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2-deoxy-D-glucose 6-phosphate + NAD(P)+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NAD(P)H
-
low activity
-
-
?
2-deoxy-D-glucose 6-phosphate + NADP+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADPH
2-deoxy-D-glucose 6-phosphate + NADP+
?
-
-
-
-
?
2-deoxy-D-glucose-6-phosphate + NADP+
2-deoxy-D-gluconate 6-phosphate + NADPH
-
-
-
-
?
6-phosphonogluconate + NADPH
?
D-galactose 6-phosphate + NAD(P)+
D-galactonate 6-phosphate + NADH
D-glucose + NAD(P)+
D-gluconate + NAD(P)H
-
activity only with dimethylsulfoxide added by 40% (v/v)
-
-
?
D-glucose 6-phosphate + deamino-NADP+
?
-
-
-
-
?
D-glucose 6-phosphate + deamino-NADP+
D-glucono-1,5-lactone 6-phosphate + deamino-NADPH
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
D-glucose 6-phosphate + NAD(P)+
D-glucono-1,5-lactone 6-phosphate + NAD(P)H
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
D-glucose 6-phosphate + NADP+
NADPH + ?
-
assay at pH 7.4
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
D-glucose 6-phosphate + thio-NAD(P)+
D-glucono-1,5-lactone 6-phosphate + thio-NAD(P)H
-
the thio-cofactors give increased activity compared to the non-thio-cofactors
-
-
?
D-glucose 6-phosphate + thio-NAD+
6-phospho-D-glucono-1,5-lactone + thio-NADH + H+
-
-
-
-
r
additional information
?
-
2-deoxy-D-glucose 6-phosphate + NADP+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADPH
-
-
-
-
?
2-deoxy-D-glucose 6-phosphate + NADP+
2-deoxy-D-glucono-1,5-lactone 6-phosphate + NADPH
-
wild-type and mutant P409R, below 10% activity compared to D-glucose 6-phosphate
-
-
?
6-phosphonogluconate + NADPH
?
-
isoenzyme II
-
-
?
6-phosphonogluconate + NADPH
?
-
isoenzyme II
-
-
?
D-galactose 6-phosphate + NAD(P)+
D-galactonate 6-phosphate + NADH
-
-
-
-
?
D-galactose 6-phosphate + NAD(P)+
D-galactonate 6-phosphate + NADH
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
sigmoidal relationship in cofactor binding
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
?, ir
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
isoform A(-) shows sigmoidal enzyme-substrate interaction, isoform A(+) shows hyperbolic enzyme-substrate interaction
D-glucose-delta-lactone 6-phosphate
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
hyperbolic cofactor binding
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
glucono-delta-lactone-6-phosphate
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
Penicillium duponti
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
ir
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + NAD(P)+
D-glucono-1,5-lactone 6-phosphate + NAD(P)H
-
key enzyme catalyzing the first step of the pentose phosphate pathway generating NADPH for anabolic metabolsim pathways and protection systems in the liver
-
-
?
D-glucose 6-phosphate + NAD(P)+
D-glucono-1,5-lactone 6-phosphate + NAD(P)H
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
very low activity with NAD+
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
D-glucono-1,5-lactone 6-phosphate + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
r
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
first enzyme of the pentose phosphate pathway, one of the main sources of NADPH
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
oxidative pentose pathway
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
the enzyme is involved pentose biosynthesis
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
NADP+-specific enzyme. In presence of NAD+ 410fold reduction in the performance of the enzyme. Modeling of the sensitivity of reduced cofactor production by G6PDH as a function of the redox ratios of NAD/NADH (rRNAD) and NADP/NADPH (rRNADP). NADPH production sharply increases within the range of thermodynamically feasible values of rRNADP, but NADH production remains low within the range feasible for rRNAD
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
oxidative pentose pathway
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
the enzyme is involved pentose biosynthesis
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
ir
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
ir
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
inhibition by divalent metal ions, at low NADPH /NADP+ ratio, is another means of controlling the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
the substrate specificity is extremely strict
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
catalyzes the first step of the pentose phosphate pathway, enzyme deficiency often causes hemolytic anaemia
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
key enzyme catalyzing the first step in the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
wild-type and mutant P409R
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
involved in oxidative pentose phosphate pathway in roots, related to glutamate synthesis in the plastids
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
key enzyme of the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
G6PDH is the rate-limiting step in the formation of NADPH via the triphosphate, and is responsible for the major supply of NADPH in the cell
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
first step in the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
key enzyme catalyzing the first step of the hexose monophosphate shunt pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
oxidative enzyme of pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
enzyme catalyzes the first step of the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
key regulatory enzyme of the pentose phosphate pathway, regulation mechanism study
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
differential regulation of isozymes, the cytosolic enzyme is regulated by sugar availability at transcriptional level, while the plastidic isozymes are regulated by redox mechanism
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
random bi bi sequential mechanism in rapid equilibrium
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
-
the enzyme is responsible for the production of NADPH, which is required for biosynthetic reactions and protection of cells from free radicals
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
additional information
?
-
-
G6PDH plays a role in supplying NADPH for oil accumulation in developing seeds in which photosynthesis may be light limited
-
-
?
additional information
?
-
-
no activity with glucose and glucosamine 6-phosphate
-
-
?
additional information
?
-
-
no activity with glucose, glucose 1-phosphate, 2-deoxyglucose 6-phosphate, fructose, fructose 6-phosphate, fructose 1,6-diphosphate, mannose, galactose 6-phosphate, NAD+
-
-
?
additional information
?
-
-
no activity with glucose, glucose 1-phosphate, 2-deoxyglucose 6-phosphate, fructose, fructose 6-phosphate, fructose 1,6-diphosphate, mannose, galactose 6-phosphate, NAD+
-
-
?
additional information
?
-
-
the following substances, 1 mM, are not substrates when substituted for D-glucose 6-phosphate: D-glucose 6-phosphate, D-fructose 1-phosphate, D-gluconate 6-phosphate, D-galactose 6-phosphate, D-ribose 5-phosphate, and D-glucose
-
-
?
additional information
?
-
-
the following substances, 1 mM, are not substrates when substituted for D-glucose 6-phosphate: D-glucose 6-phosphate, D-fructose 1-phosphate, D-gluconate 6-phosphate, D-galactose 6-phosphate, D-ribose 5-phosphate, and D-glucose
-
-
?
additional information
?
-
-
the following substances, 1 mM, are not substrates when substituted for D-glucose 6-phosphate: D-glucose 6-phosphate, D-fructose 1-phosphate, D-gluconate 6-phosphate, D-galactose 6-phosphate, D-ribose 5-phosphate, and D-glucose
-
-
?
additional information
?
-
-
both isoenzymes show no activity with glucose and NAD+, isoenzyme I shows no activity with 6-phosphonogluconate
-
-
?
additional information
?
-
-
no activity with other sugars, such as fructose-6-phosphate, glucose-1-phosphate, ribulose 5-phosphate, and ribose 5-phosphate
-
-
?
additional information
?
-
-
G6PD overexpressed in adipocytes in obese (including db/db, ob/ob and diet-induced obesity) mice, in adipocytes and stromal-vascular cells in diabetic db/db mice, and in adipocytes cultured under high-glucose conditions in vitro induces the expression of NADPH oxidase and leads to an increase in oxidative stress
-
-
?
additional information
?
-
-
transgenic (previously susceptible) lines overexpressing G6PDH-encoding gene, displaying high NADPH tolerance engineered for cytosolic expression, show early oxidative bursts, callose deposition, and changes in metabolic parameter
-
-
?
additional information
?
-
-
G6PDH plays a critical role in maintaining cellular reduced glutathione levels under long-term salt stress in plants. NADPH, produced by G6PDH, not only acts as the reducing potential for the output of reduced glutathione, but is involved in the activity of plasma membrane NADPH oxidase under salt stress, which results in hydrogen peroxide accumulation
-
-
?
additional information
?
-
-
the enzyme is a bifunctional enzyme glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase, the enzyme activity is analyzed for the reaction of glucose-6-phosphate dehydrogenase, EC 1.1.1.49, in a coupled assay with diaphorase activity, which uses NADPH to reduce resazurin to form the highly fluorescent molecule resorufin
-
-
?
additional information
?
-
-
physiological regulation of NADP+-NADPH-ratio in the brain is dicussed
-
-
?
additional information
?
-
-
no activity with D-glucose, D-ribose, D-fructose-6-phosphate, D-ribose-5-phosphate
-
-
?
additional information
?
-
-
no activity with D-glucose, D-ribose, D-fructose-6-phosphate, D-ribose-5-phosphate
-
-
?
additional information
?
-
-
both isoenzymes show no activity with glucose and NAD+, isoenzyme I shows no activity with 6-phosphonogluconate
-
-
?
additional information
?
-
-
glucose-6-phosphate dehydrogenase protects the parasite against reactive oxygen species
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
D-glucose 6-phosphate + NAD(P)+
D-glucono-1,5-lactone 6-phosphate + NAD(P)H
-
key enzyme catalyzing the first step of the pentose phosphate pathway generating NADPH for anabolic metabolsim pathways and protection systems in the liver
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
additional information
?
-
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
sigmoidal relationship in cofactor binding
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
isoform A(-) shows sigmoidal enzyme-substrate interaction, isoform A(+) shows hyperbolic enzyme-substrate interaction
D-glucose-delta-lactone 6-phosphate
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
hyperbolic cofactor binding
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
Penicillium duponti
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + H2O + NADP+
D-gluconate 6-phosphate + NADPH + H+
-
-
6-phosphoglucono-delta-lactone
r
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
first enzyme of the pentose phosphate pathway, one of the main sources of NADPH
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
oxidative pentose pathway
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
the enzyme is involved pentose biosynthesis
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
oxidative pentose pathway
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
the enzyme is involved pentose biosynthesis
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
ir
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
ir
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
inhibition by divalent metal ions, at low NADPH /NADP+ ratio, is another means of controlling the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
catalyzes the first step of the pentose phosphate pathway, enzyme deficiency often causes hemolytic anaemia
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
key enzyme catalyzing the first step in the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
involved in oxidative pentose phosphate pathway in roots, related to glutamate synthesis in the plastids
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
key enzyme of the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
G6PDH is the rate-limiting step in the formation of NADPH via the triphosphate, and is responsible for the major supply of NADPH in the cell
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
first step in the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
key enzyme catalyzing the first step of the hexose monophosphate shunt pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
oxidative enzyme of pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
enzyme catalyzes the first step of the pentose phosphate pathway
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
key regulatory enzyme of the pentose phosphate pathway, regulation mechanism study
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
differential regulation of isozymes, the cytosolic enzyme is regulated by sugar availability at transcriptional level, while the plastidic isozymes are regulated by redox mechanism
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
D-glucono-1,5-lactone 6-phosphate + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
-
the enzyme is responsible for the production of NADPH, which is required for biosynthetic reactions and protection of cells from free radicals
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+ + H2O
D-gluconate 6-phosphate + NADPH + H+
-
-
-
-
?
additional information
?
-
-
the enzyme is a bifunctional enzyme glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase, the enzyme activity is analyzed for the reaction of glucose-6-phosphate dehydrogenase, EC 1.1.1.49, in a coupled assay with diaphorase activity, which uses NADPH to reduce resazurin to form the highly fluorescent molecule resorufin
-
-
?
additional information
?
-
-
physiological regulation of NADP+-NADPH-ratio in the brain is dicussed
-
-
?
additional information
?
-
-
glucose-6-phosphate dehydrogenase protects the parasite against reactive oxygen species
-
-
?
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(1H-indol-1-yl)(furan-2-yl)methanone
noncompetitive inhibitor
(1H-indol-1-yl)(tiyophen-2-yl)methanone
competitive inhibitor
(2R,3R)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
(2R,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
(2S,3R)-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
(2S,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate
-
-
(3alpha)-3,21-dihydroxypregnan-20-one
-
(4Z)-4-(3-bromobenzylidene)-1-(4-methylphenyl)pyrazolidine-3,5-dione
-
-
(5Z)-1-(4-bromophenyl)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
(5Z)-1-(4-ethoxyphenyl)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
(5Z)-5-[[5-(2-methyl-4-nitrophenyl)furan-2-yl]methylidene]-1-(3-methylphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione
-
reversible, non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
1-(2-nitro-1-(thiophen-2-yl)ethyl)-1H-indole
competitive inhibitor
16-bromoepiandrosterone
no activity at 0.03 mM
2'-phosphoadenosine 5'-diphosphoribose
-
-
2,3-diphosphoglycerate
-
-
2-[(5Z)-5-(4-hydroxy-3-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoate
-
-
2-[(E)-(4-nitrocyclohexa-2,4-dien-1-yl)(2-phenylhydrazinylidene)methyl]benzene-1,4-diol
-
non-competitive inhibition versus NADP+, non-competitive or mixed-type versus D-glucose 6-phosphate
2-[4-(4-chlorophenyl)-1,3-thiazol-2-yl]-5-methyl-4-(3,4,5-trimethoxybenzyl)-2,4-dihydro-3H-pyrazol-3-one
-
irreversible, non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
3-(3,4-dichlorophenyl)-1,1'-dimethyl urea
-
cytosolic isozyme, inhibition by uncoupling of photosynthetic electron transport
3-(4-hydroxyphenyl)-2-(pyridin-3-yl)quinazolin-4(3H)-one
-
irreversible, non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
3-(5-bromopyridin-2-yl)-2-(pyridin-3-yl)quinazolin-4(3H)-one
-
irreversible, non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
3-(5-[(E)-[2-(5-nitropyridin-2-yl)hydrazinylidene]methyl]furan-2-yl)benzoic acid
-
-
4-fluoro-N-(4-hydroxynaphthalen-1-yl)benzenesulfonamide
-
-
4-methyl-3-(propan-2-yloxy)-6H-benzo[c]chromen-6-one
-
non-competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
weak inhibition
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
weak inhibition
5-[[5-(4-methoxy-2-nitrophenyl)furan-2-yl]methylidene]-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
reversible, competitive inhibition versus NADP+, mixed-type versus D-glucose 6-phosphate
5alpha-androstan-16-alpha-bromo-3beta-ol-17-one
-
in vitro cell viability assays shows a LD50 of 20 microM for Trypanosoma cruzi epimastigotes
5alpha-Androstan-3beta-ol-17-one
-
uncompetitive inhibitor
5alpha-androsten-16-alpha-bromo-3beta-ol-17-one
-
potent inhibitor, in vitro cell viability assays shows a LD50 of 12 microM for Trypanosoma cruzi epimastigotes
6-amino-NAD+
-
irreversibly inhibits G6PD
6-amino-NADP+
-
irreversibly inhibits G6PD
adenosine 5' [beta,gamma-amido] triphosphate
-
-
adenosine 5' [beta-thio] diphosphate
-
-
adenosine 5' [gamma-thio] triphosphate
-
-
amikacin
-
in vitro, noncompetitive
ammonia
-
inhibition in vitro and in vivo at sublethal concentration of 0.0022-0.0055 mM, IC50: 0.0187 mM
beta-naphthoquinone-4-sulfonic acid
-
1 mM, 68% inhibition, G6PDH-1; 1 mM, 81% inhibition, G6PDH-2
brimonidine
competitive inhibition
Ca2+
-
about 90% residual activity at 2 mM
ceftriaxone
-
strongly inhibits
cumene hydroperoxide
-
1% residual activity after treatment with 17 mM cumene hydroperoxide at 50°C and pH 7 for 2 h
cypermethrin
-
inhibits G6PD in vitro
dehydroandrosterone
-
uncompetitive inhibitor
deltamethrin
-
inhibits G6PD both in vivo and in vitro, significantly inhibits activity after the 48th hour. Among pesticides, it is the most effective one, which is widely used both at homes and in agricultural fields. Deltamethrin inhibits the enzyme at very low doses, particularly in in vivo conditions, indicating that fish in natural and cultural environments are susceptible to this pesticide and that deltamethrin contaminations can be cause high mortality in fish population, which may lead to the increase in food insufficiency for increasing populations and cause disruption of ecological balance. Thus, usage of deltamethrin must be well controlled
dithiothreitol
-
about 40% inhibition at 5 mM
ellagic acid
mixed type inhibitor of glucose 6-phosphate activity
gentamicin sulfate
-
in vitro, noncompetitive
glyceraldehyde 3-phosphate
-
-
guanidinium hydrochloride
guanosine hydrochloride
-
the enzyme shows a sharp loss in activity above 0.75 M, but is activated by low concentrations of 0.2 M of GdmCl
hydrogen peroxide
-
inhibitory at 0.25%, at pH 7
lidocaine
-
strongly inhibits
marcaine
-
noncompetitive
meloksikam
-
strongly inhibits
N-(4-chlorobenzoyl)-indole
competitive inhibitor
N-(4-hydroxynaphthalen-1-yl)-2,5-dimethylbenzenesulfonamide
-
-
N-benzoylindole
noncompetitive inhibitor
N-ethyl-N'-[(3alpha)-17-oxoandrostan-3-yl]urea
-
N-[(3alpha)-17-oxoandrostan-3-yl]sulfuric diamide
-
N-[(3alpha)-21-hydroxy-20-oxopregnan-3-yl]sulfuric diamide
-
netilmicin
-
inhibition of wild-type and mutant enzymes 1-3
Ni2+
-
about 95% residual activity at 2 mM
Nicotine
-
inhibits the enzyme from lung, testis, kidney, stomach, and brain, in concert with vitamin E the enzyme from testis brain and liver is inhibited, tissue-specific inhibition of 12.5-48%, overview, nicotine has no effect on enzyme from muscle, heart, and liver
oleic acid
-
G6PDH-1 is more susceptible to oleic acid than G6PDH-2
Pb2+
-
noncompetitive inhibition
penicillin G potassium
-
in vitro, noncompetitive
pental sodium
-
noncompetitive
peracetic acid
-
1% residual activity after treatment with 4 mM peracetic acid at 25°C and pH 7 for 15 min
phenylmethylsulfonyl fluoride
-
about 48% inhibition at 5 mM
phosphoenol pyruvate
-
25% inhibition at 10 mM
prilocaine
-
strongly inhibits
propoxur
-
inhibits G6PD in vitro
pyridoxal 5'-phosphate
-
-
quartz
-
24 h incubation with quartz particles (80 microg/cm(2)) inhibits G6PD activity by 70%. Inhibition is fully prevented by glutathione. Silica exerts on G6PD an oxidative damage
-
Ribulose 1,5-diphosphate
-
-
sodium ceftizoxime
-
inhibition of wild-type and mutant enzymes 1-3
sodium cefuroxime
-
inhibition of wild-type and mutant enzymes 1-3
streptomycin
-
inhibition of wild-type and mutant enzyme 3
suramin
-
77% inhibition at 0.05 mM
tert-butyl hydroperoxide
-
1% residual activity after treatment with 290 mM tert-butyl hydroperoxide at 50°C and pH 7 for 3 h
Thioredoxin f
-
from chloroplasts
-
Tl+
-
201Tl solution and radiation exposure has inhibitory effects on the enzyme activity both in vivo and in vitro
Trypsin
after 2 h of trypsin digestion in the presence of 0.01 mM NADP+ the enzyme retains about 57% of its original activity
-
Urea
-
inhibition in vitro and in vivo at sublethal concentration of 0.02-0.05 mM, IC50: 0.0238 mM
vitamin E
-
in concert with nicotine the enzyme from testis brain and liver is inhibited, while the enzyme from muscle and stomach is activated, overview
ADP
-
-
ADP
-
15% inhibition at 2 mM
ADP
-
about 65% inhibition at 5 mM
AMP
-
5% inhibition at 2 mM
ATP
-
-
ATP
-
31% inhibition at 5 mM, non-competitive inhibition with respect to D-glucose 6-phosphate
ATP
-
2.0 mM, 65% inhibition, G6PDH-2; G6PDH-1
ATP
-
10 mM, 50-75% inhibition, assay without MgCl2
ATP
-
weak, noncompetitive inhibition
ATP
-
15% inhibition at 2.5 mM, 24% inhibition at 10 mM
Cd2+
-
-
Cd2+
-
1 mM, 53% inhibition, G6PDH-1
Cd2+
-
1 mM, 83% inhibition
Cd2+
-
noncompetitive inhibition
Co2+
-
competitive, 60% inhibition at 0.01 mM
Co2+
-
1 mM, 56% inhibition
Cu2+
-
potent inhibitor, about 65% residual activity at 2 mM (isoform G6PD2), about 50% residual activity at 2 mM (isoform G6PD1)
Cu2+
-
about 15% residual activity at 5 mM
Cu2+
-
1 mM, 24% inhibition, G6PDH-1; 1 mM, 78% inhibition, G6PDH-2
Cu2+
-
1 mM, complete inhibition
Cu2+
-
noncompetitive inhibition
D-glucose 6-phosphate
-
about 48% inhibition at 5 mM
D-glucose 6-phosphate
-
-
dehydroepiandrosterone
-
non-competitively inhibits
dehydroepiandrosterone
-
uncompetitively inhibits bloodstream form cells
DTT
-
-
DTT
-
1 mM, 2 h, 20% loss of activity in the first 15 min and then the enzyme activity remains steady throughout the incubation
EDTA
-
5 mM, 85% inhibition, G6PDH-1; 5 mM, 97% inhibition, G6PDH-2
epiandrosterone
-
non-competitively inhibits
epiandrosterone
-
uncompetitively inhibits bloodstream form cells
epiandrosterone
uncompetitive inhibitor, 12% residual activity at 0.03 mM
Fe2+
-
potent inhibitor, about 10% residual activity at 5 mM (isoform G6PD2), about 30% residual activity at 5 mM (isoform G6PD1)
Fe2+
-
about 30% residual activity at 5 mM
Fe2+
-
strong competitive inhibition
Fe3+
-
enzyme activities are significantly decreased in the presence of 30 and 300 ppm Fe3+
Fe3+
competitive inhibitor against the G6PD enzyme with respect to NADP+ and D-glucose 6-phosphate
glucosamine 6-phosphate
-
competitive G6PDH inhibitor
glucosamine 6-phosphate
-
parabolic inhibition
glucose
-
at concentration above 10 mM
glucose
-
high glucose level of 25 mM leads to a decrease in G6PD activity and protein level in islets
GTP
-
-
guanidinium hydrochloride
-
denatures
guanidinium hydrochloride
-
in the presence of 4 M, after 2 hours all secondary structure is lost
Hg2+
-
1 mM, 47% inhibition, G6PDH-2; 1 mM, 84% inhibition, G6PDH-1
Hg2+
-
1 mM, complete inhibition
Hg2+
-
noncompetitive inhibition
metamizol
-
strongly inhibits
metamizol
-
inhibition of wild-type and mutant enzyme 3
Mn2+
-
about 10% residual activity at 5 mM (isoform G6PD2)
Mn2+
-
1 mM, 56% inhibition
NADH
-
about 38% inhibition at 5 mM
NADH
-
allosteric inhibition, inhibition is not reversed by NAD+, AMP, or spermidine
NADP+
-
substrate inhibition
NADP+
-
at concentrations above 0.3 mM
NADP+
-
at high concentration, dead-end ternary complexes are formed
NADPH
-
-
NADPH
-
product inhibition
NADPH
-
competitive inhibition
NADPH
-
competitive inhibition with respect to NADP+ and D-glucose 6-phosphate
NADPH
-
about 90% inhibition at 0.2 mM
NADPH
-
has a regulatory role in pentaose phosphate pathway
NADPH
-
product inhibition with NADP+ or D-glucose 6-phosphate as the varying substrate
NADPH
-
when NADP+ is the varied substrate, NADPH NADPH is a competitive inhibitor both in the presence and absence of Mg2+, linear competitive inhibition. When glucose 6-phosphate is the varied substrate NADPH causes linear noncompetitive inhibition
NADPH
-
NADPH binding is important for physiological regulation of pentose phosphate pathway
NADPH
-
slight inhibition
NADPH
-
inhibition patterns of substrates and product
NADPH
-
liver enzyme is more sensitive to inhibition than kidney enzyme
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
can be reversed 100% by dithiothreitol, partially by glutathione
p-chloromercuribenzoate
-
-
palmitoyl-CoA
-
-
palmitoyl-CoA
-
non-competitive
palmitoyl-CoA
-
leads to dissociation of active tetramers to inactive dimers
palmitoyl-CoA
-
leads to dissociation of active tetramers to inactive dimers
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
13% inhibition at 2.5 mM, 31% inhibition at 10 mM
RNAi
-
suppression of endogenous cytosolic G6PDH isoforms result in highly uniform defense responses and also enhanced drought tolerance and flowering
-
RNAi
-
mediates reduction of the G6PDH level in bloodstream form cells
-
Vancomycin
-
-
Zn2+
-
competitive, 40% inhibition at 0.01 mM
Zn2+
-
potent inhibitor, about 58% residual activity at 5 mM (isoform G6PD2), about 35% residual activity at 2 mM (isoform G6PD1)
Zn2+
-
about 50% residual activity at 5 mM
Zn2+
-
1 mM, 83% inhibition, G6PDH-2; 1 mM, 94% inhibition, G6PDH-1
Zn2+
-
noncompetitive inhibition
additional information
Trx f1 regulates G6PDH1 activity as efficiently as Trx m1 or m4. Trx x is a very poor regulator of G6PDH activity. Trx y1 is inefficient as inhibitor but it shows high efficiency in activation. Upon illumination, a strong and fast reductive inhibition of G6PDH1 activity dependent on the presence of all the components of the Fd/Trx system
-
additional information
during 7 days of phosphate starvation, G6PD5 is continuously expressed throughout phosphate-starvation; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced
-
additional information
during 7 days of phosphate starvation, G6PD5 is continuously expressed throughout phosphate-starvation; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced
-
additional information
during 7 days of phosphate starvation, G6PD5 is continuously expressed throughout phosphate-starvation; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced
-
additional information
during 7 days of phosphate starvation, G6PD5 is continuously expressed throughout phosphate-starvation; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced
-
additional information
during 7 days of phosphate starvation, G6PD5 is continuously expressed throughout phosphate-starvation; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced
-
additional information
during 7 days of phosphate starvation, G6PD5 is continuously expressed throughout phosphate-starvation; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced
-
additional information
-
during 7 days of phosphate starvation, G6PD5 is continuously expressed throughout phosphate-starvation; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced; during 7 days of phosphate starvation, transcript levels are reduced
-
additional information
-
product and dead-end inhibition studies, overview, no inhibition by AMP
-
additional information
-
less than 8% inhibition with 1,10-phenanthroline, ATP, EDTA, and iodoacetamide. Not inhibited by NAD+
-
additional information
-
NADH: no inhibition at up to 0.5 mM
-
additional information
-
hyperaldosteronism downregulates G6PD and whereby decreases GSH levels and conversely increases oxidative stress, which evokes endothelial-derived NO and impairs vascular function
-
additional information
-
fluoride-containing bioactive glasses as used in tissue engineering as well as bone repair, inhibit the pentose phosphate oxidative pathway and the glucose 6-phosphate dehydrogenase activity. The effects are ascribable to the fluoride content/release of glass powders, they are mimicked by NaF solutions and are prevented by radical scavengers dimethyl sulfoxide and tempol, by superoxide dismutase, and by glutathione, but not by apocynin
-
additional information
-
non-radioactive Tl+, Fe3+ and Cu2+ do not influence the enzyme in vitro
-
additional information
-
is not inhibited by dehydroepiandrosterone and epiandrosterone
-
additional information
-
effects of streptomycin sulfate and tetracyclin antibiotics
-
additional information
-
high-throughput screening for small-molecule inhibitors of the enzyme from Plasmodium falciparum, inhibitor evaluation, structure-activity relationship analysis, overview
-
additional information
presence of H2O2 only slightly alters enzyme activity or expression
-
additional information
-
presence of H2O2 only slightly alters enzyme activity or expression
-
additional information
-
not inhibited by ATP, phosphate, or Mg2+
-
additional information
-
inhibition of G6PD protects rat hearts from ischemia-reperfusion injury induced by oxidative stress
-
additional information
-
the cytosolic isoyzme is not affected by osmotic change, phosphate sequestration, or ocidative stress
-
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0.374 - 35
2-deoxy-D-glucose 6-phosphate
0.279 - 0.864
6-phosphonogluconate
0.031 - 0.051
D-galactose 6-phosphate
0.0021 - 50.7
D-glucose 6-phosphate
1.5
thio-NAD+
-
pH 7.4, 80°C, recombinant enzyme
0.06
thio-NADP+
-
pH 7.4, 80°C, recombinant enzyme
additional information
additional information
-
0.374
2-deoxy-D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant mutant R454C, with NADP+
24
2-deoxy-D-glucose 6-phosphate
-
pH 7.4, 37°C, with NADP+
35
2-deoxy-D-glucose 6-phosphate
-
pH 7.4, 80°C, recombinant enzyme
0.279
6-phosphonogluconate
-
isoenzyme II
0.864
6-phosphonogluconate
-
isoenzyme II
0.031
D-galactose 6-phosphate
-
isoenzyme II
0.046 - 0.047
D-galactose 6-phosphate
-
isoenzyme I
0.046 - 0.047
D-galactose 6-phosphate
-
isoenzyme I
0.051
D-galactose 6-phosphate
-
isoenzyme II
0.0021
D-glucose 6-phosphate
-
nephridic enzyme
0.0033
D-glucose 6-phosphate
-
hepatic enzyme
0.0078
D-glucose 6-phosphate
-
wild-type enzyme, pH 7.5, 30°C
0.00953
D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant mutant R454C, with NADP+
0.00971
D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant mutant R454H, with NADP+
0.014
D-glucose 6-phosphate
-
25°C, pH 7.8
0.0145
D-glucose 6-phosphate
-
pH 7.5, temperature not specified in the publication
0.019
D-glucose 6-phosphate
-
pH 7.8, 85°C, recombinant enzyme
0.024
D-glucose 6-phosphate
-
-
0.026
D-glucose 6-phosphate
-
pH 8.5, 30°C
0.036
D-glucose 6-phosphate
-
pH 8.0, 25°C
0.037
D-glucose 6-phosphate
-
-
0.04
D-glucose 6-phosphate
-
-
0.04
D-glucose 6-phosphate
-
-
0.04
D-glucose 6-phosphate
-
22°C, liver extralesional parenchyma
0.041
D-glucose 6-phosphate
-
pH 7.4, 37°C
0.042
D-glucose 6-phosphate
-
cosubstrate NADP+
0.0478
D-glucose 6-phosphate
at pH 8.0 and 37°C
0.048
D-glucose 6-phosphate
-
pH 8.0, 25, mutant 2
0.0488
D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant mutant R454C, with deamino-NADP+
0.0491
D-glucose 6-phosphate
-
clinical mutant G488S
0.05
D-glucose 6-phosphate
-
pH 8.0, 25°C
0.05
D-glucose 6-phosphate
-
purified enzyme, at pH 7.5 and 70°C
0.052
D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.052
D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant wild-type enzyme, with NADP+
0.052
D-glucose 6-phosphate
-
native G6PD
0.0538
D-glucose 6-phosphate
-
clinical mutant G488V
0.0547
D-glucose 6-phosphate
-
refolded G6PD
0.056
D-glucose 6-phosphate
-
isoenzyme II
0.0578
D-glucose 6-phosphate
-
-
0.061
D-glucose 6-phosphate
-
isoenzyme I
0.063
D-glucose 6-phosphate
-
70°C, recombinant enzyme, with NADP+
0.067
D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant mutant R393G
0.069
D-glucose 6-phosphate
-
recombinant from E. coli
0.07
D-glucose 6-phosphate
-
pH 7.4, 37°C
0.07
D-glucose 6-phosphate
-
pH 8.0, temperature not specified in the publication
0.072
D-glucose 6-phosphate
-
-
0.073
D-glucose 6-phosphate
-
mutant enzyme A117S/F277I/Q324H/M381I/V443I/S470I, pH 7.5, 30°C
0.074
D-glucose 6-phosphate
mutant enzyme L80G, at pH 7.5 and 25°C
0.0745
D-glucose 6-phosphate
-
-
0.075
D-glucose 6-phosphate
-
pH 7.5
0.077
D-glucose 6-phosphate
-
pH 8.0, 37°C, native wild-type enzyme
0.077
D-glucose 6-phosphate
wild type enzyme, at pH 7.5 and 25°C
0.081
D-glucose 6-phosphate
-
mutant enzyme L99I/A117S/G225S/F277I/Q324H/M381I/V443I/S470I/A476V, pH 7.5, 30°C
0.083
D-glucose 6-phosphate
-
pH 8.0, 37°C, recombinant wild-type enzyme
0.083
D-glucose 6-phosphate
-
pH 8.0, 25, mutant 3
0.092
D-glucose 6-phosphate
-
-
0.099
D-glucose 6-phosphate
-
mutant enzyme A117S/Q324H/M381I/V443I/S470I, pH 7.5, 30°C
0.1
D-glucose 6-phosphate
-
25°C, pH 8.0, wild-type strain K-10
0.1073
D-glucose 6-phosphate
-
pH 7.6, 25°C
0.122
D-glucose 6-phosphate
-
pH 7.4, 37°C, with NADP+ or deamino-NADP+
0.138
D-glucose 6-phosphate
-
-
0.145
D-glucose 6-phosphate
-
25°C, pH 8.0, high-level glucose-6-phosphate dehydrogenase strain DF82
0.15
D-glucose 6-phosphate
-
pH 7.4, 80°C, recombinant enzyme
0.15
D-glucose 6-phosphate
-
pH 8.0, 25, mutant 1
0.151
D-glucose 6-phosphate
-
mutant enzyme A117S/Q324H/V443I/S470I, pH 7.5, 30°C
0.153
D-glucose 6-phosphate
-
-
0.167
D-glucose 6-phosphate
-
isoenzyme I
0.168
D-glucose 6-phosphate
mutant enzyme R408A, at pH 7.5 and 25°C
0.174
D-glucose 6-phosphate
-
25°C, pH 8.0, cofactor: NADP+
0.18
D-glucose 6-phosphate
-
isoenzyme II
0.19
D-glucose 6-phosphate
-
pH 8.0, 25°C, recombinant mutant R393H
0.2
D-glucose 6-phosphate
-
22°C, normal liver parenchyma
0.206
D-glucose 6-phosphate
-
pH 7.6, temperature not specified in the publication
0.21
D-glucose 6-phosphate
pH and temperature not specified in the publication
0.23
D-glucose 6-phosphate
-
-
0.24
D-glucose 6-phosphate
-
G6PDH activity extracted from source leaves of wild-type tobacco SNN cultivars
0.25
D-glucose 6-phosphate
-
G6PDH activity extracted from source leaves of wild-type tobacco Xanthi cultivars
0.286
D-glucose 6-phosphate
-
pH 8.0, 37°C, recombinant mutant P409R
0.44
D-glucose 6-phosphate
-
pH 8.0, 25°C
0.5
D-glucose 6-phosphate
-
pH 8.0, 25, wild-type enzyme
0.537
D-glucose 6-phosphate
mutant enzyme K83A, at pH 7.5 and 25°C
0.57
D-glucose 6-phosphate
-
0.618
D-glucose 6-phosphate
mutant enzyme K84A, at pH 7.5 and 25°C
0.78
D-glucose 6-phosphate
-
native enzyme, pH and temperature not specified in the publication
0.86
D-glucose 6-phosphate
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication
0.96
D-glucose 6-phosphate
-
25°C
1.25
D-glucose 6-phosphate
-
25°C, pH 8.0, cofactor: NAD+
1.9
D-glucose 6-phosphate
-
22°C, liver (pre)neoplastic lesions
44.4
D-glucose 6-phosphate
25°C, pH 8.0, mutant enzyme G163D
45.8
D-glucose 6-phosphate
25°C, pH 8.0, wild-type enzyme
50.7
D-glucose 6-phosphate
25°C, pH 8.0, mutant enzyme G163S
0.0156
deamino-NADP+
-
pH 8.0, 25°C, recombinant mutant R454C, with D-glucose 6-phosphate
2 - 3
deamino-NADP+
-
pH 7.4, 37°C, with D-glucose 6-phosphate
0.047
NAD+
-
-
2.477
NAD+
-
mutant enzyme K18A, at pH 8.2 and 25°C
5.09
NAD+
-
wild type enzyme, at pH 8.2 and 25°C
11.74
NAD+
-
mutant enzyme K18A/R50A, at pH 8.2 and 25°C
12
NAD+
-
pH 7.4, 80°C, recombinant enzyme
14.66
NAD+
-
mutant enzyme R50A, at pH 8.2 and 25°C
0.000012
NADP+
-
pH 8.0, 25°C
0.0003
NADP+
-
nephridic enzyme
0.001
NADP+
-
hepatic enzyme
0.0013
NADP+
-
25°C, pH 7.8
0.00238
NADP+
-
pH 8.0, 25°C, recombinant mutant R454H, with D-glucose 6-phosphate
0.00276
NADP+
-
pH 8.0, 25°C, recombinant mutant R454C, with D-glucose 6-phosphate
0.006 - 0.008
NADP+
-
isoenzymes I and II, with glucose 6-phosphate
0.006 - 0.008
NADP+
-
isoenzymes I and II, with glucose 6-phosphate
0.0066
NADP+
-
native enzyme, pH and temperature not specified in the publication
0.00694
NADP+
-
refolded G6PD
0.00707
NADP+
-
pH 8.0, 25°C, recombinant wild-type enzyme, with D-glucose 6-phosphate
0.00707
NADP+
-
native G6PD
0.0071
NADP+
-
pH 8.0, 25°C, recombinant wild-type enzyme
0.0072
NADP+
at pH 8.0 and 37°C
0.0075
NADP+
-
25°C, pH 8.0
0.0075
NADP+
-
wild type enzyme, at pH 8.2 and 25°C
0.00839
NADP+
-
pH 8.0, 25°C, recombinant mutant R454C, with deoxy-D-glucose 6-phosphate
0.0086
NADP+
-
pH 7.5, temperature not specified in the publication
0.0093
NADP+
-
pH 8.0, 25°C, recombinant mutant R393G
0.01
NADP+
-
pH 7.4, 37°C, with D-glucose 6-phosphate or 2-deoxy-D-glucose 6-phosphate
0.0107
NADP+
-
clinical mutant G488V
0.0118
NADP+
-
clinical mutant G488S
0.012
NADP+
-
recombinant from E. coli
0.0143
NADP+
-
wild-type enzyme, pH 7.5, 30°C
0.0147
NADP+
-
pH 7.4, 37°C
0.015
NADP+
-
pH 8.0, temperature not specified in the publication
0.015
NADP+
-
25°C, pH 8.0, high-level glucose-6-phosphate dehydrogenase strain DF82
0.015
NADP+
-
recombinant His-tagged enzyme, pH and temperature not specified in the publication
0.0159
NADP+
-
mutant enzyme L99I/A117S/G225S/F277I/Q324H/M381I/V443I/S470I/A476V, pH 7.5, 30°C
0.016
NADP+
wild type enzyme, at pH 7.5 and 25°C
0.016
NADP+
-
25°C, pH 8.0, wild-type strain K-10
0.0165
NADP+
-
pH 8.0, 25°C, recombinant mutant R393H
0.017
NADP+
-
0.0025 mM glucose 6-phosphate
0.017
NADP+
-
pH 8.0, 25°C
0.017
NADP+
mutant enzyme K84A, at pH 7.5 and 25°C
0.017
NADP+
mutant enzyme R408A, at pH 7.5 and 25°C
0.0199
NADP+
-
mutant enzyme A117S/F277I/Q324H/M381I/V443I/S470I, pH 7.5, 30°C
0.02
NADP+
-
with D-glucose 6-phosphate or D-galactose 6-phosphate
0.021
NADP+
mutant enzyme K83A, at pH 7.5 and 25°C
0.0225
NADP+
-
pH 7.6, temperature not specified in the publication
0.0225
NADP+
-
mutant enzyme A117S/Q324H/M381I/V443I/S470I, pH 7.5, 30°C
0.023
NADP+
-
pH 7.4, 37°C
0.024
NADP+
-
mutant enzyme A117S/Q324H/V443I/S470I, pH 7.5, 30°C
0.025
NADP+
-
isoenzyme II, with 6-phosphonogluconate 0.1 mM
0.03
NADP+
-
with 2-deoxyglucose 6-phosphate, KM decreases to 10 mM with increasing substrate concentration from 0.3 to 1.5 mM
0.03
NADP+
-
pH 7.4, 80°C, recombinant enzyme
0.041
NADP+
-
G6PDH activity extracted from source leaves of wild-type tobacco SNN cultivars
0.041
NADP+
-
G6PDH activity extracted from source leaves of wild-type tobacco Xanthi cultivars
0.0474
NADP+
pH and temperature not specified in the publication
0.059
NADP+
-
isoform G6PD1, at pH 8.0, temperature not specified in the publication
0.06
NADP+
-
isoform G6PD1, at pH 8.0, temperature not specified in the publication
0.07
NADP+
-
pH 8.0, 25, mutant enzyme 2
0.075
NADP+
mutant enzyme L80G, at pH 7.5 and 25°C
0.077
NADP+
-
pH 8.0, 25°C
0.08
NADP+
-
pH 7.8, 85°C, recombinant enzyme
0.081
NADP+
-
at pH 8.0 temperature not specified in the publication
0.085
NADP+
-
pH 8.0, 25, mutant enzyme 3
0.099
NADP+
-
mutant enzyme K18A, at pH 8.2 and 25°C
0.116
NADP+
-
pH 8.5, 30°C
0.13
NADP+
-
pH 8.0, 25, mutant enzyme 1
0.21
NADP+
-
pH 8.0, 25, wild-type enzyme
0.382
NADP+
-
mutant enzyme R50A, at pH 8.2 and 25°C
1.98
NADP+
-
purified enzyme, at pH 7.5 and 70°C
4.67
NADP+
25°C, pH 8.0, wild-type enzyme
4.8
NADP+
25°C, pH 8.0, mutant enzyme G163D
6.46
NADP+
25°C, pH 8.0, mutant enzyme G163S
17.7
NADP+
-
mutant enzyme K18A/R50A, at pH 8.2 and 25°C
0.014
NADPH
-
recombinant from E. coli
0.023
NADPH
-
isoenzyme II, with 6-phosphonogluconate 0.1 mM
additional information
additional information
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additional information
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Penicillium duponti
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-
-
additional information
additional information
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-
-
additional information
additional information
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kinetics
-
additional information
additional information
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kinetics and thermodynamics, rapid equilibrium random bi bi kinetic model
-
additional information
additional information
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Michaelis-Menten kinetics
-
additional information
additional information
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thermodynamics, steady-state kinetics
-
additional information
additional information
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kinetics, kinetic mechanism analysis, ternary-complex mechanism, overview
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additional information
additional information
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ping pong bi bi kinetic mechanism
-
additional information
additional information
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steady-state kinetics of wild-type and mutant enzymes
-
additional information
additional information
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steady-state kinetics of wild-type and mutant enzymes
-
additional information
additional information
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hyperbolic kinetics versus D-glucose 6-phosphate
-
additional information
additional information
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the initial velocity plots of the enzyme follow the Michaelis-Menten equation in the absence of NADH. In its presence, however, the velocity versus substrate plots for NADP+ become sigmoidal but remain hyperbolic for glucose 6-phosphate as the variable substrate. Inhibition against both of the substrates of the enzyme by NADH is noncompetitive. The inhibition curves for NADH are also sigmoidal, suggesting a multisite binding of the inhibitor on the enzyme surface
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K18A
-
the mutant with reduced catalytic efficiency shows 35fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold)
K18A/R50A
-
the mutant shows almost no activity
K18T
-
the mutant with reduced catalytic efficiency sshows 35fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold)
R50A
-
the mutant with reduced catalytic efficiency shows 50fold preference for NADP+ over NAD+ as compared to the wild type enzyme (386fold)
A44T
-
asymptomatic patient with high in vitro glucose-6-phosphate dehydrogenase deficiency, carrying a inherited mutation at A55T
G163D
mutant is markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values
G163S
mutant markedly less stable than wild-type G6PD in both thermostability and urea-induced inactivation tests. According to unfolding and refolding experiments, the mutant is impaired in its folding properties. KM-values and turnover numbers are similar to wild-type values
G488S
-
clinical mutant G6PDFukaya, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
G488V
-
clinical mutant G6PDCampinas, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
P409R
-
natural occurring point mutation, reconstructed by site-directed mutagenesis, the gene g6pd is highly polymorphic with over 130 mutations identified, reduced activity drastically altered kinetics, and altered tertiary structure, disturbing the binding of NADP+, compared to the wild-type enzyme, reduced thermal stbility
P489S
-
missense mutation associated with severe enzyme deficiency
R393E
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is slightly reduced compared to the activity of the wild-type enzyme
R393I
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is similar to the activity of the wild-type enzyme
R393L
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is similar to the activity of the wild-type enzyme
R393V
-
site-directed mutagenesis, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is reduced compared to the activity of the wild-type enzyme
R454C
-
site-directed mutagenesis, the mutant strain overexpresses the clinical enzyme mutants, i.e. Union clone, C1360T, the mutation abolishes a salt bridge between Arg454 and Asp 286, and leads to 10% decreased kcat and activity, Km values for both G6P and NADP+ are decreased approximately 5fold, the mutant shows decreased thermostability
R454H
-
site-directed mutagenesis, the mutant strain overexpresses the clinical enzyme mutants, i.e. Andalus clone, G1361A, the mutation abolishes a salt bridge between Arg454 and Asp 286, and leads to 10% decreased kcat and activity, Km values for both G6P and NADP+ are decreased approximately 5fold, the mutant shows decreased thermostability
K83A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
K84A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
L80G
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
R408A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
A117S/F277I/Q324H/M381I/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 95fold higher than the t1/2 value for the wild-type enzyme
A117S/Q324H/M381I/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 75fold higher than the t1/2 value for the wild-type enzyme
A117S/Q324H/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 13.5fold higher than the t1/2 value for the wild-type enzyme
L99I/A117S/G225S/F277I/Q324H/M381I/V443I/S470I/A476V
-
t1/2 for the mutant enzyme at 60°C is 124 fold higher than the t1/2 value for the wild-type enzyme. 3.4 °C increase in melting temperature (Tm), and a 5 °C increase in optimal temperature (Topt), without compromising the specific activity. The thermostable mutant is conducted to generate hydrogen from maltodextrin via in vitro synthetic biosystems, gaining a more than 8fold improvement of productivity rate with 76% of theoretical yield at 60°C
A117S/F277I/Q324H/M381I/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 95fold higher than the t1/2 value for the wild-type enzyme
-
A117S/Q324H/M381I/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 75fold higher than the t1/2 value for the wild-type enzyme
-
A117S/Q324H/V443I/S470I
-
t1/2 for the mutant enzyme at 60°C is 13.5fold higher than the t1/2 value for the wild-type enzyme
-
L99I/A117S/G225S/F277I/Q324H/M381I/V443I/S470I/A476V
-
t1/2 for the mutant enzyme at 60°C is 124 fold higher than the t1/2 value for the wild-type enzyme. 3.4 °C increase in melting temperature (Tm), and a 5 °C increase in optimal temperature (Topt), without compromising the specific activity. The thermostable mutant is conducted to generate hydrogen from maltodextrin via in vitro synthetic biosystems, gaining a more than 8fold improvement of productivity rate with 76% of theoretical yield at 60°C
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R393G
-
naturally occuring mutation corresponding to the clinical variants G6PD Wisconsin, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is similar to the activity of the wild-type enzyme
R393G
-
clinical mutant G6PDWisconsin, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays thermostability as the wild-type and low susceptibility to chymotrypsin digestion
R393H
-
naturally occuring mutation corresponding to the clinical variants G6PD Nashville, the mutation affects a residue in the dimer interface close to the structural NADP+ site, the mutant activity is reduced compared to the activity of the wild-type enzyme
R393H
-
clinical mutant G6PDNashville, mutation in the vicinity of the structural NADP+ site, elevated Kd values of the structural NADP+, is denatured by guanidinium hydrochloride and refolded by rapid dilution in the presence of L-Arg, NADP+ and dithiothreitol at 25°C, displays decreased thermostability and high susceptibility to chymotrypsin digestion as compared to the wild-type
additional information
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activities of the cytosolic isoforms G6PD5 and G6PD6 are reciprocally increased in single mutants with no increase of their respective transcript levels. Seeds of the double mutant but not of the single mutants have higher oil content and increased weight compared to those of the wild-type, with no alteration in the carbon to nitrogen ratio or fatty acid composition. Total G6PDH activity is reduced only in the double mutant
additional information
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G6PD mutations are thought to cause haemolytic anaemia by compromising enzyme stability, phenotypes
additional information
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study of functional complementation of the yeast deletion mutant strain zwf1 by human wild-type and mutant enzymes, construction of a human enzyme mutant library containing all possible single nucleotide missense mutations in the eight-residue glucose 6-phosphate binding peptide of the enzyme, all mutations of residues Asp200, His201, Lys205 lead to inactive enzymes, some mutations of residues Ile199, Leu203, Arg198, Tyr202, Gly204 result in active, some in inactive enzymes, overview
additional information
the kcat value of the mutant enzymes is markedly reduced, resulting in a 10 and 18fold reduction in catalytic efficiency for NADP+ catalysis for mutant G6PDViangchan and mutant G6PDViangchan+Mahidol, respectively
additional information
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the kcat value of the mutant enzymes is markedly reduced, resulting in a 10 and 18fold reduction in catalytic efficiency for NADP+ catalysis for mutant G6PDViangchan and mutant G6PDViangchan+Mahidol, respectively
additional information
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stable overexpression in WEHI7.2 murine thymic lymphoma cells models glucose deprivation and sensitizes lymphoma cells to dexamethasone-induced apoptosis, overview, G6PDH-overexpressing WEHI7.2 cells are more sensitive to oxidative stress and glucocorticoids
additional information
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construction of a genetically modified yeast using DNA recombination technique and the PGK1 promoter, optimization of pH, temperature, dissolved oxygen, and composition of the culture medium, to achieve a high enzyme production rate, growth through a batch fermentation process, overview
additional information
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construction of a genetically modified yeast using DNA recombination technique and the PGK1 promoter, optimization of pH, temperature, dissolved oxygen, and composition of the culture medium, to achieve a high enzyme production rate, growth through a batch fermentation process, overview
-
additional information
generation of a N-terminally truncated version of the enzyme glucose-6-phosphate dehydrogenase from Trypanosoma cruzi lacking the first 37 residues, mutant DELTA37N
additional information
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generation of a N-terminally truncated version of the enzyme glucose-6-phosphate dehydrogenase from Trypanosoma cruzi lacking the first 37 residues, mutant DELTA37N
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