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3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
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-
-
-
r
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+
3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
additional information
?
-
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
in the gluconeogenic direction the enzyme is specific for NADPH
-
-
r
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
in the gluconeogenic direction the enzyme is specific for NADPH
-
-
r
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+
3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+
3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+
3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
both NAD+ and NADP+ are utilized in the glycolytic direction
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
comparable activity with NADP+ and NAD+
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
both NAD+ and NADP+ are utilized in the glycolytic direction
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
comparable activity with NADP+ and NAD+
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
NADP+ is the preferred cofactor
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
both NAD+ and NADP+ are utilized in the glycolytic direction
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
comparable activity with NADP+ and NAD+
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
both NAD+ and NADP+ are utilized in the glycolytic direction
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
comparable activity with NADP+ and NAD+
-
-
r
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
r
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
r
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
-
r
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
r
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
r
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
-
r
-
?
additional information
?
-
the enzyme plays dual coenzyme specificity with NAD+ and NADP+
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-
additional information
?
-
glyceraldehyde-3-phosphate dehydrogenase from chloroplasts has a dual cofactor specificity and can use both NADPH and NADH
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-
additional information
?
-
-
glyceraldehyde-3-phosphate dehydrogenase from chloroplasts has a dual cofactor specificity and can use both NADPH and NADH
-
-
-
additional information
?
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highest activity in Bis-Tris buffer, lowest in imidazole-HCL, overview
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-
additional information
?
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highest activity in Bis-Tris buffer, lowest in imidazole-HCL, overview
-
-
-
additional information
?
-
highest activity in Bis-Tris buffer, lowest in imidazole-HCL, overview
-
-
-
additional information
?
-
highest activity in Bis-Tris buffer, lowest in imidazole-HCL, overview
-
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-
additional information
?
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-
high hydrolase activity with a variety of organic p-nitrophenyl esters
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?
additional information
?
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-
possible amphibolic role: anabolic in photosynthetic carbon assimilation and catabolic in carbohydrate degradative pathways
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+
3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
additional information
?
-
-
possible amphibolic role: anabolic in photosynthetic carbon assimilation and catabolic in carbohydrate degradative pathways
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
in the gluconeogenic direction the enzyme is specific for NADPH
-
-
r
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
in the gluconeogenic direction the enzyme is specific for NADPH
-
-
r
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+
3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+
3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+
3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
both NAD+ and NADP+ are utilized in the glycolytic direction
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
both NAD+ and NADP+ are utilized in the glycolytic direction
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
both NAD+ and NADP+ are utilized in the glycolytic direction
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
both NAD+ and NADP+ are utilized in the glycolytic direction
-
-
r
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
the enzyme GapDH interacts with the intrinsically disordered protein CP12, when oxidized but not when reduced, in chloroplasts forming a stable complex. In this bienzyme complex, the activity of ADK3 is unchanged while the NADPH-dependent activity of GAPDH is significantly inhibited. The ADK3-GAPDH bienzyme complex is unable to recruit phosphoribulokinase (PRK), in contrast with the ternary complex formed between GAPDH-CP12 and PRK. The interaction between ADK3 and GAPDH might be a mechanism to regulate the crucial ATP: NADPH ratio within chloroplasts to optimize the Calvin-Benson cycle during rapid fluctuation in environmental resources
physiological function
glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NAD(P)H are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
physiological function
the enzyme plays a key role in glycolysis. GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate
physiological function
in Chlamydomonas reinhardtii, the chloroplast GAPDH is a homotetrameric A4-isoform that lacks regulatory cysteine residues found in the B subunit of the heterotetrameric A2B2-GAPDH isoform. Whereas A2B2-GAPDHs from higher plants are autonomously regulated, CP12 is required to confer redox regulation to the algal A4-GAPDH. In contrast, the CP12-like tail bearing two cysteine residues present on ADK3 is not involved in its redoxregulation
physiological function
phosphorylating glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a ubiquitous cellular enzyme that has a defined role in glycolysis and other pathways where it catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. The enzyme complexes with ADP and might be moonlighting
physiological function
-
glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NAD(P)H are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
-
physiological function
-
the enzyme plays a key role in glycolysis. GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate
-
physiological function
-
glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes an inevitable step in the central metabolism of most industrially important sugars such as glucose, fructose and sucrose. During the glycolysis of 1 mol glucose and 2 mol of NAD(P)H are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
-
additional information
ADK3, like CP12, can protect GAPDH against thermal inactivation and aggregation. CP12 acts as a chaperone for GAPDH. Detection o f a solubilizing effect of ADK3 on GAPDH
additional information
-
ADK3, like CP12, can protect GAPDH against thermal inactivation and aggregation. CP12 acts as a chaperone for GAPDH. Detection o f a solubilizing effect of ADK3 on GAPDH
additional information
comparison of Gapdh protein from Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, homology modeling, overview. The Gapdh from Thermoanaerobacterium saccharolyticum is less sensitive to ethanol and the NAD+/NADH ratio. Recombinant Gapdh from Thermoanaerobacterium saccharolyticum expressed in Clostridium thermocellum cells can improve the growth rate and ethanol resistance
additional information
-
comparison of Gapdh protein from Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, homology modeling, overview. The Gapdh from Thermoanaerobacterium saccharolyticum is less sensitive to ethanol and the NAD+/NADH ratio. Recombinant Gapdh from Thermoanaerobacterium saccharolyticum expressed in Clostridium thermocellum cells can improve the growth rate and ethanol resistance
-
additional information
-
comparison of Gapdh protein from Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, homology modeling, overview. The Gapdh from Thermoanaerobacterium saccharolyticum is less sensitive to ethanol and the NAD+/NADH ratio. Recombinant Gapdh from Thermoanaerobacterium saccharolyticum expressed in Clostridium thermocellum cells can improve the growth rate and ethanol resistance
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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D35G
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+
D35G/L36R/P192S
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
D35G/L36T/T37K
site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme
D35G/L36T/T37K/P192S
site-directed mutagenesis, the mutant shows high catalytic efficiency with NADP+ while the catalytic efficiency with NAD+ also increases. The replacement of Pro192 to Ser benefits the binding affinity of both NAD+ and NADP+
L36T
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+
D35G
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+
-
D35G/L36R/P192S
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
-
D35G/L36T/T37K
-
site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme
-
L36T
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+
-
D35G
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+
-
D35G/L36R/P192S
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
-
D35G/L36T/T37K
-
site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme
-
L36T
-
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+
-
C150S
-
the mutant is unable to turn over D-glyceraldehyde 3-phosphate in the presence of either NAD+ or NADP+
C150S
-
the mutant is unable to turn over D-glyceraldehyde 3-phosphate in the presence of either NAD+ or NADP+
-
additional information
the coenzyme specificity of GAPDH, EC 1.2.1.12, of Corynebacterium glutamicum is systematically manipulated by rational protein design and the effect of the manipulation for cellular metabolism and lysine production is evaluated. By a combinatorial modification of four key residues within the coenzyme binding sites, different GAPDH mutants with varied coenzyme specificity are constructed. While increasing the catalytic efficiency of GAPDH towards NADP+ enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (about 60%) is achieved with the mutant showing similar preference towards both NAD+ and NADP+, EC 1.2.1.59
additional information
-
the coenzyme specificity of GAPDH, EC 1.2.1.12, of Corynebacterium glutamicum is systematically manipulated by rational protein design and the effect of the manipulation for cellular metabolism and lysine production is evaluated. By a combinatorial modification of four key residues within the coenzyme binding sites, different GAPDH mutants with varied coenzyme specificity are constructed. While increasing the catalytic efficiency of GAPDH towards NADP+ enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (about 60%) is achieved with the mutant showing similar preference towards both NAD+ and NADP+, EC 1.2.1.59
additional information
-
the coenzyme specificity of GAPDH, EC 1.2.1.12, of Corynebacterium glutamicum is systematically manipulated by rational protein design and the effect of the manipulation for cellular metabolism and lysine production is evaluated. By a combinatorial modification of four key residues within the coenzyme binding sites, different GAPDH mutants with varied coenzyme specificity are constructed. While increasing the catalytic efficiency of GAPDH towards NADP+ enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (about 60%) is achieved with the mutant showing similar preference towards both NAD+ and NADP+, EC 1.2.1.59
-
additional information
-
the coenzyme specificity of GAPDH, EC 1.2.1.12, of Corynebacterium glutamicum is systematically manipulated by rational protein design and the effect of the manipulation for cellular metabolism and lysine production is evaluated. By a combinatorial modification of four key residues within the coenzyme binding sites, different GAPDH mutants with varied coenzyme specificity are constructed. While increasing the catalytic efficiency of GAPDH towards NADP+ enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (about 60%) is achieved with the mutant showing similar preference towards both NAD+ and NADP+, EC 1.2.1.59
-
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Anabaena cylindrica, Anabaena sp., Trichormus variabilis, Anabaena sp. 7119
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Arabidopsis thaliana (Q71V79), Arabidopsis thaliana
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Expression, purification, crystallization and preliminary X-ray analysis of wild-type and of an active-site mutant of glyceraldehyde-3-phosphate dehydrogenase from Campylobacter jejuni
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Campylobacter jejuni, Campylobacter jejuni NCTC 11168
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Comparative analysis of two glyceraldehyde-3-phosphate dehydrogenases from a thermoacidophilic archaeon, Sulfolobus tokodaii
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586
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Sulfurisphaera tokodaii (Q971K2), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q971K2)
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Kim, S.; Lee, C.H.; Nam, S.W.; Kim, P.
Alteration of reducing powers in an isogenic phosphoglucose isomerase (pgi)-disrupted Escherichia coli expressing NAD(P)-dependent malic enzymes and NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
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Bacillus subtilis (O34425), Bacillus subtilis, Bacillus subtilis 168 (O34425)
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Malay, A.D.; Bessho, Y.; Ellis, M.J.; Antonyuk, S.V.; Strange, R.W.; Hasnain, S.S.; Shinkai, A.; Padmanabhan, B.; Yokoyama, S.
Structure of glyceraldehyde-3-phosphate dehydrogenase from the archaeal hyperthermophile Methanocaldococcus jannaschii
Acta Crystallogr. Sect. F
65
1227-1233
2009
Methanocaldococcus jannaschii (Q58546), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58546)
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Ayres, C.A.; Schormann, N.; Senkovich, O.; Fry, A.; Banerjee, S.; Ulett, G.C.; Chattopadhyay, D.
Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface
Acta Crystallogr. Sect. F
70
1333-1339
2014
Streptococcus agalactiae (Q8E3E8), Streptococcus agalactiae, Streptococcus agalactiae NEM316 (Q8E3E8)
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Jiang, L.; Zhang, Y.; Li, Z.; Liu, J.
Metabolic engineering of Corynebacterium glutamicum for increasing the production of L-ornithine by increasing NADPH availability
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Clostridium acetobutylicum (O52631), Clostridium acetobutylicum
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Bommareddy, R.R.; Chen, Z.; Rappert, S.; Zeng, A.P.
A de novo NADPH generation pathway for improving lysine production of Corynebacterium glutamicum by rational design of the coenzyme specificity of glyceraldehyde 3-phosphate dehydrogenase
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Corynebacterium glutamicum (Q01651), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC13032 (Q01651)
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Gluconeogenesis from pyruvate in the hyperthermophilic archaeon Pyrococcus furiosus involvement of reactions of the Embden-Meyerhof pathway
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354-363
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Pyrococcus furiosus (P61879)
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Tian, L.; Perot, S.; Stevenson, D.; Jacobson, T.; Lanahan, A.; Amador-Noguez, D.; Olson, D.; Lynd, L.
Metabolome analysis reveals a role for glyceraldehyde 3-phosphate dehydrogenase in the inhibition of C. thermocellum by ethanol
Biotechnol. Biofuels
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Thermoanaerobacterium saccharolyticum (I3VY89), Thermoanaerobacterium saccharolyticum DSM 8691 (I3VY89), Thermoanaerobacterium saccharolyticum JW/SL-YS485 (I3VY89)
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Aziz, I.; Rashid, N.; Ashraf, R.; Siddiqui, M.; Imanaka, T.; Akhtar, M.
Pcal_0632, a phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Pyrobaculum calidifontis
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22
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2018
Pyrobaculum calidifontis (A3MTU1), Pyrobaculum calidifontis, Pyrobaculum calidifontis JCM 11548 (A3MTU1), Pyrobaculum calidifontis VA1 (A3MTU1)
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Interaction between adenylate kinase 3 and glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii
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Chlamydomonas reinhardtii (P50362), Chlamydomonas reinhardtii
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Ayna, A.; Moody, P.
Crystal structures of a dual coenzyme specific glyceraldehyde-3-phosphate dehydrogenase from the enteric pathogen Campylobacter jejuni
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Campylobacter jejuni (A0A1E7PFR0)
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