
-
mutant R107A, S0.5 value, Hill coefficient 2.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.67
ATP
-
S0.5 value, Hill coefficient 2.5, presence of 25 mM pyruvate, pH 8.0, 37°C
1.98
ATP
mutant F240M, pH 8.0, 37°C
2
ATP
-
pH 8.0, 37°C, strain JP102, kinetic study
2.03
ATP
mutant D276A, pH 8.0, 37°C
2.2
ATP
-
pH 7.0, 37°C, wild-type enzyme in the absence of fructose 1,6-bisphosphate, comparison of Km of wild-type and mutant enzymes in the presence and absence of fructose 1,6-bisphosphate
2.3
ATP
mutant D276N, pH 8.0, 37°C
2.3
ATP
-
mutant Y114A, S0.5 value, Hill coefficient 1.9, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
2.4
ATP
-
pH 8.4, 37°C, influence of activators on Km
2.4
ATP
-
pH 8.0, 37°C, strain LT-2, kinetic study
2.5
ATP
-
mutant W113A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
2.5
ATP
-
mutant Q106A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C
2.5
ATP
-
mutant R107A, S0.5 value, Hill coefficient 2.1, pH 8.0, 37°C
2.5
ATP
-
mutant Y114A, S0.5 value, Hill coefficient 2.0, pH 8.0, 37°C
2.5
ATP
-
wild-type, S0.5 value, Hill coefficient 2.4, pH 8.0, 37°C
3
ATP
-
mutant R115A, S0.5 value, Hill coefficient 2.1, pH 8.0, 37°C
3.1
ATP
-
mutant W113A, S0.5 value, Hill coefficient 1.1, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
3.2
ATP
-
pH 7.0, 37°C, kinetic study
3.42
ATP
S0.5 value, Hill coefficient 1.2, subunit GlgC, pH 8.0, 37°C
3.5
ATP
-
mutant W113A, S0.5 value, Hill coefficient 1.2, pH 8.0, 37°C
3.6
ATP
pH 7.8, 37°C, large subunit isoform L3
4
ATP
wild-type, 37°C, pH 7.4
4
ATP
wild-type, pH 7.4, 37°C
4.4
ATP
-
mutant Q106A, S0.5 value, Hill coefficient 1.2, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
4.77
ATP
mutant D276E, pH 8.0, 37°C
5
ATP
-
S0.5 value, Hill coefficient 2.1, presence of 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
5.8
ATP
-
mutant W113A, pH 8.0, 37°C
6.49
ATP
-
S0.5 value, Hill coefficient 1.5, pH 8.0, 37°C
7.6
ATP
-
mutant Q74A, pH 8.0, 37°C
9.8
ATP
-
mutant Q74A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
11
ATP
-
wild-type, pH 8.0, 37°C
0.033
diphosphate
-
pH 7.4, 37°C
0.08
diphosphate
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S
0.12
diphosphate
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L3 and small subunit S
0.35
diphosphate
pH 8.0, 37°C
0.41
diphosphate
pH 7.8, 37°C, large subunit isoform L3
2.32
diphosphate
-
pH 7.4, 37°C, wild-type BT2
4.07
diphosphate
-
pH 7.4, 37°C, mutant BT2-TI
5.87
diphosphate
-
pH 7.4, 37°C, mutant MP-TI
6.61
diphosphate
-
pH 7.4, 37°C, mutant MP
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic parameters
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
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kinetic study
-
additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
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kinetic study
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additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
-
additional information
additional information
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kinetic study
-
additional information
additional information
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kinetic study
-
additional information
additional information
Sorghum sp.
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
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kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
Escherichia aurescens
-
kinetic study
-
additional information
additional information
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kinetic study
-
additional information
additional information
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kinetic study
-
additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
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additional information
additional information
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kinetic study
-
additional information
additional information
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kinetic study
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
Sorghum sp.
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
Escherichia aurescens
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
comparison of Km of proteolyzed and non-proteolyzed enzyme at pH 7.4 and pH 6.8
-
additional information
additional information
-
comparison of Km of alpha-D-glucose 1-phosphate at different ATP concentrations, at two levels of 3-phosphoglycerate and in aqueous or by polyethylenglycol crowded medium, comparison of Km of ATP at different alpha-D-glucose 1-phosphate concentrations, at two levels of 3-phosphoglycerate and in aqueous or by polyethylenglycol crowded medium
-
additional information
additional information
-
the allosteric properties of Enterobacter hafniae are distinctly different from other bacteria of the genus Enterobacter
-
additional information
additional information
-
the allosteric properties of Enterobacter hafniae are distinctly different from other bacteria of the genus Enterobacter
-
additional information
additional information
-
KM-values for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
-
additional information
additional information
-
KM-values for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
-
additional information
additional information
-
kinetics of wild-type and mutant large subunits, overview
-
additional information
additional information
-
kinetics wild-type and mutant enzymes, photoaffinity labeling of the AGPase heterotetramers, overview
-
additional information
additional information
-
ordered kinetic mechanism, regulation of AGPase by effectors, detailed overview
-
additional information
additional information
-
recombinant wild-type and mutant AGPase kinetic and allosteric properties for the forward and reverse reaction directions, overview
-
additional information
additional information
wild-type and ADPGlc PPase H379R and ADPGlc PPase H379K mutant kinetics, overview
-
additional information
additional information
-
wild-type and ADPGlc PPase H379R and ADPGlc PPase H379K mutant kinetics, overview
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
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0.25
8-N3ADPglucose
-
pH 8.5, 37°C
1.25
8-N3ATP
-
pH 8.5, 37°C
0.007 - 1.2
ADP-alpha-D-glucose
0.00038 - 0.9
diphosphate
0.047 - 0.12
phosphoenolpyruvate
additional information
additional information
-
0.104
ADP
-
pH 8.0, 37°C, in absence of phosphoenolpyruvate
0.235
ADP
-
pH 8.0, 37°C, strain ATCC 15365
0.41
ADP
-
influence of activators
0.42
ADP
-
pH 8.0, 37°C, strains JP102 and LT-2, in presence of 0.25 mM fructose 1,6-bisphosphate
1
ADP
-
pH 8.0, 37°C, strains JP102, in presence of 1 mM fructose 1,6-bisphosphate
1.1
ADP
-
pH 8.0, 37°C, strains LT-2, in presence of 1 mM fructose 1,6-bisphosphate
1.2
ADP
-
pH 7.5, 37°C, in absence of 3-phosphoglycerate
1.7
ADP
-
pH 8.0, 37°C, in presence of fructose 1,6-bisphosphate
2
ADP
-
pH 7.5, 37°C, in presence of 3-phosphoglycerate
2
ADP
-
pH 8.0, 37°C, in presence of fructose 6-phosphate
3.8
ADP
-
in absence of fructose 6-phosphate
3.8
ADP
-
in absence of fructose 6-phosphate
5
ADP
-
in presence of 0.5 mM fructose 6-phosphate
5
ADP
-
in presence of 0.5 mM fructose 6-phosphate
0.007
ADP-alpha-D-glucose
wild-type, substrate ATP, pH 7.4, 37°C
0.01
ADP-alpha-D-glucose
chimeric mutant, substrate ATP, pH 7.4, 37°C
0.045
ADP-alpha-D-glucose
-
oxidized wild-type, substrate ATP, pH 7.4, 37°C
0.05
ADP-alpha-D-glucose
-
chimeric mutant, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.05
ADP-alpha-D-glucose
chimeric mutant, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.083
ADP-alpha-D-glucose
-
chimeric mutant, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.083
ADP-alpha-D-glucose
chimeric mutant, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.09
ADP-alpha-D-glucose
-
chimeric mutant, substrate glucose 1-phosphate, pH 7.4, 37°C
0.09
ADP-alpha-D-glucose
chimeric mutant, substrate glucose 1-phosphate, pH 7.4, 37°C
0.09
ADP-alpha-D-glucose
wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.11
ADP-alpha-D-glucose
-
oxidized wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.11
ADP-alpha-D-glucose
-
oxidized wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.12
ADP-alpha-D-glucose
wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.13
ADP-alpha-D-glucose
-
oxidized wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.14
ADP-alpha-D-glucose
-
reduced wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.19
ADP-alpha-D-glucose
-
chimeric mutant, substrate ATP, pH 7.4, 37°C
0.21
ADP-alpha-D-glucose
-
reduced wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.46
ADP-alpha-D-glucose
-
reduced wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
1.2
ADP-alpha-D-glucose
wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.007
AMP
-
pH 8.0, 37°C, wild-type enzyme in presence of 0.1 mM fructose-1,6-bisphosphate
0.012
AMP
-
pH 8.0, 37°C, in absence of phosphoenolpyruvate
0.015
AMP
-
pH 8.0, 37°C, strain ATCC 15365
0.023
AMP
-
pH 8.0, 37°C, in presence of phosphoenolpyruvate
0.028
AMP
-
pH 8.0, 37°C, strain LT-2, in presence of 0.25 mM fructose 1,6-bisphosphate
0.031
AMP
-
pH 8.0, 37°C, strain ATCC 274
0.032
AMP
-
pH 8.0, 37°C, strain JP102, in presence of 0.25 mM fructose 1,6-bisphosphate
0.04
AMP
-
pH 7.6, 37°C, wild-type enzyme
0.06
AMP
-
pH 7.6, 37°C, mutant enzyme D142E
0.062
AMP
-
in absence of pyruvate
0.094
AMP
-
pH 7.0, 37°C, wild-type enzyme, in the presence of a saturating concentration of fructose 1,6-bisphosphate
0.096
AMP
-
pH 8.0, 37°C, strain JP102, in presence of 1 mM fructose 1,6-bisphosphate
0.11
AMP
-
pH 8.0, 37°C, strain LT-2, in presence of 1 mM fructose 1,6-bisphosphate
0.13
AMP
-
pH 7.6, 37°C, mutant enzyme D142A
0.204
AMP
-
pH 8.0, 37°C, in presence of phosphoenolpyruvate
0.26
AMP
-
in presence of 0.05 mM pyruvate
0.3
AMP
-
pH 7.0, 37°C, mutant enzyme P295G, in the presence of a saturating concentration of fructose 1,6-bisphosphate,
0.34
AMP
-
pH 7.0, 37°C, mutant enzyme P295N, in the presence of a saturating concentration of fructose 1,6-bisphosphate
0.38
AMP
-
pH 7.0, 37°C, mutant enzyme P295Q, in the presence of a saturating concentration of fructose 1,6-bisphosphate
0.64
AMP
-
influence of activators
0.95
AMP
-
pH 7.0, 37°C, mutant enzyme G336D, in the presence of a saturating concentration of fructose 1,6-bisphosphate
0.96
AMP
-
pH 7.0, 37°C, mutant enzyme P295E, in the presence of a saturating concentration of fructose 1,6-bisphosphate
1
AMP
-
pH 7.6, 37°C, mutant enzyme D142N
2
AMP
-
pH 7.0, 37°C, mutant enzyme P295D, in the presence of a saturating concentration of fructose 1,6-bisphosphate
2.5
AMP
-
in presence of 1 mM pyruvate
3
AMP
-
pH 8.0, 37°C, wild-type enzyme in presence of 0.3 mM fructose-1,6-bisphosphate
4.95
AMP
-
pH 7.0, 37°C, double mutant enzyme P295D/G336D
9
AMP
-
pH 8.0, 37°C, the chimeric enzymes, AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme is slightly activated by AMP in the range of 0.1-2 mM
9
AMP
-
pH 8.0, 37°C, the chimeric enzymes, AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme is slightly activated by AMP in the range of 0.1-2 mM
0.00038
diphosphate
-
pH 7.4, 37°C
0.025
diphosphate
-
reduced wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.03
diphosphate
chimeric mutant, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.047
diphosphate
-
oxidized wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.047
diphosphate
-
oxidized wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.047
diphosphate
-
reduced wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.075
diphosphate
chimeric mutant, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.1
diphosphate
wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.11
diphosphate
wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.19
diphosphate
-
oxidized wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.19
diphosphate
wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.35
diphosphate
-
chimeric mutant, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.35
diphosphate
-
reduced wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.36
diphosphate
-
chimeric mutant, substrate ATP, pH 7.4, 37°C
0.36
diphosphate
chimeric mutant, substrate ATP, pH 7.4, 37°C
0.44
diphosphate
-
chimeric mutant, substrate glucose 1-phosphate, pH 7.4, 37°C
0.44
diphosphate
chimeric mutant, substrate glucose 1-phosphate, pH 7.4, 37°C
0.55
diphosphate
-
chimeric mutant, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.55
diphosphate
-
reduced wild-type, substrate ATP, pH 7.4, 37°C
0.81
diphosphate
-
oxidized wild-type, substrate ATP, pH 7.4, 37°C
0.9
diphosphate
wild-type, substrate ATP, pH 7.4, 37°C
0.022
phosphate
-
pH 7.5, in absence of activators
0.025
phosphate
pH 8.0, in absence of 0.25 mM 3-phosphoglycerate
0.038
phosphate
-
pH 8.5, 37°C, in absence of 3-phosphoglycerate
0.04
phosphate
-
pH 8.0, 37°C, recombinant heterotetrameric enzyme, in absence of 3-phosphoglycerate
0.044
phosphate
-
pH 7.0, 37°C, in absence of 3-phosphoglycerate
0.045
phosphate
-
pH 8.0, 37°C, in absence of 3-phosphoglycerate
0.054
phosphate
-
pH 8.0, 37°C, in absence of 3-phosphoglycerate
0.06
phosphate
-
pH 7.5, 37°C, in absence of 3-phosphoglycerate
0.064
phosphate
-
pH 7.3, 37°C, in absence of phosphoglycerate
0.072
phosphate
-
in absence of 3-phosphoglycerate
0.08
phosphate
-
pH 8.0, 37°C, the small subunit of enzyme, in presence of 3 mM 3-phosphoglycerate
0.088
phosphate
-
pH 7.5, 37°C, in absence of 3-phosphoglycerate
0.095
phosphate
-
pH 7.0, 37°C, in absence of 3-phosphoglycerate
0.12
phosphate
-
pH 7.5, 37°C, in presence of 3-phosphoglycerate
0.14
phosphate
-
pH 7.0, 37°C, in absence of 3-phosphoglycerate
0.18
phosphate
-
pH 8.5, in absence of 3-phosphoglycerate
0.18
phosphate
-
pH 7.5, 30°C, in the absence of 3-phosphoglycerate
0.19
phosphate
-
pH 8.0, in presence of 0.5 mM 3-phosphoglycerate
0.2
phosphate
-
pH 8.0, 37°C, in presence of 0.25 mM 3-phosphoglycerate
0.2
phosphate
leaf enzyme in absence of 3-phosphoglycerate
0.23
phosphate
-
in absence of 0.01 mM fructose 6-phosphate
0.26
phosphate
-
influence of activators
0.37
phosphate
pH 8.0, 37°C
0.4
phosphate
-
pH 8.0, in presence of 1 mM 3-phosphoglycerate
0.44
phosphate
-
pH 7.4, 37°C, in presence of 1 mM 3-phosphoglycerate
0.46
phosphate
-
pH 7.0, 37°C, in presence of 2.5 mM 3-phosphoglycerate
0.53
phosphate
-
pH 8.0, 37°C, in presence of 2.5 mM 3-phosphoglycerate
0.57
phosphate
-
pH 7.0, 37°C, in presence of 2.5 mM 3-phosphoglycerate
0.63
phosphate
-
pH 8.0, 37°C, recombinant heterotetrameric enzyme, in presence of 3 mM 3-phosphoglycerate
0.7
phosphate
-
in absence of fructose 6-phosphate
0.7
phosphate
endosperm enzyme in absence of 3-phosphoglycerate
0.72
phosphate
-
pH 8.5, 37°C, in presence of 3-phosphoglycerate
0.91
phosphate
endosperm enzyme in presence of 0.25 mM 3-phosphoglycerate
0.93
phosphate
-
pH 8.0, 37°C, strains LT-2, in presence of 0.25 mM fructose 1,6-bisphosphate
0.97
phosphate
-
pH 7.3, 37°C, in presence of 3-phosphoglycerate
1
phosphate
-
pH 8.5, in presence of 2 mM 3-phosphoglycerate
1
phosphate
-
the phosphate inhibition pattern of Mos(1-198) is complex and biphasic. Inhibition at relatively high phopshate concentrations is less than predicted at low phosphate concentrations, the calculated Ki for phosphate is about 1 mM before 50% inhibition and 36 mM after 50% inhibition. Inhibition kinetics of mutants in presence and absence of 3-phosphoglycerate
1
phosphate
-
the phosphate inhibition pattern of Mos(1-198) is complex and biphasic. Inhibition at relatively high phosphate concentrations is less than predicted at low phosphate concentrations, the calculated Ki for phosphate is about1 mM before 50% inhibition and 36 mM after 50% inhibition. Inhibition kinetics of mutants in presence and absence of 3-phosphoglycerate
1.15
phosphate
-
pH 7.5, 37°C, in presence of 3-phosphoglycerate
1.27
phosphate
-
pH 7.3, 37°C, in presence of 3-phosphoglycerate
1.3
phosphate
-
pH 8.0, 37°C, strains JP102, in presence of 0.25 mM fructose 1,6-bisphosphate
1.3
phosphate
-
pH 7.5, in presence of 1 mM 3-phosphoglycerate
1.4
phosphate
-
wild-type enzyme, in presence of 3-phosphoglycerate
1.4
phosphate
-
wild-type enzyme, in presence of 3-phosphoglycerate
1.5
phosphate
-
pH 7.0, 37°C, in presence of 3-phosphoglycerate
1.5
phosphate
-
pH 7.5, 5°C, in the absence of 3-phosphoglycerate
1.52
phosphate
endosperm enzyme in presence of 1 mM 3-phosphoglycerate
1.7
phosphate
-
pH 8.0, 37°C, strains LT-2, in presence of 1 mM fructose 1,6-bisphosphate
1.83
phosphate
mutant BT2/S163F, 15 mM 3-phosphoglycerate
2
phosphate
-
pH 8.0, 37°C, strains JP102, in presence of 1 mM fructose 1,6-bisphosphate
2.28
phosphate
mutant BT2/C382F, 15 mM 3-phosphoglycerate
2.4
phosphate
-
in absence of 0.1 mM fructose 6-phosphate
2.49
phosphate
endosperm enzyme in presence of 5 mM 3-phosphoglycerate
2.96
phosphate
-
pH 7.4, 37°C, enzyme from maize endosperm
3.21
phosphate
mutant BT2/Q213H, 15 mM 3-phosphoglycerate
3.72
phosphate
mutant BT2/P372A, 15 mM 3-phosphoglycerate
3.95
phosphate
-
pH 7.4, 37°C, short day photoperiod
3.96
phosphate
mutant BT2/H149S, 15 mM 3-phosphoglycerate
4.26
phosphate
mutant BT2/D368S, 15 mM 3-phosphoglycerate
4.26
phosphate
-
pH 7.4, 37°C, long day photoperiod
5.34
phosphate
mutant BT2/T361C, 15 mM 3-phosphoglycerate
8.7
phosphate
-
pH 8.0, 37°C, strain ATCC 15365
8.7
phosphate
-
mutant Mos(1-198), in presence of 3-phosphoglycerate
8.7
phosphate
-
mutant Mos(1-198), in presence of 3-phosphoglycerate
9.8
phosphate
-
pH 7.4, 37°C, in presence of 10 mM 3-phosphoglycerate
13.23
phosphate
mutant BT2/C114A, 15 mM 3-phosphoglycerate
14.5
phosphate
mutant BT2/V227R, 15 mM 3-phosphoglycerate
15.22
phosphate
mutant BT2/E438Q, 15 mM 3-phosphoglycerate
16.8
phosphate
wild type BT2/SH2, 15 mM 3-phosphoglycerate
17.61
phosphate
mutant BT2/M172T, 15 mM 3-phosphoglycerate
17.93
phosphate
mutant BT2/V502T, 15 mM 3-phosphoglycerate
18.36
phosphate
mutant BT2/C424V, 15 mM 3-phosphoglycerate
20.43
phosphate
mutant BT2/A508S, 15 mM 3-phosphoglycerate
0.047
phosphoenolpyruvate
-
influence of activators
0.12
phosphoenolpyruvate
pH 8.0, 37°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Ki of AMP, effect of fructose 1,6-bisphosphate on wild-type and mutant enzymes
-
additional information
additional information
-
Ki of phosphate, ADP, AMP when NADPH, fructose 1,6-bisphosphate and pyridoxalphosphate are activators
-
additional information
additional information
-
Ki of phosphate, ADP, AMP when NADPH, fructose 1,6-bisphosphate and pyridoxalphosphate are activators
-
additional information
additional information
comparison of Ki of phosphate
-
additional information
additional information
-
comparison of Ki of phosphate
-
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H379K
site-directed mutagenesis, kinetics compared to the wild-type enzyme
H379R
site-directed mutagenesis, kinetics compared to the wild-type enzyme
A114T
14% of wild-type activity
A33K
-
mutation in leaf-specific large subunit ApL1, little effect on affinity of holoenzyme for substrates
A33K/G96N
-
mutation in leaf-specific large subunit ApL1, little effect on affinity of holoenzyme for substrates. Double mutant is less susceptible for inhibition by phosphate and shows increased sensitivity to 3-phosphoglycerate
C81S
mutation in small subunit APS1. Substitution of Cys81 by serine prevents small subunit APS1 dimerization. Cys81 is both necessary and sufficient for dimerization of APS1. Compared to control plants, the C81S lines have higher levels of ADP-glucose and maltose, and either increased rates of starch synthesis or a starch-excess phenotype, depending on the daylength. APS1 protein levels are five- to tenfold lower than in control plants
D349N
49% of wild-type activity
G118D
43% of wild-type activity
G284D
82% of wild-type activity
G284S
109% of wild-type activity
G96N
-
mutation in leaf-specific large subunit ApL1, little effect on affinity of holoenzyme for substrates
G98E
30% of wild-type activity
K267R
site-directed mutagenesis, co-expression of the wild-type APS1 subunit with mutated APL2K267R subunit produces enzymes with altered alpha-D-glucose-1-phosphate S0.5
K271R
site-directed mutagenesis, co-expression of the wild-type APS1 subunit with mutated APL1K71R subunit produces enzymes with altered alpha-D-glucose-1-phosphate S0.5
L106F
68% of wild-type activity
L142F
83% of wild-type activity
P105S
33% of wild-type activity
R102H
30% of wild-type activity
R246Q
106% of wild-type activity
R260H
118% of wild-type activity
R306K
90% of wild-type activity
V52I
93% of wild-type activity
R22A
-
about 15fold decrease in apparent affinity for fructose 6-phosphate compared to that of wild-type
R33A
-
mutant enzyme is insensitive to activation by fructose 6-phosphate
R8A
-
mutant enzyme exhibits reduced fold-activation by fructose 6-phosphate compared to that of wild-type but increased apparent affinity for ATP in the presence of fructose 6-phosphate
D142A
-
Km values are not significantly different in comparison to the wild-type enzyme, no significant changes for fructose 1,6-bisphosphate activation, Ki value of AMP 3fold increases in comparison to the wild-type enzyme
D142E
-
47fold increase of Km value of glucose 1-phosphate and 11.5fold increase of Km value of ATP in comparison to the wild-type enzyme, activation by fructose 1,6-bisphosphate increases, no significant changes for AMP-inhibition in comparison to the wild-type enzyme
D142N
-
Km values are not significantly different in comparison to the wild-type enzyme, Ki value of AMP 25fold increases in comparison to the wild-type enzyme
D239A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D239E
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D239N
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D276A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D276E
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D276N
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
E194A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
E194D
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
E194Q
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
F240A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
F240M
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
G336D
-
a higher activity enzyme form, 10fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
K195Q
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
LP17L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP26L
-
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
LP44E
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44K
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44R
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44S
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44Y
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP55L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP66L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
P103A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
P295D
-
extremely high activity in the absence of fructose 1,6-bisphosphate, 20fold decreased affinity for AMP than wild-type enzyme
P295D/G336D
-
the double mutant enzyme is more active in the absence of fructose 1,6-bisphosphate, with a higher affinity for fructose 1,6-bisphosphate and a lower apparent affinity for AMP than either single mutated enzyme
P295E
-
extremely high activity in the absence of fructose 1,6-bisphosphate, 10fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
P295N
-
3.4fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
P295Q
-
3.8fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
Q106A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
R107A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
R115A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
S212A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
S212T
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
S212V
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
S212Y
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
W274A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
W274F
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
W274L
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
Y114A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
Y216F
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
LP17L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
-
LP26L
-
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
-
LP44L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
-
LP55L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
-
LP66L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
-
A171V
-
mutation in large subunit gene AGPL2. Seeds of mutant plants are severely shriveled and have seed weight and starch content comparable with the shriveled seeds from AGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme are significantly impaired, showing lower specific activities and affinities for the activator 3-phosphoglycerate
T139I
-
mutation in large subunit gene AGPL2. Seeds of mutant plants are severely shriveled and have seed weight and starch content comparable with the shriveled seeds from AGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme are significantly impaired, showing lower specific activities and affinities for the activator 3-phosphoglycerate
OtaL_D171A
-
mutant subunit L
OtaL_K224R
-
mutant subunit L
OtaS_D148A
-
mutant subunit S
OtaS_D148A/K201R
-
double mutant subunit S
OtaS_K201R
-
mutant subunit S
A132D
mutation in ATP binding region of large subunit, kinetic analysis
A132F
mutation in ATP binding region of large subunit, kinetic analysis
A132N
mutation in ATP binding region of large subunit, kinetic analysis
A132V
mutation in ATP binding region of large subunit, kinetic analysis
D157E
mutation in ATP binding region of large subunit, kinetic analysis
D157N
mutation in ATP binding region of large subunit, kinetic analysis
E370G
mutation in the large subunit alters the heterotetrameric stability along with the binding properties of substrate and effectors of the enzyme. The affinity of the large subunit E370G/small subunit wild-type AGPase for glucose-1-phosphate is 3fold less than for wild type AGPase. The mutant enzyme complex requires 3fold more 3-phosphogyceric acid to be activated and lis less heat stable
E38K
the enzyme activities of large subunit mutants E38K, G101N, and E38K/G101N are more readily stimulated by phosphate-ester metabolites, such as fructose 6-phosphate, fructose 2,6-bisphosphate, and ribose 5-phosphate, than that of wild-type
E38K/G101N
in an Escherichia coli mutant defective in the synthesis of ADP-glucose, expression of large subunit mutant E38K/G101N mediates higher glycogen production than wild-type potato AGPase and the single mutant enzymes, E38K and G101N, individually. Purified large subunit mutant E38K/G101N shows higher sensitivity to 3-phosphoglycerate activation and tolerance to phosphate inhibition than mutants E38K or G101N. The enzyme activities of mutants E38K, G101N, and E38K/G101N are more readily stimulated by phosphate-ester metabolites, such as fructose 6-phosphate, fructose 2,6-bisphosphate, and ribose 5-phosphate, than that of wild-type
F332S
-
site-directed mutagenesis in the potato part of the chimeric mutant
G101N
the enzyme activities of large subunit mutants E38K, G101N, and E38K/G101N are more readily stimulated by phosphate-ester metabolites, such as fructose 6-phosphate, fructose 2,6-bisphosphate, and ribose 5-phosphate, than that of wild-type
G128A
mutation in ATP binding region of large subunit, kinetic analysis
G128L
mutation in ATP binding region of large subunit, kinetic analysis
G267L
mutation in ATP binding region of large subunit, kinetic analysis
G267S
mutation in ATP binding region of large subunit, kinetic analysis
G36A
mutation in ATP binding region of large subunit, kinetic analysis
G37A
mutation in ATP binding region of large subunit, kinetic analysis
H341Y
-
site-directed mutagenesis in the potato part of the chimeric mutant
I323V
-
site-directed mutagenesis in the potato part of the chimeric mutant
L46F
-
mutation of small subunit, coexpression with mutation P52L of large subunit, partly restores sensitivity to 3-phosphoglycerate
L48F/V59I
TG-15, significant alteration in effector sensitivity of this homotetrameric enzyme in comparison to wild-type heterotetrameric enzyme
LSH342A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSH89A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSI330K
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSI335R
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSI339A/I330A
-
large subunit mutant, substitution of critical amino acids regarding the formation of the native heterotetrameric enzyme
LSK334A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSK336A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSN102A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSN87A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSP327A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSR45A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSR88A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSR92A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LST328A/I330A
-
large subunit mutant, substitution of critical amino acids regarding the formation of the native heterotetrameric enzyme
LSW135A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSW135R
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
N369H
-
site-directed mutagenesis in the potato part of the chimeric mutant
P112L
-
mutation of small subunit, coexpression with mutation P52L of large subunit, partly restores sensitivity to 3-phosphoglycerate
P17L
-
mutation in large enzyme subunit, moderate effect on catalytic properties
P26L
-
mutation in large enzyme subunit, moderate effect on catalytic properties but severely impaired catalytic rates
P308L
-
mutation of small subunit, coexpression with mutation P52L of large subunit, partly restores sensitivity to 3-phosphoglycerate
P44L
-
mutation in large enzyme subunit, moderate changes in properties toward 3-phosphoglycerate
P55L
-
mutation in large enzyme subunit, moderate effect on catalytic properties
P66L
-
mutation in large enzyme subunit, up-regulatory properties toward 3-phosphoglycerate
Q127M
mutation in ATP binding region of large subunit, kinetic analysis
R350K
-
mutation of small subunit, coexpression with mutation P52L of large subunit, partly restores sensitivity to 3-phosphoglycerate
S302N
-
site-directed mutagenesis, the mutant shows increased solubility of the recombinant potato tuber large subunit and, in turn, enabling it to form a homotetrameric structure. The LS302N homotetramer possesses very little enzyme activity at a level 100fold less than that seen for the unactivated small subunit homotetramer. Unlike the small subunit enzyme, the LS302N homotetramer enzyme is neither activated by the effector 3-phosphoglycerate nor inhibited by phosphate. The mutation significantly enhances glycogen production in bacterial host cells
T129V
mutation in ATP binding region of large subunit, kinetic analysis
T129V/A132V
mutation in ATP binding region of large subunit, kinetic analysis
V347M
-
site-directed mutagenesis in the potato part of the chimeric mutant
L48F/V59I
-
TG-15, significant alteration in effector sensitivity of this homotetrameric enzyme in comparison to wild-type heterotetrameric enzyme
-
H145G
-
mutant shows UDP-glucose pyrophosphorylase activity
H145G/A325V
-
mutant shows UDP-N-acetylglucose pyrophosphorylase activity. Residue A325 is associated with sugar binding
H145G
-
mutant shows UDP-glucose pyrophosphorylase activity
-
H145G/A325V
-
mutant shows UDP-N-acetylglucose pyrophosphorylase activity. Residue A325 is associated with sugar binding
-
A508S
large subunit mutation
bt2-H2328
mutant, an insertion is located in exon 6 of the Bt2 gene generating a 9-bp duplication of bases TGATGTGAC, position 4,422 - 4,431, a comparative transcriptome analysis of wild-type and bt2-H2328 kernels at mid-development leads to the conclusion that the lack of Bt2-encoded AGPase triggers large-scale changes on the transcriptional level that concern mainly genes involved in carbohydrate or amino acid metabolic pathways
C114A
large subunit mutation
C382F
large subunit mutation
C424V
large subunit mutation
D161G
large subunit mutant isolated by iterative saturation mutagenesis to improve heat stability of the enzyme
D368S
large subunit mutation
E438Q
large subunit mutation
F332S
-
site-directed mutagenesis in the potato part of the chimeric mutant
H149S
large subunit mutation
H333T
-
Sh2hs33, coexpression with wild-type Brittle2: 5 min 60°C heat treatment, 76% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2, enhanced subunit interaction in this mutant
H333T/T460I
-
Sh2hs40, coexpression with wild-type Brittle2: 5 min 60°C heat treatment, 72% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
H341Y
-
site-directed mutagenesis in the potato part of the chimeric mutant
I323V
-
site-directed mutagenesis in the potato part of the chimeric mutant
L38E
-
UpReg-1, this mutation greatly increases activation by 3-phosphoglycerate
L93Thr
-
Sh2-UR1, this mutation does not alter 3-phosphoglycerate activation and phosphate inhibition
M172T
large subunit mutation
N369H
-
site-directed mutagenesis in the potato part of the chimeric mutant
P372A
large subunit mutation
Q213H
large subunit mutation
Q96G/D161G/A443R
large subunit mutant isolated by iterative saturation mutagenesis to improve heat stability of the enzyme. Mutant additionally shows an increase affinity for activator 3-phosphoglyceric acid
R104A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R104T
-
Sh2hs16, coexpression with wild-type Brittle2: 5 min 60°C heat treatment, 37% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
R107A
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R116A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R146A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R217P/H333T
-
Sh2hs47, coexpression with wild-type Brittle2: 5min 60°C heat treatment, about 65% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
R340A
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R381A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R77K
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
S163F
large subunit mutation
S34E/Y36C
-
significant increase in heat stability as compared to wild-type enzyme
S34Q/Y36C
-
significant increase in heat stability as compared to wild-type enzyme. The ratio of turnover-number to KM-value for ATP is 2.1fold higher than wild-type ratio, the ratio of turnover-number to KM-value for alpha-D-glucose 1-phosphate is 2.6fold higher than wild-type ratio
T361C
large subunit mutation
T462I
-
random mutagenesis, small subunit mutant BT2-TI, BT2-TI exhibits enhanced heat stability compared to wildtype maize endosperm AGPase
V227R
large subunit mutation
V347M
-
site-directed mutagenesis in the potato part of the chimeric mutant
V502T
large subunit mutation
Y36C
-
significant increase in heat stability as compared to wild-type enzyme
P295G
-
activity in the absence of fructose 1,6-bisphosphate is similar to wild-type enzyme
P295G
-
3fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
W113A
-
mutation does not change apparent affinities for the substrates, but mutant becomes insensitive to activation by fructose-1,6-bisphosphate. The mutant enzymes still binds fructose-1,6-bisphosphate, with similar affinity as the wild type enzyme
W113A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
D157L
mutation in ATP binding region of large subunit, kinetic analysis
D157L
mutation in ATP binding region of large subunit, plus mutation D143N in small subunit, kinetic analysis
K41R
mutation in ATP binding region of large subunit plus mutation D143N in small subunit, kinetic analysis
K41R
mutation in ATP binding region of large subunit, kinetic analysis
K41R/T51K
mutation in ATP binding region of large subunit, kinetic analysis
K41R/T51K
mutation in ATP binding region of large subunit, plus mutation D143N in small subunit, kinetic analysis
P52L
-
mutation in large enzyme subunit, down-regulatory properties toward 3-phosphoglycerate
P52L
-
mutation in large subunit, mutant is 5fold less sensitive to activation by 3-phosphoglycerate
T51K
mutation in ATP binding region of large subunit, kinetic analysis
T51K
mutation in ATP binding region of large subunit, plus mutation D143N in small subunit, kinetic analysis
additional information
-
construction of two chimeric enzymes, AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme and EA is the inverse construction, chimeric enzyme AE is activated by D-fructose 1,6-bisphosphate, D-fructose 6-phosphate and pyruvate, chimeric enzyme AE is only activated by pyruvate
additional information
site-directed mutagenesis of conserved glycines in this region, G20, G21, and G23, results in substantial loss of activity
additional information
-
site-directed mutagenesis of conserved glycines in this region, G20, G21, and G23, results in substantial loss of activity
additional information
-
chimeric enzyme containing N-terminus of Solanum tuberosum enzyme small subunit and C-terminus of Anabaena sp. small subunit and the inverse chimera. The N-terminus determines stability and regulatory redox-dependent properties. The interaction between the putative N- and C-domains determines the affinity for 3-phosphoglycerate
additional information
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
-
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
-
generation of hybrid enzymes using Solanum tuberosum large subunit and Arabidopsis thaliana small subunit and vice versa using different arabidospsis large subunit isoforms. Hybrid potato small subunit with Arabidopsis large subunit APL1 is extremely sensitive against 3-phosphoglycerate and phosphate, while hybrid potato small subunit with Arabidosis large subunit APL2 is rather insensitive to both
additional information
construction of a T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
construction of a T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
construction of a T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
construction of a T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
construction of a T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
additional information
complementation of an aps1 null mutant with a series of constructs containing a full-length APS1 gene encoding either the wild-type APS1 protein or mutated forms in which one of the five cysteine residues is replaced by serine. Substitution of Cys81 by serine prevents small subunit APS1 dimerization, whereas mutation of the other cysteines had no effect
additional information
-
complementation of an aps1 null mutant with a series of constructs containing a full-length APS1 gene encoding either the wild-type APS1 protein or mutated forms in which one of the five cysteine residues is replaced by serine. Substitution of Cys81 by serine prevents small subunit APS1 dimerization, whereas mutation of the other cysteines had no effect
additional information
use of TILLING, i.e.Targeting Induced Local Lesions IN Genomes, of a chemically mutagenised population of plants to identify novel mutations in the APS1 gene, and high throughput measurements using a robotised cycling assay
additional information
-
use of TILLING, i.e.Targeting Induced Local Lesions IN Genomes, of a chemically mutagenised population of plants to identify novel mutations in the APS1 gene, and high throughput measurements using a robotised cycling assay
additional information
enzyme inactivation mutant results in complete loss of glycogen in all media tested and a distinct lag phase upon inoculation of cells in minimal medium containing 750 mM NaCl. Inactivation does not affect survival of cells in stationary phase or its glutamate and lysine production
additional information
-
enzyme inactivation mutant results in complete loss of glycogen in all media tested and a distinct lag phase upon inoculation of cells in minimal medium containing 750 mM NaCl. Inactivation does not affect survival of cells in stationary phase or its glutamate and lysine production
additional information
-
construction of two chimeric enzymes, AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme and EA is the inverse construction, chimeric enzyme AE is activated by D-fructose 1,6-bisphosphate, D-fructose 6-phosphate and pyruvate, chimeric enzyme AE is only activated by pyruvate
additional information
-
deletion of 3,7,11, and 15 amino acids from N-terminus results in specific activites of mutants comparable to wild-type. Deletion of N-terminal 19 amino acids decreases the catalytic activity by two orders of magnitude. Coexpression of a mutant lacking N-terminal 15 amino acids and C-terminal 108 amino acids with C-terminal peptide of 108 amino acids recovers the sensitivity for allosteric effectors that is lost in the N-terminal deletion mutants that lack more than 7 amino acids
additional information
-
expression of gene in maize under control of an endosperm-specific promoter. Developing seeds show 2-4fold higher levels of enzyme activity in the presence of 5 mM phosphate. Under phosphate-inhibitory conditions, transgenic plants show increases in seed weight over the control. In transgenic plants, the seeds are fully filled, and the seed number has no significant difference from untransformed control
additional information
-
generation of pentapeptide insertions at different positions of the enzyme and analysis of proteins with homology model. Region around L102P103 is critical for allosteric regulation of the enzyme
additional information
-
mutational analysis using random mutagenesis for creation of diverse insertion, deletion and point mutations, structure-function analysis, overview, the mutant enzyme with a pentapeptide insertion between Leu102 and Pro103 is catalytically competent but insensitive to activation
additional information
-
Escherichia coli mutant glgC gene, glgC16, encodes a highly active and allosterically insensitive AGPase, developing seeds from transgenic maize plants show up to 2-4-fold higher levels of AGPase activity in the presence of phosphate, phenotype, overview
additional information
-
Escherichia coli mutant glgC gene, glgC16, encodes a highly active and allosterically insensitive AGPase, developing seeds from transgenic maize plants show up to 2-4-fold higher levels of AGPase activity in the presence of phosphate, phenotype, overview
-
additional information
generation of transgenic plants bearing antisense DNA of enzyme small subunit FagpS. Most transgenic fruit do not show differences in weight and hardness, but starch content in fruit is decreased to 27-47% and total soluble sugar content is increased to 16-37% compared to control. Sugar contents are particularly higher in the red stage of fruit. In other tissues, FagpS expression levle is similar to wild-type
additional information
-
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additional information
in mutant Riso 16, the Hv.AGP.S.1. gene is substantially deleted and therefore inactive and lacks the cytosolic small subunit of enzyme in the endosperm and cytosolic enzyme activity, the Hv.AGP.S.2. gene is not affected in Riso and it has a normal plastidial enzyme activity
additional information
in mutant Riso 16, the Hv.AGP.S.1. gene is substantially deleted and therefore inactive and lacks the cytosolic small subunit of enzyme in the endosperm and cytosolic enzyme activity, the Hv.AGP.S.2. gene is not affected in Riso and it has a normal plastidial enzyme activity
additional information
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in mutant Riso 16, the Hv.AGP.S.1. gene is substantially deleted and therefore inactive and lacks the cytosolic small subunit of enzyme in the endosperm and cytosolic enzyme activity, the Hv.AGP.S.2. gene is not affected in Riso and it has a normal plastidial enzyme activity
additional information
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AGP-antisense plants show flowers with abnormal petal limbs due to the early termination of the expansion growth of the petal limbs between the corolla lobes, the cell expansion is limited in NtAGP-antisense plants but cell numbers remained unchanged. Enzyme mRNA levels and starch content in the sepal tissues of AGP-antisense plants are reduced, resulting in significantly lower levels of sugars, sucrose, glucose, and fructose, in the petal limbs. The feeding of these sugars to flower buds of the AGP-antisense plants restores the expansion growth in the limb area between the corolla lobes, which is severely arrested in Xanthi flowers from which sepals are removed
additional information
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lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
additional information
lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
additional information
lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
additional information
lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
additional information
lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
additional information
lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
additional information
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isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
additional information
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isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
additional information
isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
additional information
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mutant apl1 of rice with a Tos17 insertion and lacking the leaf large subunit of ADP-glucose pyrophosphorylase has drastically reduced leaf starch content but grows normally, phenotype, overview
additional information
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tomato plants harboring the gene AgpL1 for ADP-glucose pyrophosphorylase large subunit from wild species Solanum habrochaites show an increase in enzyme activity correlating with a prolonged expression of the L1 protein. The small subunit also remains for an extended period of fruit development due to prolonged stability of the heterotetramer in presence of the L1 protein. Mature fruit show an increased starch content and higher soluble solids
additional information
expression of the large subunit isoforms L1 to L3 in Escherichia coli, in conjunction with small subunit S and individually and kinetic characterisation of the L1/S and L3/S heterotetramers. The recombinant L3 subunit is also active when expressed alone
additional information
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expression of the large subunit isoforms L1 to L3 in Escherichia coli, in conjunction with small subunit S and individually and kinetic characterisation of the L1/S and L3/S heterotetramers. The recombinant L3 subunit is also active when expressed alone
additional information
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mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber. Km for ATP and alpha-D-glucose 1-phosphate do not differ significantly for the mosaic enzymes in the presence of 3-phosphoglycerate. 2fold increase in Km for ATP when the potato small subunit is combined with the maize large subunit (Pss/Mls). Interestingly, the turnover number is increased for all mosaics
additional information
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chimeric enzyme containing N-terminus of Solanum tuberosum enzyme small subunit and C-terminus of Anabaena sp. small subunit and the inverse chimera. The N-terminus determines stability and regulatory redox-dependent properties. The interaction between the putative N- and C-domains determines the affinity for 3-phosphoglycerate
additional information
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generation of hybrid enzymes using Solanum tuberosum large subunit and Arabidopsis thaliana small subunit and vice versa using different arabidospsis large subunit isoforms. Hybrid potato small subunit with Arabidopsis large subunit APL1 is extremely sensitive against 3-phosphoglycerate and phosphate, while hybrid potato small subunit with Arabidosis large subunit APL2 is rather insensitive to both
additional information
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construction of a LRKNSWT heterotetramer, the LS mutant homotetramer LRKN is catalytically very inefficient, binds ATP less efficiently, and is less heat-stable, overview
additional information
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expression of the maize/potato small subunit mosaic mutant MP, Mos(1-198), containing the first 198 amino acids of the small subunit of the maize endosperm enzyme and the last 277 amino acids from the potato tuber enzyme, Mos(1-198) and its derivatives are expressed exclusively with the wt maize large subunit, SH2. In the absence of activator, performs like a wild-type AGPase that is partially activated with ADP-D-glucose, enzymatic activity in the absence of 3-phosphoglycerate is substantially 2-5fold higher than that of wild-type enzyme, while in presence of 3-phosphoglycerate, Mos(1-198) AGPase activity is actually less than that of wild-type enzyme, phenotype, mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator, overview. Mutational exchange of carboxylterminal region containing 15 polymorphic amino acids from 377 to 475 to create Mos(1-198, 430-475) and Mos(1-198, 377-429) leading to reduced enzyme activity independent of 3-phosphoglycerate. Constructed mutant Mos(1-277) exhibits 3-phosphoglycerate-independent activity that is less than mutant Mos(1-198) and wild-type activity. Mutant Mos(1-321) has no detectible activity in the absence of 3-phosphoglycerate. In the presence of 3-phosphoglycerate however, Mos(1-321) activity in the reverse direction is identical to that of Mos(1-277), overview
additional information
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construction of a hybrid AGPase composed of portions from the maize endosperm and the potato tuber AGPases in the small subunit paired with a wild-type maize large subunit. The chimeric maize/potato heat stable enzyme lacks the cysteine responsible for redox changes
additional information
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the modified maize AGP large subunit sequence Sh2r6hs encodes a subunit with increased AGP activity leading to plants with increased seed yield, and plant size, phenotypes of transgenic plants, overview
additional information
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mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber. Km for ATP and alpha-D-glucose 1-phosphate do not differ significantly for the mosaic enzymes in the presence of 3-phosphoglycerate. 2fold increase in Km for ATP when the potato small subunit is combined with the maize large subunit (Pss/Mls). Interestingly, the turnover number is increased for all mosaics
additional information
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expression of maize Sh2r6hs transgene, a modified maize Sh2 cDNA coding sequence with alterations conferring reduced sensitivity to phosphate inhibition and greater heat stability, in Triticum aestivum results in increased photosynthetic rates under high light but not low light conditions, peaking at 7 days after flowering. Transgenic plants show increases in levels of fructose, glucose, and sucrose in flag leaves at 7 and 14 days after flowering
additional information
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expression of the maize/potato small subunit mosaic mutant MP, Mos(1-198), containing the first 198 amino acids of the small subunit of the maize endosperm enzyme and the last 277 amino acids from the potato tuber enzyme, Mos(1-198) and its derivatives are expressed exclusively with the wild-type maize large subunit, SH2. In the absence of activator, performs like a wild-type AGPase that is partially activated with 3-phosphoglycerate, enzymatic activity in the absence of 3-phosphoglycerate is substantially 2-5fold higher than that of wild-type enzyme, while in presence of 3-phosphoglycerate, Mos(1-198) AGPase activity is actually less than that of wild-type enzyme, phenotype, mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator, overview. Mutational exchange of carboxylterminal region containing 15 polymorphic amino acids from 377 to 475 to create Mos(1-198, 430-475) and Mos(1-198, 377-429) leading to reduced enzyme activity independent of 3-phosphoglycerate. Constructed mutant Mos(1-277) exhibits 3-phosphoglycerate-independent activity that is less than mutant Mos(1-198) and wild-type activity. Mutant Mos(1-321) has no detectible activity in the absence of 3-phosphoglycerate. In the presence of 3-phosphoglycerate however, Mos(1-321) activity in the reverse direction is identical to that of Mos(1-277), overview
additional information
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heat-stable small subunit variant MP is composed of sequences from the maize endosperm and the potato tuber small subunit, construction of a double mutant MP-TI, which may lead to increased starch yield when expressed in monocot endosperms
additional information
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identification of a mutant allele of the leaf-expressed small subunit of ADP-glucose pyrophosphorylase agps-m1, the AGPase mutant is unable to synthesize transitory starch and lacks leaf starch, phenotype, overview
additional information
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mutant Sh2r6hs, expressed in transgenic wheat plants, shows increases in ADP-glucose, UDP-glucose, and fructose at maturity , phenotype, overview
additional information
construction of a hybrid AGPase composed of portions from the maize endosperm and the potato tuber AGPases in the small subunit paired with a wild-type maize large subunit. The chimeric maize/potato heat stable enzyme lacks the cysteine responsible for redox changes
additional information
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construction of a hybrid AGPase composed of portions from the maize endosperm and the potato tuber AGPases in the small subunit paired with a wild-type maize large subunit. The chimeric maize/potato heat stable enzyme lacks the cysteine responsible for redox changes
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