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3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
acetaldehyde + phosphate + NAD+
acetyl phosphate + NADH
arsenate + GSH + NAD+ + glyceraldehyde 3-phosphate
arsenite + ?
butyraldehyde + phosphate + NAD+
butyryl phosphate + NADH
-
enzyme form E6.6 shows 10% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E6.8 shows 15% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 12% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.9% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine hypoxanthine nucleotide + phosphate
3-phospho-D-glyceroyl phosphate + ?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + ?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arseno-3-phosphoglycerate + NADH + H+
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH + H+
D-glyceraldehyde 3-phosphate + C8-(4-(2,2,6,6-tetramethyl-piperidinyl-l-oxyl)-amino)-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + C8-(4-(2,2,6,6-tetramethyl-piperidinyl-l-oxyl)-amino)-NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + N6-(2-carboxyethyl)-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + N6-(2-carboxyethyl)-NADH
D-glyceraldehyde 3-phosphate + N6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + N6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl)-NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NAD+
D-3-phosphoglycerate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
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 + poly(ethylene glycol)-bound NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + poly(ethylene glycol)-bound NADH
D-glyceraldehyde 3-phosphate + thio-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + thio-NADH
DL-glyceraldehyde + phosphate + NAD+
D-glyceroyl phosphate + NADH
-
enzyme form E6.6 shows no activity, enzyme form E6.8 shows 2.5% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 30% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 3.0% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
erythrose 4-phosphate + phosphate + NAD+
? + NADH
-
enzyme form E6.6 shows no activity, enzyme form E6.8 shows 1.2% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 25% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 1.5% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
glucose + phosphate + NAD+
? + NADH
-
enzyme form E6.6 shows no activity, enzyme form E6.8 shows 0.6% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 6.0% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.8% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
glyceraldehyde 3-phosphate + NAD+
? + NADH
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
propionaldehyde + phosphate + NAD+
propionyl phosphate + NADH
-
enzyme form E6.6 shows 33% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E6.8 shows 12% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 10% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.8% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
valeraldehyde + phosphate + NAD+
pentanoyl phosphate + NADH
-
enzyme form E6.6 shows no activity, enzyme form E6.8 shows 19% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 18% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.9% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
additional information
?
-
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
enzyme plays a central role in glyconeogenesis
-
-
?
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
Q81X74, YP_027084
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
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+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
?
acetaldehyde + phosphate + NAD+
acetyl phosphate + NADH
-
enzyme form E6.6 shows 27% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E6.8 shows 9% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 6% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.4% of the activity with D-glyceraldehyde 3-phosphate
-
-
?
acetaldehyde + phosphate + NAD+
acetyl phosphate + NADH
-
-
-
-
?
acetaldehyde + phosphate + NAD+
acetyl phosphate + NADH
-
-
-
-
?
arsenate + GSH + NAD+ + glyceraldehyde 3-phosphate
arsenite + ?
-
-
-
-
?
arsenate + GSH + NAD+ + glyceraldehyde 3-phosphate
arsenite + ?
-
-
-
-
?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine hypoxanthine nucleotide + phosphate
3-phospho-D-glyceroyl phosphate + ?
-
1.3% of the activity with NAD+
-
-
?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine hypoxanthine nucleotide + phosphate
3-phospho-D-glyceroyl phosphate + ?
-
3.2% of activity with NAD+
-
-
?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + ?
-
2.8% of the activity with NAD+
-
-
?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + ?
-
4.5% of activity with NAD+
-
-
?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + ?
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arseno-3-phosphoglycerate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + arsenate + NAD+
1-arseno-3-phosphoglycerate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
the product arseno-3-phosphoglycerate is decomposed readily to 3-phosphoglycerate
-
-
ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH + H+
-
strictly NAD+-dependent enzyme. The maximal velocity for the reaction with arsenate instead of phosphate is about 10 times higher. The maximal reaction velocity is higher with arsenate because the degradation of the instable product phospho-arseno glyceric acid pushes the reaction into the direction of phospho-arseno glyceric acid formation
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH + H+
-
strictly NAD+-dependent enzyme. The maximal velocity for the reaction with arsenate instead of phosphate is about 10 times higher. The maximal reaction velocity is higher with arsenate because the degradation of the instable product phospho-arseno glyceric acid pushes the reaction into the direction of phospho-arseno glyceric acid formation
-
-
?
D-glyceraldehyde 3-phosphate + N6-(2-carboxyethyl)-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + N6-(2-carboxyethyl)-NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + N6-(2-carboxyethyl)-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + N6-(2-carboxyethyl)-NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + N6-(2-carboxyethyl)-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + N6-(2-carboxyethyl)-NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
enzyme plays a central role in glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
glycolytic enzyme
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
Hippoglossus sp.
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
glycolytic enzyme
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
absolute specificity for NAD+
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
hydride transfer is a major rate-limiting step
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
enzyme is involved in cytosolic glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
Psithyrus suckleyi
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
Psithyrus suckleyi
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
GAPDH I is responsible for glycolysis when koningic acid is produced
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
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+
-
activity of the enzyme is confirmed by proteome analysis and enzyme assays with cell extract glycerol-grown cells
-
-
?
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+
-
-
-
?
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+
Q81X74, YP_027084
-
-
-
?
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+
-
-
-
?
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+
substrate binding structure analysis, overview
-
-
?
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+
-
activity assay
-
-
?
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+
-
strictly NAD+-dependent enzyme
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
strictly NAD+-dependent enzyme
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
671070, 673629, 684120, 684972, 685025, 685292, 686080, 688250, 688661, 725592, 742751 -
-
?
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+
-
-
-
r
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+
-
-
-
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+
-
-
-
-
r
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+
-
-
-
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+
-
-
-
-
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+
-
-
-
r
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+
-
-
-
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+
-
-
-
r
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+
-
-
-
r
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+
-
-
-
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+
-
-
-
?
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+
-
-
-
?
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+
the enzyme utilizes either NAD+ or NADP+ as coenzyme but its affinity for the latter is about 50fold higher
-
-
?
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+
-
-
-
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+
-
-
-
-
?
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+
-
-
-
-
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+
-
-
-
?
D-glyceraldehyde 3-phosphate + poly(ethylene glycol)-bound NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + poly(ethylene glycol)-bound NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + poly(ethylene glycol)-bound NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + poly(ethylene glycol)-bound NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + poly(ethylene glycol)-bound NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + poly(ethylene glycol)-bound NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + thio-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + thio-NADH
-
7.2% of the activity with NAD+
-
-
?
D-glyceraldehyde 3-phosphate + thio-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + thio-NADH
-
9.3% of activity with NAD+
-
-
?
D-glyceraldehyde 3-phosphate + thio-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + thio-NADH
-
thionicotinamide adenine dinucleotide is not as effective as NAD+
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
-
-
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
-
-
-
-
?
glyceraldehyde 3-phosphate + NAD+
? + NADH
-
-
-
-
?
glyceraldehyde 3-phosphate + NAD+
? + NADH
-
-
-
-
?
additional information
?
-
-
enzymatic activity strictly depends on residue Cys149. Catalytic Cys149 is the only solvent-exposed cysteine of the protein and its thiol is relatively acidic, pKa =5.7
-
-
?
additional information
?
-
enzymatic activity strictly depends on residue Cys149. Catalytic Cys149 is the only solvent-exposed cysteine of the protein and its thiol is relatively acidic, pKa =5.7
-
-
?
additional information
?
-
-
the overproducing transformant grows faster and more efficient than the wild-type strain
-
-
?
additional information
?
-
-
wild-type enzyme has no activity with NADP+, the mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+
-
-
?
additional information
?
-
-
the enzyme is a GABA(A) receptor kinase linking glycolysis to neuronal inhibition
-
-
?
additional information
?
-
-
activity of isoenzyme 2 increases during postembryonic development
-
-
?
additional information
?
-
substrate and cofactor binding analysis and kinetics, overview
-
-
-
additional information
?
-
-
substrate and cofactor binding analysis and kinetics, overview
-
-
-
additional information
?
-
-
mutant enzyme C149selenocysteine shows selenoperoxidase activity with tert-butyl hydroperoxide and 3-carboxy 4-nitrobenzenethiol. Wild-type enzyme has no peroxidase activity
-
-
?
additional information
?
-
-
mutant enzyme L187A/P188S is catalytically active not only with NAD+, as the wild-type enzyme, but also with NADP+
-
-
?
additional information
?
-
-
enzyme is regulated by ATP and by D-glyceraldehyde 3-phosphate
-
-
?
additional information
?
-
-
classical glycolytic protein involved exclusively in cytosolic energy production
-
-
?
additional information
?
-
-
hypoxia upregulates the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase in endothelial cells through a 5'-hypoxic regulatory element. Cell-specific patterns of HIF-1alpha and HIF-2alpha expression lead to cell-specific gene upregulation during hypoxia
-
-
?
additional information
?
-
GAPDH interacts with DNA damages, such as uracil
-
-
?
additional information
?
-
the enzyme interacts directly with the D-serine synthetic enzyme serine racemase, SRR. Glyceraldehyde-3-phosphate (G3P) augments the SRR-GAPDH interaction in a dose-dependent manner, whereas NAD+ and its reduced form, NADH, inhibit the interaction
-
-
?
additional information
?
-
-
GAPDH directly binds to cyclic adenosine diphosphoribose (cADPR), molecule docking and molecular dynamic simulations, overview. Arg234 and His179 in GAPDH might be the potential binding sites for cADPR
-
-
?
additional information
?
-
interaction analysis of the purified enzyme with oligodeoxyribonucleotides, poly(dA-dU) and poly(dA-dT) substrate synthesis, overview. GAPDH, like DNA glycosylases/AP lyases, is able to cleave DNA and to remain bound with the 5'-terminal product of beta-elimination via the Schiff base-dependent bonding. But unlike DNA glycosylases/AP lyases, GAPDH forms considerably more stable complexes with the product of beta-elimination that potentially can make it inefficient as an AP lyase. Lack of the UDG activity in classical GAPDH. Disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA
-
-
?
additional information
?
-
-
binds plasminogen
-
-
?
additional information
?
-
-
binds plasminogen
-
-
?
additional information
?
-
-
GAPDH is a Ca2+-dependent substrate of phosphorylase kinase although the rate of phosphorylation is very slow
-
-
?
additional information
?
-
-
no activity with NADP+
-
-
?
additional information
?
-
-
no activity with NADP+
-
-
?
additional information
?
-
enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer
-
-
-
additional information
?
-
-
enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer
-
-
-
additional information
?
-
enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer
-
-
-
additional information
?
-
enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer
-
-
-
additional information
?
-
enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer
-
-
-
additional information
?
-
enzyme CbbG shows about 6fold higher Km value for 1,3-bisphospho-D-glycerate(1,3bicPGA) but about 5fold higher kcat for the oxidation of D-glyceraldehyde 3-phosphate (Ga3P). CbbG is a Ga3PDHase specific for D-Ga3P and NAD+. NADP+ or NADPH are not used as cofactors, and the enzyme exhibits 11fold lower Km value and two orders of magnitude lower kcat when L-Ga3P is used instead of the D-isomer
-
-
-
additional information
?
-
-
oxidation of GAPDH could be the signal for binding with nucleic acids and for change of quarternary structure. Theses events could facilitate GAPDH functioning in DNA reparation and tRNA transportation during oxidative stress
-
-
?
additional information
?
-
-
oxidation of SH-groups of the active site of GAPDH enhances its binding with total transfer RNA or with total DNA. Both NAD+ and NADH inhibit GAPDH-RNA or GAPDH-DNA interaction
-
-
?
additional information
?
-
GAPDH interacts with DNA damages, such as uracil
-
-
?
additional information
?
-
no activity with NADP+
-
-
?
additional information
?
-
interaction of recombinant PfGapdh with Pfeno, human plasminogen, lysozyme and alpha-tubulin
-
-
?
additional information
?
-
-
interaction of recombinant PfGapdh with Pfeno, human plasminogen, lysozyme and alpha-tubulin
-
-
?
additional information
?
-
-
importance of the enzyme in glucose catabolism. Activity is reduced severalfold after growth on gluconeogenic substrates such as citrate compared to growth on glucose
-
-
?
additional information
?
-
-
plays a role in microtubule dynamics in the early secretory pathway
-
-
?
additional information
?
-
-
the isoproteins TLAb-a and TLAb-2 change depending on the cell growth phase, the carbon source and sodium chloride shock
-
-
?
additional information
?
-
-
high-affinity binding of cAMP to D-glyceraldehyde 3-phosphate dehydrogenase may significantly reduce intracellular cAMP
-
-
?
additional information
?
-
-
NADH-reductive stress in Saccharomyces cerevisiae induces the expression of the minor isoform of glyceraldehyde-3-phosphate dehydrogenase, TDH1
-
-
?
additional information
?
-
-
Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase shows high affinity for tonB-dependent receptor protein RagA4, arginine-specific proteinase B, 4-hydroxybutyryl-coenzyme A dehydratase, glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent glutamate dehydrogenase, and malate dehydrogenase from Porphyromonas gingivalis which function as regulators in biofilm formation with oral streptococci
-
-
?
additional information
?
-
Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase shows high affinity for tonB-dependent receptor protein RagA4, arginine-specific proteinase B, 4-hydroxybutyryl-coenzyme A dehydratase, glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent glutamate dehydrogenase, and malate dehydrogenase from Porphyromonas gingivalis which function as regulators in biofilm formation with oral streptococci
-
-
?
additional information
?
-
-
Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase shows high affinity for tonB-dependent receptor protein RagA4, arginine-specific proteinase B, 4-hydroxybutyryl-coenzyme A dehydratase, glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent glutamate dehydrogenase, and malate dehydrogenase from Porphyromonas gingivalis which function as regulators in biofilm formation with oral streptococci
-
-
?
additional information
?
-
the concerted action of both alpha-enolase and GAPDH on the bacterial cell surface might result in an enhancement of the pathogens ability to degrade the extracellular matrix and to invade host tissues
-
-
?
additional information
?
-
-
the concerted action of both alpha-enolase and GAPDH on the bacterial cell surface might result in an enhancement of the pathogens ability to degrade the extracellular matrix and to invade host tissues
-
-
?
additional information
?
-
the enzyme has a specific plasmin- and plasminogen-binding activity, high affinity for plasmin and significantly lower affinity for plasminogen
-
-
?
additional information
?
-
-
the enzyme has a specific plasmin- and plasminogen-binding activity, high affinity for plasmin and significantly lower affinity for plasminogen
-
-
?
additional information
?
-
the enzyme binds hemoglobin and heme, it is a heme-binding protein
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
enzyme plays a central role in glyconeogenesis
-
-
?
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
additional information
?
-
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+
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
enzyme plays a central role in glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
glycolytic enzyme
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
glycolytic enzyme
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
enzyme is involved in cytosolic glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
GAPDH I is responsible for glycolysis when koningic acid is produced
-
-
?
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+
-
-
-
-
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+
Q81X74, YP_027084
-
-
-
?
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+
-
-
-
?
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+
-
activity assay
-
-
?
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+
-
-
-
-
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+
-
-
-
r
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+
-
-
-
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+
-
-
-
-
r
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+
-
-
-
-
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+
-
-
-
r
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+
-
-
-
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+
-
-
-
r
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+
-
-
-
r
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+
-
-
-
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+
-
-
-
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+
-
-
-
?
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+
-
-
-
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+
-
-
-
?
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+
-
-
-
?
additional information
?
-
-
the overproducing transformant grows faster and more efficient than the wild-type strain
-
-
?
additional information
?
-
-
the enzyme is a GABA(A) receptor kinase linking glycolysis to neuronal inhibition
-
-
?
additional information
?
-
-
activity of isoenzyme 2 increases during postembryonic development
-
-
?
additional information
?
-
-
enzyme is regulated by ATP and by D-glyceraldehyde 3-phosphate
-
-
?
additional information
?
-
-
classical glycolytic protein involved exclusively in cytosolic energy production
-
-
?
additional information
?
-
-
hypoxia upregulates the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase in endothelial cells through a 5'-hypoxic regulatory element. Cell-specific patterns of HIF-1alpha and HIF-2alpha expression lead to cell-specific gene upregulation during hypoxia
-
-
?
additional information
?
-
GAPDH interacts with DNA damages, such as uracil
-
-
?
additional information
?
-
the enzyme interacts directly with the D-serine synthetic enzyme serine racemase, SRR. Glyceraldehyde-3-phosphate (G3P) augments the SRR-GAPDH interaction in a dose-dependent manner, whereas NAD+ and its reduced form, NADH, inhibit the interaction
-
-
?
additional information
?
-
-
oxidation of GAPDH could be the signal for binding with nucleic acids and for change of quarternary structure. Theses events could facilitate GAPDH functioning in DNA reparation and tRNA transportation during oxidative stress
-
-
?
additional information
?
-
GAPDH interacts with DNA damages, such as uracil
-
-
?
additional information
?
-
no activity with NADP+
-
-
?
additional information
?
-
interaction of recombinant PfGapdh with Pfeno, human plasminogen, lysozyme and alpha-tubulin
-
-
?
additional information
?
-
-
interaction of recombinant PfGapdh with Pfeno, human plasminogen, lysozyme and alpha-tubulin
-
-
?
additional information
?
-
-
importance of the enzyme in glucose catabolism. Activity is reduced severalfold after growth on gluconeogenic substrates such as citrate compared to growth on glucose
-
-
?
additional information
?
-
-
plays a role in microtubule dynamics in the early secretory pathway
-
-
?
additional information
?
-
-
the isoproteins TLAb-a and TLAb-2 change depending on the cell growth phase, the carbon source and sodium chloride shock
-
-
?
additional information
?
-
-
high-affinity binding of cAMP to D-glyceraldehyde 3-phosphate dehydrogenase may significantly reduce intracellular cAMP
-
-
?
additional information
?
-
-
NADH-reductive stress in Saccharomyces cerevisiae induces the expression of the minor isoform of glyceraldehyde-3-phosphate dehydrogenase, TDH1
-
-
?
additional information
?
-
-
Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase shows high affinity for tonB-dependent receptor protein RagA4, arginine-specific proteinase B, 4-hydroxybutyryl-coenzyme A dehydratase, glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent glutamate dehydrogenase, and malate dehydrogenase from Porphyromonas gingivalis which function as regulators in biofilm formation with oral streptococci
-
-
?
additional information
?
-
Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase shows high affinity for tonB-dependent receptor protein RagA4, arginine-specific proteinase B, 4-hydroxybutyryl-coenzyme A dehydratase, glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent glutamate dehydrogenase, and malate dehydrogenase from Porphyromonas gingivalis which function as regulators in biofilm formation with oral streptococci
-
-
?
additional information
?
-
-
Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase shows high affinity for tonB-dependent receptor protein RagA4, arginine-specific proteinase B, 4-hydroxybutyryl-coenzyme A dehydratase, glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent glutamate dehydrogenase, and malate dehydrogenase from Porphyromonas gingivalis which function as regulators in biofilm formation with oral streptococci
-
-
?
additional information
?
-
the concerted action of both alpha-enolase and GAPDH on the bacterial cell surface might result in an enhancement of the pathogens ability to degrade the extracellular matrix and to invade host tissues
-
-
?
additional information
?
-
-
the concerted action of both alpha-enolase and GAPDH on the bacterial cell surface might result in an enhancement of the pathogens ability to degrade the extracellular matrix and to invade host tissues
-
-
?
additional information
?
-
the enzyme binds hemoglobin and heme, it is a heme-binding protein
-
-
?
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(3-[(4-nitrophenoxy)carbonyl]but-3-en-1-yl)phosphonic acid
-
(8E,11E)-C15:2-anacardic acid
-
(8E,11E,14E)-C15:3-anacardic acid
-
(E)-2-hydroxy-6-(pentadec-8-en-1-yl)benzoic acid
-
(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide
-
treatment with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide between 0.001 and 1 mM induces the oligomerization of GAPDH, dithiothreitol reduces (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide-induced aggregation in a concentration-dependent manner
1-hydroxy-2-oxo-3,3-bis(2-aminoethyl)-1-triazene
2'-deoxy-2'-[(quinolin-7-ylcarbonyl)amino]adenosine
-
2-(6-amino-2-methyl-9H-purin-9-yl)-5-(hydroxymethyl)tetrahydrofuran-3,4-diol
-
2-(dodec-1-en-1-yl)-6-hydroxybenzoic acid
-
inhibition is not reversed or prevented by addition of Triton X-100. Noncompetitive with respect to both substrate and cofactor
2-(hydroxymethyl)-5-[6-[(2-methylphenyl)amino]-9H-purin-9-yl]tetrahydrofuran-3,4-diol
-
2-(hydroxymethyl)-5-[6-[(3-methylbutyl)amino]-9H-purin-9-yl]tetrahydrofuran-3,4-diol
-
2-(hydroxymethyl)-5-[6-[(3-methylphenyl)amino]-9H-purin-9-yl]tetrahydrofuran-3,4-diol
-
2-methyl-9H-purin-6-amine
-
2-pentadecyl-6-hydroxybenzoic acid
-
inhibition is not reversed or prevented by addition of Triton X-100. Noncompetitive with respect to both substrate and cofactor
2-[6-amino-8-(pyrimidin-2-ylsulfanyl)-9H-purin-9-yl]-5-(hydroxymethyl)tetrahydrofuran-3,4-diol
-
2-[9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-yl]-2,3-dihydroisoquinoline
-
3',4',5',5,7-pentamethoxyflavone
-
3',4'-methylenedioxy-5,6,7-trimethoxyflavone
-
3-(1,3-benzodioxol-5-yl)-2-oxo-2H-chromen-6-ylacetate
-
3-(1,3-benzodioxol-5-yl)-2-oxo-2H-chromen-7-ylacetate
-
3-(1,3-benzodioxol-5-yl)-2-oxo-2H-chromen-8-ylacetate
-
3-(1,3-benzodioxol-5-yl)-2H-chromen-2-one
-
3-(1,3-benzodioxol-5-yl)-6-hydroxy-2H-chromen-2-one
-
3-(1,3-benzodioxol-5-yl)-6-nitro-2H-chromen-2-one
-
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-1H-indol-3-ylmethylene]amino]-2H-chromen-2-one
-
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-1H-pyrrol-2-ylmethylene]amino]-2H-chromen-2-one
-
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-2-furylmethylene]amino]-2H-chromen-2-one
-
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-pyridin-2-ylmethylene]amino]-2H-chromen-2-one
-
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-thien-2-ylmethylene]amino]-2H-chromen-2-one
-
3-(1,3-benzodioxol-5-yl)-7-hydroxy-2H-chromen-2-one
-
3-(1,3-benzodioxol-5-yl)-8-hydroxy-2H-chromen-2-one
-
3-(chloroacetyl)-pyridine adenine dinculeotide
-
-
3-(p-nitrophenoxycarboxyl)-3-ethylene propyl dihydroxyphosphinate
propyl dihydroxyphosphonate analogue of substrate glyceraldehyde 3-phosphate. The energy profiles correspond to the nucleophilic attack of Cys166 on the atom C1 of the carbonyl group of the inhibitor. The barrier for the inhibition reaction is lower than that observed for a natural substrate
3-morpholino-sydnonimine
-
the NO-generating compound inactivates by induction of a covalent binding of NAD+ to the enzyme. The superoxide anion released by 3-morpholino-sydnonimine potentiates the inactivation
3-phospho-D-glyceroyl phosphate
-
-
4-chloromercuribenzoate
complete inhibition at 10 mM
4-hydroxymercuribenzoate
complete inhibition at 10 mM
5'-deoxy-5'-[(diphenylacetyl)amino]adenosine
-
5'-deoxy-5'-[[(4'-ethylbiphenyl-4-yl)carbonyl]amino]adenosine
-
6-amino-3-(1,3-benzodioxol-5-yl)-2H-chromen-2-one
-
9-(2-aminoethyl)-8-thiophen-2-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-2-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dihydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-2-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(2-hydroxy-3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3,4-dihydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3,5-dihydroxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(2-methylphenyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3-methylphenyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-phenyl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-[(3-methoxynaphthalen-1-yl)methyl]-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-ethoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-hydroxy-4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-hydroxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-hydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-hydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(2-methoxyphenyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-phenyl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-[(7-methylnaphthalen-1-yl)methyl]-9H-purin-6-amine
-
9-(2-deoxy-2-[[(4-heptylphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(4-hydroxy-3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(4-hydroxy-3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(1-phenylethyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(2,5-dimethylphenyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3,4-dimethylphenyl)-9H-purin-6-amine
-
9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amine
-
9-(2-[[(4-chlorophenyl)carbonyl]amino]-2-deoxypentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amine
-
9-(2-[[(4-chlorophenyl)carbonyl]amino]-2-deoxypentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
-
9-(2-[[(4-chlorophenyl)carbonyl]amino]-2-deoxypentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amine
-
9-[2-(benzylamino)ethyl]-8-thiophen-2-yl-9H-purin-6-amine
-
9-[2-([[2,4-bis(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amine
-
9-[2-([[3,4-bis(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amine
-
9-[2-([[3-(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
-
9-[2-([[3-(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amine
-
9-[2-([[4-(acetyloxy)-3-methoxyphenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-(naphthalen-1-ylmethyl)-9H-purin-6-amine
-
9-[2-deoxy-2-([[4-(dimethylamino)phenyl]carbonyl]amino)pentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amine
-
9-[2-deoxy-2-[(phenylcarbonyl)amino]pentofuranosyl]-8-thiophen-2-yl-9H-purin-6-amine
-
acetone
inhibits about 60% at 15%
acetonitril
inhibits about 90% at 15%
acetylleucine chloromethyl ketone
-
binds to GAPDH to modulate the conformation of the enzyme, the modified enzyme is susceptible to chymotrypsin-like protease activity, cleavage at TRp195-Arg196; irreversible inhibition, enzyme modified by acetylleucine chloromethyl ketone is deduced to be digested at the peptide bond Trp196-Arg196
ADP-ribose
coenzyme analogue with a non-cooperative behaviour of binding, is a potent competitive inhibitor
alpha-chlorohydrin
the contraceptive activity of alpha-chlorohydrin and its apparent specificity for the sperm isoform in vivo are likely to be due to differences in metabolism to 3-chlorolactaldehyde in spermatozoa and somatic cells
arsenate
linear substrate inhibition, competitive versus phosphate
beta-mercaptoethanol
-
strong inhibition at 10 mM
CGP-3466
-
deprenyl-related compound that inhibits the pro-apoptotic activity of GAPDH
D-glyceraldehyde 3-phosphate
demethylasterriquinone B1
-
binding of demethylasterriquinone B1 toGAPDH could disrupt phosphatase acting upon phosphatidylinositol lipids and thereby potentiate insulin signaling via the phosphatidylinositol-3-kinase pathway
diepoxybutane
-
incubation of GAPDH with bis-electrophiles results in inhibition of its catalytic activity, but only at high concentrations of diepoxybutane
ethanol
inhibits about 55% at 15%
Fe2+
-
in the absence of quercetin, GAPDH can be oxidized by ferrous ions due to the formation of reactive oxygen species according to the following series of reactions
FK506-binding protein 36
-
guajaverin
molecular docking studies. Guajaverin is stabilized by five hydrogen bonds with the amino acids Ser165, Thr226, Arg249, Ser134, and Glu336
guanidine hydrochloride
unfolding of both wild type and mutant dN-GAPDS proteins is described by a single [GdnHCl]50 value. For the truncated mutant dN-GAPDS, it constitutes 1.83 M. Different mutations of dN-GAPDS alter this parameter to various extents. The most pronounced effect is observed in the case of mutants P111A, P157A, and D311N. The mutation P111A increases the value of [GdnHCl]50 by 0.43 M, the mutations P157A and D311N decrease the GdnHCl50 value by 0.36 and 0.48 M, respectively. In other mutants, the [GdnHCl]50 value is less affected or does not change, overview; unfolding of muscle isoenzyme GAPD is a two step process
hydrogen peroxide
-
maximum inhibition is observed at concentrations of 0.2 mM
Isopropanol
inhibits about 60% at 15%
monoclonal antibody 8B7
-
antibody is specific for glyceraldehyde 3-phosphate dehydrogenase. In lysates of Sf21 cells, the antibody inhibits protein translation, possibly due to inhibition of the binding of glyceraldehyde 3-phosphate dehydrogenase to mRNA and tRNA
-
N-(1,2,3,4-tetrahydronaphthalen-1-yl)adenosine
-
N-(2-[[2-(hydroxymethyl)phenyl]sulfanyl]phenyl)adenosine
-
N-(3-acetylnaphthalen-1-yl)-9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
N-(3-acetylnaphthalen-1-yl)-9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
N-(4-acetylnaphthalen-1-yl)-9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
N-(4-acetylnaphthalen-1-yl)-9-[2-deoxy-2-([[4-(methylamino)phenyl]carbonyl]amino)pentofuranosyl]-9H-purin-6-amine
-
N-(diphenylmethyl)adenosine
-
N-(naphthalen-2-ylmethyl)-9-pentofuranosyl-9H-purin-6-amine
-
N-(phenoxyacetyl)-L-cysteine
N-(phenylacetyl)-glutathione
N-acetylcysteine
-
5 mM N-acetylcysteine significantly reduces G3PD activation induced by both H2O2 and ferric protoporphyrin IX
N-benzyl-9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amine
-
N-ethylmaleimide
-
1 mM completely inactivates the enzyme in 10 min
N-[2-(6-amino-8-bromo-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]benzamide
-
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]-1H-benzimidazole-5-carboxamide
-
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]-3,4,5-trihydroxybenzamide
-
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]benzamide
-
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]thiophene-2-carboxamide
-
N-[2-(6-amino-9H-purin-9-yl)cyclopentyl]-3-bromobenzamide
-
N-[2-(6-amino-9H-purin-9-yl)ethyl]-4-methylbenzamide
-
Na+
-
120 mM almost complete inhibition. Cys, GSH and deproteinated crude extract protect against inhibition
NADP+
-
75% inhibition in the presence of 2 mM NADP+
nitric oxide
isoform GAPC1 is irreversibly inhibited in a time- and concentration-dependent manner
NO3-
-
uncompetitive inhibitor with NAD+, dead end inhibitor
p-hydroxymercuribenzoate
-
-
quercetin
molecular docking studies. Quercetin is stabilized by two hydrogen bonds with the amino acids Ala198 and Pro253
S-(2-succinyl)cysteine
-
chemical modification by S-(2-succinyl)cysteine causes irreversible inactivation of glyceraldehyde-3-phosphate dehydrogenase in vitro. In diabetic rats, succination of GAPDH is increased in muscle, and the extent of succination correlates strongly with the decrease in specific activity of the enzyme
suramin
-
cyosolic enzyme: competitive with NAD+. Effect on Km-value and maximal veocity of glyoxysomal enzyme
tiliroside
molecular docking studies. Tiliroside is stabilized by four hydrogen bonds with the amino acids Cys166, Ser134, and Ser110
trehalose
might be an inhibitor, trehalose induces a conformational change in ecGAPDH in the current structure. The rotation of GAPDH also induced a conformational change in its active site. This suggests that the binding of trehalose to GAPDH induced a conformational change in its active site to prevent the binding of NAD+, although the NAD+- and trehalose-binding sites differ from one another
Trinitrobenzenesulfonic acid
tris(2-carboxyethyl)phosphine
a reducing agent to break the disulfide bonds, inhibits formation of the GAPDH-AP DNA-borohydride-independent adduct
tubulin
-
GAPDH catalytic activity is inhibited upon formation of a complex with tubulin
-
Tween 20
inhibits about 60% at 1%
1-hydroxy-2-oxo-3,3-bis(2-aminoethyl)-1-triazene
-
1-hydroxy-2-oxo-3,3-bis(2-aminoethyl)-1-triazene
-
-
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
-
-
ADP
-
-
ADP
-
inhibition of esterase activity with p-nitrophenyl acetate
ADP
-
moderately inhibits arsenate reductase activity
ADP
-
moderately inhibits arsenate reductase activity
Agaricic acid
-
0.14 mM, 50% inhibition in absence of NAD+. 2 mM, 35% loss of activity in presence of 0.017 mM NAD+
Agaricic acid
-
glyoxysomal enzyme: 0.2 mM, 60% loss of activity. Cytosolic enzyme: 2 mM, less than 20% loss of activity
AMP
-
-
AMP
-
18 mM, only 5% loss of activity
AMP
-
inhibition of esterase activity with p-nitrophenyl acetate
ATP
-
-
ATP
-
1 mM, 25% loss of activity
ATP
-
inhibition of esterase activity with p-nitrophenyl acetate
ATP
-
10 mM, 50% inhibition
ATP
-
noncompetitive inhibitor
ATP
-
moderately inhibits arsenate reductase activity
ATP
-
inhibition is less pronounced for enzyme from sarcoma tissue as compared to normal muscle tissue
ATP
-
moderately inhibits arsenate reductase activity
ATP
-
at 0°C, loss of activity. Some of the lost activity is regained upon warming to room temperature
cAMP
-
-
cAMP
about 80% inhibition at 30 mM, competitive versus NAD+
CdCl2
20 mM, about 30% inhibition. 10 mM, 70% inhibition
CdCl2
-
20 mM, about 65% inhibition
chalepin
-
chalepin
-
natural inhibitor of GAPDH
Cu2+
-
-
Cu2+
-
1 mM CuCl2, complete inhibition
Cu2+
complete inhibition at 10 mM
CuSO4
0.001 mM, 90% inhibition within 2 min
CuSO4
-
0.001 mM, 70% inhibition in 2 min
D-glyceraldehyde 3-phosphate
-
substrate inhibition
D-glyceraldehyde 3-phosphate
-
substrate inhibition
D-glyceraldehyde 3-phosphate
2-mercaptoethanol protects against the inhibition
D-glyceraldehyde 3-phosphate
-
substrate inhibition
dithiothreitol
-
DTT
dithiothreitol
-
strong inhibition at 2 mM
ferriprotoporphyrin IX
-
enzyme is partially inactivated through oxidation of critical thiols
ferriprotoporphyrin IX
-
-
ferriprotoporphyrin IX
strongly inhibits PfGapdh, in contrast to the human GAPDH
FK506-binding protein 36
-
i.e. FKBP36. The interaction between FKBP36 and GAPDH directly inhibits the catalytic activity of GAPDH. FKBP36 expression causes a significant reduction of the GAPDH level and activity in COS-7 cells. GAPDH is depleted by FKBP36 expression, particularly in the cytosolic fraction
-
FK506-binding protein 36
-
i.e. FKBP36, forms complexes with glyceraldehyde-3-phosphate dehydrogenase and Hsp90. Both proteins bind independently to different sites of the FKBP36 tetratricopeptide repeat domain. The interaction between FKBP36 and GAPDH directly inhibits the catalytic activity of GAPDH
-
fumarate
-
approximately 20% of GAPDH activity is lost by incubation with 0.5 mM fumarate for 24 h, and 100% activity is lost in incubations with 500 mM fumarate at 24 h, NADH in the presence or absence of D-glyceraldehyde 3-phosphate significantly accelerates the inactivation of GAPDH by fumarate
fumarate
-
inactivation of GAPDH by fumarate in vitro correlates with formation of S-(2-succinyl)cysteine, in diabetic compared with control rats fumarate and S-(2-succinyl)cysteine concentration increase approximately 5fold, accompanied by an about 25% decrease in GAPDH specific activity
glutathione
-
5 mM oxidized glutathione, GSSG, formation of mixed disulfide between glutathione and A4-GAPDH results in the inhibition of enzyme activity
glutathione
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
glutathione
-
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
glutathione
-
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
glutathione
-
formation of mixed disulfide between glutathione and GAPDH results in the inhibition of enzyme activity
glutathione
-
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
H2O2
-
-
H2O2
inhibits enzyme activity by converting the thiolate of Cys149 into irreversibly oxidized forms, -SO2- and SO3- via a labile sulfenate intermediate SO?. Reduced glutathione prevents this irreversible process by reacting with Cys149 sulfenates to give rise to a mixed disulfide. Glutathionylated enzyme can be fully reactivated either by cytosolic glutaredoxin, via a glutathione-dependent monothiol mechanism, or, less efficiently, by cytosolic thioredoxins physiologically reduced by NADPH:thioredoxin reductase
H2O2
isoform GAPC1 is irreversibly inhibited in a time- and concentration-dependent manner
H2O2
irreversible inhibition
H2O2
-
GAPDH is oxidized by H2O2 which is likely formed due to the spontaneous dismutation of the superoxide anion that is formed during the autooxidation of quercetin that can result in the oxidation of SH-groups of GAPDH
Hg2+
-
strong inhibition
Hg2+
complete inhibition at 10 mM
HgCl2
-
1 mM, complete inhibition
iodoacetamide
-
5 mM, complete inhibition
iodoacetamide
an irreversible, cysteine-specific alkylator, inactivation kinetics for inactivation of mutant C162A
iodoacetamide
-
0.5 mM, 9% inhibition
iodoacetate
-
-
iodoacetate
-
0.2 mM, 67% inhibition
K+
-
-
Koningic acid
-
inhibits arsenate reductase activity and activity with D-glyceraldehyde 3-phosphate, phosphate and NAD+
Koningic acid
-
inhibits arsenate reductase activity and activity with D-glyceraldehyde 3-phosphate, phosphate and NAD+
Koningic acid
-
irreversible inhibition, GAPDH I : 50% inhibition by 1 mM, no effect at 0.1 mM. GAPDH II: 50% inhibition by 0.01 mM. Under conditions of koningic acid production the koningic-acid-resistant isoenzyme GAPDH I is produced. In peptone-rich medium where non koningic acid is produced the koningic-acid-sensitive isoenzyme GAPDH II is produced in addition to GAPDH 1
N-(phenoxyacetyl)-L-cysteine
-
65% inhibition at 0.56 mM
N-(phenoxyacetyl)-L-cysteine
-
inhibits by forming disulfide bonds with the Cys149 residue in the enzyme active site
N-(phenylacetyl)-glutathione
-
45% inhibition at 0.56 mM
N-(phenylacetyl)-glutathione
-
inhibits by forming disulfide bonds with the Cys149 residue in the enzyme active site
Na2S4O6
-
-
Na2S4O6
-
0.1 mM, complete inhibition
NAD+
-
competitive against NADH
NAD+
-
competitive against NADH
NAD+
-
substrate inhibition
NAD+
NAD+ inhibition for GAPDH3 RNA binding capability, NAD+ inhibits the AUUUA binding. The inhibition effect is weaker for the 5-base substrate than for the 13-base substrate. RNA substrate binding needs to competitively displace the NAD+ molecules from the binding groove
NADH
-
-
NADH
-
competitive with respect to NAD+ and phosphate
NADH
-
competitive against NAD+
NADH
-
strongly inhibits arsenate reductase activity
NADH
2-mercaptoethanol protects against the inhibition, but the inhibitory effect of NADH is not influenced by heavy metal ions or EDTA
NADH
noncompetitive inhibition versus D-glyceraldehyde 3-phosphate, competitive inhibition versus both NAD+ and arsenate
NADH
-
competitive with NAD+ and with D-glyceraldehyde 3-phosphate
NADH
-
strongly inhibits arsenate reductase activity
NEM
-
-
NEM
-
1 mM, complete inhibition
NO
-
inactivation by induction of a covalent binding of NAD+ to the enzyme
NO
-
diminishes GAPDH specific activity by 10%-20%
oxidized glutathione
inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found glutathionylated; inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found glutathionylated
oxidized glutathione
-
inactivation, at least partially reversible upon addition of dithiothreitol
oxidized glutathione
-
inactivation, at least partially reversible upon addition of dithiothreitol
PCMB
-
-
PCMB
-
1 mM, complete inhibition, partially reversed by dithiothreitol; 1 mM, inhibition is partially reversed by dithiothreitol
PCMB
-
5 mM, complete inhibition
pentalenolactone
-
reversible
pentalenolactone
-
insensitive to
pentalenolactone
-
irreversible
pentalenolactone
-
irreversible
pentalenolactone
-
pentalenolactone-sensitive enzyme is strongly inhibited, pentalenolactone-insensitive enzyme is not inhibited
pentalenolactone
-
most potent inhibitor; reversible
phosphate
linear substrate inhibition, competitive versus arsenate
phosphate
-
substrate inhibition
pseudo-GAPDH
psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction
-
pseudo-GAPDH
psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction
-
pseudo-GAPDH
psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction
-
pseudo-GAPDH
psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction
-
pseudo-GAPDH
psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction
-
pseudo-GAPDH
psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction
-
pyridoxal 5'-phosphate
-
inactivation with pseudo-first-order kinetics
pyridoxal 5'-phosphate
-
-
S-nitrosoglutathione
inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found nitrosylated; inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found nitrosylated; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol
S-nitrosoglutathione
-
inactivation, at least partially reversible upon addition of dithiothreitol; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol
S-nitrosoglutathione
-
inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol
S-nitrosoglutathione
-
inactivation, at least partially reversible upon addition of dithiothreitol; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol
sodium nitroprusside
-
the NO-generating compound inactivates by induction of a covalent binding of NAD+ to the enzyme
sodium nitroprusside
-
inhibition in presence of NAD+ is due primarily to active-site nitrosylation, covalent binding of NAD+ through a NO-dependent thiol intermediate
sodium nitroprusside
-
maximum inhibition is observed at concentrations of 0.2 mM
Sodium tetrathionate
-
-
T0501_7749
2-[2-amino-3-(4-methylphenyl)sulfonylpyrrolo[3,2-b]quinoxalin-1-yl]-1-(4-nitrophenyl)ethanol, a small-molecule, highly selective isozyme GAPDHS inhibitor, molecular docking simulations in GAPDHS and GAPDH isozymes, binding structure, overview; 2-[2-amino-3-(4-methylphenyl)sulfonylpyrrolo[3,2-b]quinoxalin-1-yl]-1-(4-nitrophenyl)ethanol, identification of a small-molecule GAPDHS inhibitor with micromolar potency and high selectivity that exerts the expected inhibitory effects on sperm glycolysis and motility. The compound causes significant reductions in the percentage of motile human sperm. Molecular docking simulations in GAPDHS and GAPDH isozymes, binding structure, overview
T0501_7749
2-[2-amino-3-(4-methylphenyl)sulfonylpyrrolo[3,2-b]quinoxalin-1-yl]-1-(4-nitrophenyl)ethanol, a small-molecule, highly selective isozyme GAPDHS inhibitor, molecular docking simulations in GAPDHS and GAPDH isozymes, binding structure, overview; 2-[2-amino-3-(4-methylphenyl)sulfonylpyrrolo[3,2-b]quinoxalin-1-yl]-1-(4-nitrophenyl)ethanol, a small-molecule, highly selective isozymeGAPDHS inhibitor, the compound causes significant reductions in mouse sperm lactate production and in the percentage of motile mouse sperm. Molecular docking simulations in GAPDHS and GAPDH isozymes, binding structure, overview
T0506_9350
1-cyclohexyl-3-[4-[(4-methoxyphenyl)sulfamoyl]-2-nitroanilino]urea, a partial selective isozyme GAPDH inhibitor, binding structure, overview; 1-cyclohexyl-3-[4-[(4-methoxyphenyl)sulfamoyl]-2-nitroanilino]urea, a partial selective isozyme GAPDH inhibitor, binding structure, overview. T0506_9350 inhibition of human and mouse tGAPDHS is competitive with both D-glyceraldehyde 3-phosphate and NAD+
T0506_9350
1-cyclohexyl-3-[4-[(4-methoxyphenyl)sulfamoyl]-2-nitroanilino]urea, a partial selective isozyme GAPDH inhibitor, binding structure, overview. T0506_9350 inhibition of human and mouse tGAPDHS is competitive with both D-glyceraldehyde 3-phosphate and NAD+
Trinitrobenzenesulfonic acid
-
inactivation with pseudo-first-order kinetics. D-glyceraldehyde-3-phosphate, NAD+, NADH and 3-phospho-D-glyceroyl phosphate almost completely protect from inactivation
Trinitrobenzenesulfonic acid
-
-
Tyr-Asp
a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions; a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions
-
Tyr-Asp
a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions; a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions
-
ZnSO4
20 mM, 70% inhibition
ZnSO4
-
20 mM, 50% inhibition
additional information
-
wild-type Clostridium thermocellum is unable to initiate growth when inoculated into medium containing ethanol at concentrations of 20 g/l or higher. Strains adapted for improved tolerance by serial transfer over a period of several weeks have been shown to initiate growth in the presence of 50-55 g/l ethanol. A dramatic accumulation of NADH and NADPH is observed when ethanol is added to the culture. The Gapdh from Clostridium thermocellum (Ctherm_Gapdh) is very sensitive to the NADH/NAD+ ratio
-
additional information
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH
-
additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
-
additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
-
additional information
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH
-
additional information
no effect on enzyme activity by SDS at 1%
-
additional information
-
no effect on enzyme activity by SDS at 1%
-
additional information
development of GAPDH inhibitors as anti-cancer and anti-parasitic agents
-
additional information
-
development of GAPDH inhibitors as anti-cancer and anti-parasitic agents
-
additional information
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH
-
additional information
-
the produced type I antibody induces a time-dependent decrease in the activity by 80-90% of the active holoenzyme and 25% of the apoenzyme
-
additional information
-
inhibited by binding to the cell membrane
-
additional information
-
stauroporine does not inhibit stimulation of G3PD activity
-
additional information
-
not inhibited by DMSO, dibromomethane and 1,2-dibromoethane
-
additional information
-
anti-GAPDH immunoglobulin G in the cerebrospinal fluid of patients with multiple sclerosis inhibits GAPDH glycolytic activity (38% or 58% inhibition after incubation of GAPDH with 0.002 or 0.004 mg, respectively)
-
additional information
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH
-
additional information
-
stable suppression of GAPDH (possibly by some reversible posttranslational modification) during ground squirrel torpor, which likely contributes to the overall reduction in carbohydrate metabolism when these animals switch to lipid fuels during dormancy. Action of commercial alkaline phosphatase causes a 50% increase in euthermic GAPDH activity, activities of protein kinase C, AMP-dependent protein kinase, or calcium-calmodulin protein kinase lead to about 80% decreases in euthermic GAPDH activity
-
additional information
-
no inhibition by D-glucose 6-phosphate, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, pyruvate
-
additional information
-
the NADH/NAD+ ratio is shown to modulate the in vivo activity; the wild type GADPH is strongly inhibited in vitro by decreased pH values
-
additional information
-
not inhibited by thiorphan and lipopolysaccharide
-
additional information
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH
-
additional information
-
NADH, glucose-1-phosphate, AMP, ADP, ATP, and fructose-6-phosphate do not affect kinetic properties of GAPN and no change in cofactor preference from NAD+ to NADP+ in the presence of these metabolic intermediates is detected
-
additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
-
additional information
no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu); no inhibition by treatment with single amino acids (Tyr and Asp) or chemically unrelated dipeptide (Ile-Glu)
-
additional information
-
not inhibited by thiorphan and lipopolysaccharide
-
additional information
-
succinate has no effect on enzyme activity
-
additional information
-
not inhibited by ((R)-mandelyl)-(S)-cysteine
-
additional information
-
not inhibitory: N-((R)-mandelyl)-(S)-cysteine
-
additional information
-
not inhibited by thiorphan and lipopolysaccharide
-
additional information
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH
-
additional information
the C-terminus of CP12 is inserted into the active-site region of glyceraldehyde-3-phosphate dehydrogenase, resulting in competitive inhibition of the enzyme
-
additional information
-
H2O2 does not significantly alter GAPDH-specific activity levels in cell free extracts
-
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0.01 - 0.018
1,3-diphosphoglyceric acid
0.158 - 0.62
3-acetyl-NAD+
1.43 - 8.15
3-acetylpyridine hypoxanthine nucleotide
0.002 - 1.78
3-phospho-D-glyceroyl phosphate
0.31
acetaldehyde
-
recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C
0.2
C6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+
-
-
0.061
C8-(4-(2,2,6,6-tetramethyl-piperidinyl-l-oxyl)-amino)-NAD+
-
-
0.00025 - 15
D-glyceraldehyde 3-phosphate
0.0734 - 0.5
D-Glyceraldehyde-3-phosphate
0.1
DL-glyceraldehyde
-
enzyme form E8.5, pH 7
0.119 - 0.127
erythrose 4-phosphate
0.2
glyceraldehyde
-
recombinant enzyme, at 25°C
0.0102 - 0.145
N6-(2-carboxyethyl)-NAD+
additional information
additional information
-
0.01
1,3-diphosphoglyceric acid
-
enzyme form E6.6, pH 7
0.012
1,3-diphosphoglyceric acid
-
enzyme form E8.5, pH 7
0.018
1,3-diphosphoglyceric acid
-
enzyme form E9.0, pH 7
0.158
3-acetyl-NAD+
-
-
1.43
3-acetylpyridine hypoxanthine nucleotide
-
-
8.15
3-acetylpyridine hypoxanthine nucleotide
-
-
0.002
3-phospho-D-glyceroyl phosphate
-
enzyme form E6.8, pH 7
0.032
3-phospho-D-glyceroyl phosphate
-
enzyme form E9.0, pH 9
0.034
3-phospho-D-glyceroyl phosphate
-
-
0.035
3-phospho-D-glyceroyl phosphate
-
enzyme form E8.5, pH 9
0.036
3-phospho-D-glyceroyl phosphate
wild type enzyme, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C
0.036
3-phospho-D-glyceroyl phosphate
wild-type, pH 8.8, 25°C
0.042
3-phospho-D-glyceroyl phosphate
-
enzyme form E6.6, pH 9
0.049
3-phospho-D-glyceroyl phosphate
mutant enzyme F37L, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C
0.049
3-phospho-D-glyceroyl phosphate
mutant F36L, pH 8.8, 25°C
0.051
3-phospho-D-glyceroyl phosphate
mutant enzyme F37G, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C
0.051
3-phospho-D-glyceroyl phosphate
mutant F36G, pH 8.8, 25°C
0.053
3-phospho-D-glyceroyl phosphate
mutant enzyme F37T, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C
0.053
3-phospho-D-glyceroyl phosphate
mutant F36T, pH 8.8, 25°C
0.1
3-phospho-D-glyceroyl phosphate
-
glyoxysomal enzyme
0.13
3-phospho-D-glyceroyl phosphate
-
-
0.14
3-phospho-D-glyceroyl phosphate
-
-
0.14
3-phospho-D-glyceroyl phosphate
-
cytosolic enzyme
0.172
3-phospho-D-glyceroyl phosphate
-
enzyme form E6.8, pH 9
0.22
3-phospho-D-glyceroyl phosphate
-
pH 8.0, 5°C, euthermic
0.24
3-phospho-D-glyceroyl phosphate
-
pH 8.0, 36°C, long torpor
0.24
3-phospho-D-glyceroyl phosphate
-
pH 8.0, 5°C, euthermic
0.28
3-phospho-D-glyceroyl phosphate
-
pH 8.0, 36°C, long torpor
0.47
3-phospho-D-glyceroyl phosphate
-
-
1.78
3-phospho-D-glyceroyl phosphate
Q81X74, YP_027084
pH 8.6, temperature not specified in the publication
1
arsenate
-
-
8.3
arsenate
-
45°C, pH 7.8
0.00025
D-glyceraldehyde 3-phosphate
wild-type, pH 8.5, 25°C
0.00046
D-glyceraldehyde 3-phosphate
N-terminally truncated mutant, pH 8.5, 25°C
0.0102
D-glyceraldehyde 3-phosphate
-
in the presence of 5% (v/v) methanol, in TEA-HCl buffer (pH 7.5) at 25°C
0.0102
D-glyceraldehyde 3-phosphate
-
in the presence of 5% (v/v) methanol
0.0108
D-glyceraldehyde 3-phosphate
-
in the presence of 5% (v/v) DMSO, in TEA-HCl buffer (pH 7.5) at 25°C
0.0108
D-glyceraldehyde 3-phosphate
-
in the presence of 5% (v/v) DMSO
0.0207
D-glyceraldehyde 3-phosphate
-
pH 8.5, 25°C
0.0393
D-glyceraldehyde 3-phosphate
-
in the absence of DMSO and methanol, in TEA-HCl buffer (pH 7.5) at 25°C
0.053
D-glyceraldehyde 3-phosphate
-
-
0.064
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant wild-type enzyme
0.07
D-glyceraldehyde 3-phosphate
-
-
0.074
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant mutant S66A
0.08
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant mutant S205D
0.081
D-glyceraldehyde 3-phosphate
-
-
0.082
D-glyceraldehyde 3-phosphate
-
-
0.087
D-glyceraldehyde 3-phosphate
-
pH 7.3, enzyme isolated of sarcoma tissue
0.089
D-glyceraldehyde 3-phosphate
-
pH 8.0, enzyme isolated of sarcoma tissue
0.09
D-glyceraldehyde 3-phosphate
-
-
0.09
D-glyceraldehyde 3-phosphate
-
-
0.097
D-glyceraldehyde 3-phosphate
recombinant dN-GAPDS enzyme, pH 8.9, 20°C
0.098
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant mutant S205A
0.1
D-glyceraldehyde 3-phosphate
-
pentalenolactone-insensitive enzyme
0.11
D-glyceraldehyde 3-phosphate
-
pH 8.8, enzyme isolated of sarcoma tissue
0.111
D-glyceraldehyde 3-phosphate
wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.111
D-glyceraldehyde 3-phosphate
wild-type, pH 8.8, 25°C
0.147
D-glyceraldehyde 3-phosphate
-
in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 35°C
0.149
D-glyceraldehyde 3-phosphate
-
pH 7.3, enzyme isolated of healthy patients
0.149
D-glyceraldehyde 3-phosphate
mutant enzyme F37L, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.149
D-glyceraldehyde 3-phosphate
mutant F36L, pH 8.8, 25°C
0.15
D-glyceraldehyde 3-phosphate
-
glyoxysomal enzyme
0.153
D-glyceraldehyde 3-phosphate
pH and temperature not specified in the publication
0.156
D-glyceraldehyde 3-phosphate
mutant enzyme F37G, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.156
D-glyceraldehyde 3-phosphate
mutant F36G, pH 8.8, 25°C
0.159
D-glyceraldehyde 3-phosphate
-
pH 8.0, enzyme isolated of healthy patients
0.16
D-glyceraldehyde 3-phosphate
-
pH 8.8, enzyme isolated of healthy patients
0.16
D-glyceraldehyde 3-phosphate
-
free enzyme, at pH 8.6 and 25°C
0.16
D-glyceraldehyde 3-phosphate
-
free enzyme,25°C, pH 8.6
0.161
D-glyceraldehyde 3-phosphate
mutant enzyme F37T, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.161
D-glyceraldehyde 3-phosphate
mutant F36T, pH 8.8, 25°C
0.17
D-glyceraldehyde 3-phosphate
-
cytosolic enzyme
0.188
D-glyceraldehyde 3-phosphate
pH 8.5, 30°C, recombinant mutant S124A
0.21
D-glyceraldehyde 3-phosphate
-
in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C
0.23
D-glyceraldehyde 3-phosphate
-
-
0.24
D-glyceraldehyde 3-phosphate
-
-
0.24
D-glyceraldehyde 3-phosphate
-
pH 8.0
0.24
D-glyceraldehyde 3-phosphate
recombinant dN-GAPDS enzyme mutant D311N, pH 8.9, 20°C
0.25
D-glyceraldehyde 3-phosphate
-
pentalenolactone-sensitive enzyme
0.25
D-glyceraldehyde 3-phosphate
recombinant enzyme, pH and temperature not specified in the publication
0.25
D-glyceraldehyde 3-phosphate
glyceraldehyde-3-phosphate dehydrogenase, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
0.25
D-glyceraldehyde 3-phosphate
-
isoform TDH3, pH 8.5, 25°C
0.27
D-glyceraldehyde 3-phosphate
recombinant wild-type enzyme, pH 8.9, 20°C
0.29
D-glyceraldehyde 3-phosphate
mutant N313T/Y317G
0.3
D-glyceraldehyde 3-phosphate
-
-
0.3
D-glyceraldehyde 3-phosphate
-
-
0.31
D-glyceraldehyde 3-phosphate
-
mutant enzyme W48F
0.31
D-glyceraldehyde 3-phosphate
wild type enzyme, pH 8.7, 25°C
0.32
D-glyceraldehyde 3-phosphate
mutant enzyme H178N, pH 8.7, 25°C
0.33
D-glyceraldehyde 3-phosphate
-
GAPDH II
0.34
D-glyceraldehyde 3-phosphate
mutant enzyme C151S, pH 8.7, 25°C
0.34
D-glyceraldehyde 3-phosphate
mutant enzyme C151S/H178N, pH 8.7, 25°C
0.344
D-glyceraldehyde 3-phosphate
-
-
0.385
D-glyceraldehyde 3-phosphate
-
pH 8.9
0.4
D-glyceraldehyde 3-phosphate
-
-
0.42
D-glyceraldehyde 3-phosphate
mutant N313T
0.42
D-glyceraldehyde 3-phosphate
free enzyme, at pH 7.5 and 25°C
0.42
D-glyceraldehyde 3-phosphate
free enzyme,25°C, pH 8.6
0.42
D-glyceraldehyde 3-phosphate
-
isoform TDH2, pH 8.5, 25°C
0.45
D-glyceraldehyde 3-phosphate
-
pH 8.0, 5°C, euthermic
0.46
D-glyceraldehyde 3-phosphate
recombinant, highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
0.5
D-glyceraldehyde 3-phosphate
immobilized enzyme reactor, at pH 7.5 and 25°C
0.5
D-glyceraldehyde 3-phosphate
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
0.51
D-glyceraldehyde 3-phosphate
-
-
0.52
D-glyceraldehyde 3-phosphate
-
pH 8.0, 5°C, euthermic
0.54
D-glyceraldehyde 3-phosphate
-
GAPDH I
0.55
D-glyceraldehyde 3-phosphate
-
30°C, pH 7.2
0.6
D-glyceraldehyde 3-phosphate
-
-
0.762
D-glyceraldehyde 3-phosphate
-
0.763
D-glyceraldehyde 3-phosphate
wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, pH 8.8, temperature not specified in the publication
0.77
D-glyceraldehyde 3-phosphate
in 50 mM glycine, 50 mM potassium phosphate, 5 mM EDTA, pH 9.0
0.8
D-glyceraldehyde 3-phosphate
-
wild-type enzyme
0.8
D-glyceraldehyde 3-phosphate
mutant enzyme Y46G
0.86
D-glyceraldehyde 3-phosphate
-
isoform TDH1, pH 8.5, 25°C
0.88
D-glyceraldehyde 3-phosphate
mutant Y317A
0.89
D-glyceraldehyde 3-phosphate
wild-type enzyme
0.9
D-glyceraldehyde 3-phosphate
mutant enzyme E276G
1
D-glyceraldehyde 3-phosphate
mutant enzyme D186G and mutant enzyme S48G
1.1
D-glyceraldehyde 3-phosphate
wild-type enzyme
1.4
D-glyceraldehyde 3-phosphate
-
pH 8.0, 36°C, long torpor
1.44
D-glyceraldehyde 3-phosphate
pH 7.4, 37°C, recombinant enzyme
1.45
D-glyceraldehyde 3-phosphate
-
recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C
1.5
D-glyceraldehyde 3-phosphate
-
pH 8.0, 36°C, long torpor
1.78
D-glyceraldehyde 3-phosphate
Q81X74, YP_027084
at pH 8.5, temperature not specified in the publication
2.05
D-glyceraldehyde 3-phosphate
mutant Y317G
2.9
D-glyceraldehyde 3-phosphate
-
pH 8.0
3.7
D-glyceraldehyde 3-phosphate
-
immobilized enzyme reactor, at pH 8.6 and 25°C
3.7
D-glyceraldehyde 3-phosphate
-
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
15
D-glyceraldehyde 3-phosphate
-
45°C, pH 7.8
0.0734
D-Glyceraldehyde-3-phosphate
-
in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C
0.425
D-Glyceraldehyde-3-phosphate
-
free enzyme
0.5
D-Glyceraldehyde-3-phosphate
-
GAPDH immobilized on an octyl silica column
0.119
erythrose 4-phosphate
-
enzyme form E8.5, pH 7
0.127
erythrose 4-phosphate
-
enzyme form E9.0, pH 7
0.0102
N6-(2-carboxyethyl)-NAD+
-
-
0.0674
N6-(2-carboxyethyl)-NAD+
-
-
0.145
N6-(2-carboxyethyl)-NAD+
-
-
0.000032
NAD+
-
0.000032
NAD+
wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, pH 8.8, temperature not specified in the publication
0.01
NAD+
-
enzyme form E8.5, pH 9
0.0178
NAD+
-
pH 8.5, 25°C
0.02
NAD+
-
enzyme form E9.0, pH 9
0.022
NAD+
in 50 mM glycine, 50 mM potassium phosphate, 5 mM EDTA, pH 9.0
0.025
NAD+
-
in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C
0.027
NAD+
-
enzyme form E6.8, pH 9
0.035
NAD+
-
pH 7.3, enzyme isolated of sarcoma tissue
0.035
NAD+
N-terminally truncated mutant, pH 8.5, 25°C
0.036
NAD+
-
pH 8.0, enzyme isolated of sarcoma tissue
0.0386
NAD+
-
poly(ethylene glycol)-bound
0.04
NAD+
-
cytosolic enzyme
0.04
NAD+
mutant enzyme S48G
0.04
NAD+
-
pH 8.8, enzyme isolated of sarcoma tissue
0.045
NAD+
wild-type enzyme
0.047
NAD+
-
pH 8.8, enzyme isolated of healthy patients
0.048
NAD+
pH 8.0, 25°C, recombinant wild-type enzyme
0.048
NAD+
wild-type, pH 8.5, 25°C
0.05
NAD+
wild-type enzyme
0.05
NAD+
-
pH 8.0, 25°C, tetrameric enzyme form, wild-type
0.057
NAD+
-
recombinant enzyme, in the presence of D-glyceraldehyde 3-phosphate, in 50 mM Tricine buffer (pH 8.5), at 25°C
0.058
NAD+
mutant N313T/Y317G
0.058
NAD+
mutant D35G/L36T/P192S, pH 8.5, 25°C
0.058
NAD+
pH 8.0, 25°C, recombinant mutant D35G/L36T/P192S
0.059
NAD+
wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.059
NAD+
wild-type, pH 8.8, 25°C
0.06
NAD+
-
pH 8.0, 25°C, tetrameric enzyme form, mutant Y283V
0.062
NAD+
-
pH 8.0, enzyme isolated of healthy patients
0.064
NAD+
-
in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 35°C
0.07
NAD+
mutant enzyme E276G
0.071
NAD+
-
pH 7.3, enzyme isolated of healthy patients
0.088
NAD+
-
recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), in the presence of glyceraldehyde, at 25°C
0.092
NAD+
-
in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C
0.1
NAD+
-
wild-type enzyme
0.1
NAD+
-
pH 8.0, 25°C, tetrameric enzyme form, mutant W310F
0.1
NAD+
wild-type, pH 8.5, 25°C
0.1
NAD+
mutant D35G/L36T/T37K/P192S, pH 8.5, 25°C
0.1
NAD+
pH 8.0, 25°C, recombinant mutant D35G/L36T/T37K/P192S
0.109
NAD+
-
recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), in the presence of acetaldehyde, at 25°C
0.11
NAD+
-
mutant enzyme W84F
0.11
NAD+
-
pentalenolactone-sensitive enzyme
0.12
NAD+
-
pentalenolactone-insensitive enzyme
0.122
NAD+
pH 8.5, 30°C, recombinant mutant S205A
0.122
NAD+
pH 8.5, 30°C, recombinant mutant S66A
0.126
NAD+
pH 8.5, 30°C, recombinant wild-type enzyme
0.13
NAD+
pH 8.5, 30°C, recombinant mutant S205D
0.14
NAD+
mutant L36T, pH 8.5, 25°C
0.14
NAD+
pH 8.0, 25°C, recombinant mutant L36T
0.143
NAD+
-
enzyme form E6.6, pH 9
0.15
NAD+
-
wild-type enzyme
0.18
NAD+
-
free enzyme, at pH 8.6 and 25°C
0.18
NAD+
-
free enzyme,25°C, pH 8.6
0.19
NAD+
mutant N313T and Y317G
0.2
NAD+
-
pH 8.0, 25°C, tetrameric enzyme form, mutant D282G
0.23
NAD+
-
poly(ethylene glycol)-bound NAD+
0.255
NAD+
pH and temperature not specified in the publication
0.26
NAD+
free enzyme, at pH 7.5 and 25°C
0.26
NAD+
free enzyme,25°C, pH 8.6
0.28
NAD+
recombinant enzyme, pH and temperature not specified in the publication
0.29
NAD+
-
pH 8.0, 25°C, tetrameric enzyme form, mutant T34Q/T39S/L43Q
0.299
NAD+
pH 8.5, 30°C, recombinant mutant S124A
0.33
NAD+
mutant enzyme S186G
0.362
NAD+
mutant enzyme F37G, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.362
NAD+
mutant F36G, pH 8.8, 25°C
0.366
NAD+
Q81X74, YP_027084
pH 8.6, temperature not specified in the publication
0.366
NAD+
Q81X74, YP_027084
at pH 8.5, temperature not specified in the publication
0.417
NAD+
mutant enzyme F37T, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.417
NAD+
mutant F36T, pH 8.8, 25°C
0.45
NAD+
-
glyoxysomal enzyme
0.47
NAD+
mutant D35G/L36T/T37K, pH 8.5, 25°C
0.47
NAD+
pH 8.0, 25°C, recombinant mutant D35G/L36T/T37K
0.47
NAD+
-
pH 8.0, 36°C, long torpor
0.5
NAD+
-
mutant enzyme D32A
0.5
NAD+
-
pH 8.0, 36°C, long torpor
0.5 - 1
NAD+
-
45°C, pH 7.8
0.527
NAD+
mutant enzyme F37L, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C
0.527
NAD+
mutant F36L, pH 8.8, 25°C
0.54
NAD+
mutant D35G, pH 8.5, 25°C
0.54
NAD+
pH 8.0, 25°C, recombinant mutant D35G
0.612
NAD+
pH 7.4, 37°C, recombinant enzyme
0.67
NAD+
immobilized enzyme reactor, at pH 7.5 and 25°C
0.67
NAD+
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
0.674
NAD+
-
GAPDH immobilized on an octyl silica column
0.75
NAD+
-
mutant enzyme D32A/L187N
0.75
NAD+
-
immobilized enzyme reactor, at pH 8.6 and 25°C
0.75
NAD+
-
enzyme covalently immobilized onto an electrophoresis fused-silica capillary, 25°C, pH 8.6
1
NAD+
-
mutant enzyme L187N
1.3
NAD+
-
pH 8.0, 5°C, euthermic
2.46
NAD+
-
poly(ethylene glycol)-bound NAD+
2.5
NAD+
-
pH 8.0, 25°C, tetrameric enzyme form, mutant N313T
35
NAD+
recombinant, highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
100
NAD+
glyceraldehyde-3-phosphate dehydrogenase, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C
312
NAD+
mutant enzyme C151S/H178N, pH 8.7, 25°C
316
NAD+
wild type enzyme, pH 8.7, 25°C
320
NAD+
mutant enzyme H178N, pH 8.7, 25°C
322
NAD+
mutant enzyme C151S, pH 8.7, 25°C
0.0033
NADH
-
-
0.007
NADH
-
cytosolic enzyme
0.02
NADH
-
glyoxysomal enzyme
0.061
NADH
wild type enzyme, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C
0.061
NADH
wild-type, pH 8.8, 25°C
0.367
NADH
mutant enzyme F37G, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C
0.367
NADH
mutant F36G, pH 8.8, 25°C
0.403
NADH
mutant enzyme F37T, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C
0.403
NADH
mutant F36T, pH 8.8, 25°C
0.537
NADH
mutant enzyme F37L, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C
0.537
NADH
mutant F36L, pH 8.8, 25°C
0.07
NADP+
mutant D35G/L36T/T37K/P192S, pH 8.5, 25°C
0.1
NADP+
mutant D35G/L36T/P192S, pH 8.5, 25°C
0.1
NADP+
mutant D35G/L36T/T37K, pH 8.5, 25°C
0.83
NADP+
mutant D35G, pH 8.5, 25°C
1.46
NADP+
mutant L36T, pH 8.5, 25°C
1.7
NADP+
-
mutant enzyme D32A/L187N
7.1
NADP+
-
mutant enzyme D32A and L187N
0.2
phosphate
-
isoenzyme I and II
0.53
phosphate
wild-type enzyme
1.25
phosphate
-
45°C, pH 7.8
2.54
phosphate
wild type enzyme, pH 8.7, 25°C
3.03
phosphate
mutant enzyme H178N, pH 8.7, 25°C
3.09
phosphate
mutant enzyme C151S, pH 8.7, 25°C
3.68
phosphate
mutant enzyme C151S/H178N, pH 8.7, 25°C
4
phosphate
-
pH 8.8, enzyme isolated of healthy patients
4.8
phosphate
mutant enzyme Y317A
6
phosphate
pH 8.0, temperature not specified in the publication, recombinant His-tagged wild-type enzyme
6.9
phosphate
mutant enzyme N313T/Y317G
7
phosphate
mutant enzyme E276G and mutant enzyme S48G
8
phosphate
mutant enzyme Y46G
8.3
phosphate
-
wild-type enzyme
9.6
phosphate
-
mutant enzyme W84F
9.9
phosphate
-
pH 8.8, enzyme isolated of sarcoma tissue
18
phosphate
mutant enzyme D186G
20
phosphate
mutant enzyme N313T
35.1
phosphate
mutant enzyme Y317G
37
phosphate
wild-type enzyme
0.0435
thio-NAD+
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
activity depends non-linearly on protein concentration in the range 0.00003-0.003 mM. With increasing concentrations the apparently hyperbolic substrate saturation curves turn into sigmoidal ones
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
kinetics, overview
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additional information
additional information
kinetics, overview
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additional information
additional information
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kinetic analysis and thermodynamics of purified euthermic and torpid enzyme
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additional information
additional information
kinetic isotope effects. The enzyme exhibits a kinetic mechanism in which first NAD+, then D-glyceraldehyde 3-phosphate bind to the active site resulting in the formation of a covalently bound thiohemiacetal intermediate. After oxidation of the thiohemiacetal and subsequent nucleotide exchange (NADH off, NAD+ on), the binding of inorganic phosphate and phosphorolysis yields the product 3-phospho-D-glyceroyl phosphate. Solvent and multiple kinetic isotope effects revealed that the first halfreaction is rate limiting and utilizes a step-wise mechanism for thiohemiacetal oxidation via a transient alkoxide to promote hydride transfer and thioester formation. steady-state kinetics
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additional information
additional information
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the enzyme presents allosteric positive cooperativity for substrates NAD+ and D-glyceraldehyde 3-phosphate, kinetic analysis, overview
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additional information
additional information
the mammalian enzyme shows negative cooperativity
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additional information
additional information
the recombinant protein shows no cooperativity towards glyceraldehyde 3-phosphate as a substrate, Michaelis-Menten kinetics with glyceraldehyde 3-phosphate as a substrate
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additional information
additional information
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the recombinant protein shows no cooperativity towards glyceraldehyde 3-phosphate as a substrate, Michaelis-Menten kinetics with glyceraldehyde 3-phosphate as a substrate
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additional information
additional information
the sperm-specific isoenzyme of glyceraldehyde-3-phosphate dehydrogenase exhibits strong positive cooperativity in coenzyme binding, kinetics, overview
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additional information
additional information
the sperm-specific isoenzyme of glyceraldehyde-3-phosphate dehydrogenase exhibits strong positive cooperativity in coenzyme binding, kinetics, overview
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additional information
additional information
enzyme kinetics, the recombinant enzyme exhibits about 6fold higher Km value toward 1,3-bisPGA compared to Ga3P. kcat in the way of Ga3P oxidation is about 5fold higher than in the opposite direction, thus resulting in a similar catalytic efficiency (kcat/Km) of the enzyme for the forward and the reverse reactions
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additional information
additional information
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enzyme kinetics, the recombinant enzyme exhibits about 6fold higher Km value toward 1,3-bisPGA compared to Ga3P. kcat in the way of Ga3P oxidation is about 5fold higher than in the opposite direction, thus resulting in a similar catalytic efficiency (kcat/Km) of the enzyme for the forward and the reverse reactions
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evolution
both GAPDS and GAPD are homotetramers with the sequence identity of about 70%. They are encoded by different genes which have emerged after duplication of the original gene during the early evolution of chordates
evolution
both GAPDS and GAPD are homotetramers with the sequence identity of about 70%. They are encoded by different genes which have emerged after duplication of the original gene during the early evolution of chordates. The GAPDS gene is lost by most lineages, and specialized to a testis-specific protein in reptilians and mammals
evolution
cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a phylogenetically conserved, ubiquitous enzyme
evolution
convergent evolution in GapA/B and GapC1, plastid GapC1 and GapA represent two independent cases of functional divergence and adaptations to the Calvin cycle entailing a shift in subcellular targeting and a shift in binding preference from NAD+ to NADPH. Comparisons between GapA sequences and cytosolic GAPDH and GapC1 and cytosolic GAPDH sequences (Gap2, GapA, GapB, or GapC1) to identify possible functionally divergent sites, homology modeling, phylogenetic tree, detailed overview
evolution
the sequence of the isozyme uracil-DNA glycosylase, UDG polypeptide (331 amino acids), differs from the sequence of classical GAPDH (335 amino acids) by the substitution of the residues 194-213 and the deletion of the residues 328-330. The amino acid sequence of the GAPDH isoform UDG because of its activity is hardly connected with alternative splicing of GAPDH pre-mRNA. The UDG region with the altered amino acids 194-213 is situated within the exon far from its boundaries. It appears to be a result of the single-nucleotide deletion in the GAPDH gene exon, causing the shift of the reading frame. Downstream to this region, there is theadditional deletion of 2 nucleotides in the UDG sequence, leading to restoration of the initial reading frame. The observed discrepancies in the sequences of these proteins are likely due to a sequencing error. Interestingly, the altered region belongs to the GAPDH glyceraldehyde-3-phosphate-binding site not participating in DNA binding
evolution
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molecular phylogenetic tree using sequences from 26 GAPDH proteins from 12 species of Aspergillus and 8 species of Trichoderma genus
evolution
molecular phylogenetic tree using sequences from 26 GAPDH proteins from 12 species of Aspergillus and 8 species of Trichoderma genus
evolution
sequence comparisons
evolution
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molecular phylogenetic tree using sequences from 26 GAPDH proteins from 12 species of Aspergillus and 8 species of Trichoderma genus
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evolution
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sequence comparisons
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evolution
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sequence comparisons
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evolution
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sequence comparisons
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evolution
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sequence comparisons
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malfunction
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FAO hepatoma cells with mutations of all 4 lysine residues (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state show reduced GAPDH glycolytic activity and glycolytic flux and increased gluconeogenic GAPDH activity and glucose production. Hepatic expression of mutant 4K-R-GAPDH in mice increases GAPDH gluconeogenic activity and the contribution of gluconeogenesis to endogenous glucose production in the unfed state. Consistent with the increased reliance on the energy-consuming gluconeogenic pathway, plasma free fatty acids and ketones are elevated inmice expressing 4K-RGAPDH, suggesting enhanced lipolysis and hepatic fatty acid oxidation. GAPDH acetylation is reduced in obese and type 2 diabetic db/db mice
malfunction
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GAPDH knockdown abolishes cADPR-induced Ca2+ release. GAPDH knockdown markedly inhibits NPE-cADPR- or PALcIDPRE-induced cytosolic Ca2+ increase in Jurkat cells, RyR3-expressing HEK-293 cells, or human coronary artery smooth muscle cells. Washing saponin-treated cells with PBS abolishes cADPR-induced colocalization of GAPDH with ryanodine receptors, RyRs
malfunction
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GAPDH-deficient cells are more sensitive to bleomycin or methyl methanesulfonate. In cells challenged with these genotoxic agents, GAPDH deficiency results in reduced cell viability and filamentous growth
malfunction
GAPDHS inhibitor effects on sperm motility and metabolism, overview
malfunction
GAPDHS inhibitor effects on sperm motility and metabolism, overview
malfunction
inhibition of GAPDH leads to substantially reduced energy generation
malfunction
knockout or overexpression of GAPC isozymes causes significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Two double knockout seeds show over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
malfunction
substitution of Phe34 with smaller side chain (e.g. Gly or Leu), or polar residue (e.g. Thr) abolishes the NAD+ binding affinity, or reduce the protein's catalytic efficiency
malfunction
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TDH3 deletion or overexpression does not affect overall cellular NAD+ levels, but affects nuclear NAD+ levels in yeast
malfunction
transcriptomic and metabolomic analyses indicate that the lack of GAPCp activity affects nitrogen and carbon metabolism as well as mineral nutrition and that glycerate and glutamine are the main metabolites responding to GAPCp activity, phenotypic analysis, detailed overview. Mutants gapcp1gapcp2 display a drastic reduction not only of root growth but also of the aerial part (AP) when grown both on plates and in greenhouse conditions. This phenotype is observed in double homozygous mutants only. Single mutants (gapcp1 or gapcp2) or mutant plants homozygous for one of the genes and heterozygous for the other are phenotypically indistinguishable from the wild-type plants. At the adult stage, GAPCp1 expression in the AP is able to complement the sterile phenotype of gapcp1gapcp2, resulting in plants with siliques and fertile seeds. The developmental pattern of gapcp1gapcp2 RBCS:GAPCp1 is also altered as compared with gapcp1gapcp2, probably as a consequence of the fertile phenotype, displaying shorter shoots than gapcp1gapcp2. A similar developmental pattern alteration is observed in the sterile gapcp1gapcp2 35S:GAPCp1 lines
malfunction
transcriptomic and metabolomic analyses indicate that the lack of GAPCp activity affects nitrogen and carbon metabolism as well as mineral nutrition and that glycerate and glutamine are the main metabolites responding to GAPCp activity, phenotypic analysis, detailed overview. Mutants gapcp1gapcp2 display a drastic reduction not only of root growth but also of the aerial part when grown both on plates and in greenhouse conditions. This phenotype is observed in double homozygous mutants only. Single mutants (gapcp1 or gapcp2) or mutant plants homozygous for one of the genes and heterozygous for the other are phenotypically indistinguishable from the wild-type plants
malfunction
knockdown of GAPDHS in uveal melanoma (UM) cell lines hinders glycolysis by decreasing glucose uptake, lactate production, ATP generation, cell growth and proliferation. Conversely, overexpression of GAPDHS promotes glycolysis, cell growth and proliferation. Transcription factor SOX10 knockdown reduces the activation of GAPDHS, leading to an attenuated malignant phenotype, and SOX10 overexpression promotes the activation of GAPDHS, leading to an enhanced malignant phenotype. Mechanistically, SOX10 exerts its function by binding to the promoter of GAPDHS to regulate its expression. Importantly, SOX10 abrogation suppresses in vivo tumor growth and proliferation
malfunction
RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. Genetic manipulation of gapdh1 and gapdh2 affects the biomass and total fatty acid of Mortierella alpina through an altered NADPH/NADP ratio
malfunction
RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. MA-RGAPDH2 is found to strengthen the metabolic flux of dihydroxyacetone phosphate to glycerol-3-phosphate. Genetic manipulation of gapdh1 and gapdh2 affects the biomass and total fatty acid of Mortierella alpina through an altered NADPH/NADP ratio
malfunction
Tyr-Asp inhibition of glyceraldehyde 3-phosphate dehydrogenase affects plant redox metabolism. Tyr-Asp inhibits the activity of a key glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPC), and redirects glucose toward pentose phosphate pathway (PPP) and NADPH production. Tyr-Asp supplementation improves the growth performance of both Arabidopsis and tobacco seedlings subjected to oxidative stress conditions. Neither the combination of Tyr and Asp nor the two other tested dipeptides, Ser-Leu and Gly-Pro, exhibit the bioactivity of Tyr-Asp. Tyr-Asp treatment, but neither the combination of amino acids nor the two other tested dipeptides improves plant performance under stress conditions. Tyr-Asp supplementation increases biomass of catechin-treated wild-type seedlings. The Tyr-Asp-associated stress tolerance is dependent on the inhibition of the GAPC1 and GAPC2 activities. Proteome characterization of the Tyr-Asp feeding experiment revealed changes in protein and redox metabolism consistent with the Tyr-Asp protein interactions beyond that with GAPC, Tyr-Asp affects redox and protein metabolism, phenotypes, overview
malfunction
Tyr-Asp inhibition of glyceraldehyde 3-phosphate dehydrogenase affects plant redox metabolism. Tyr-Asp inhibits the activity of a key glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPC), and redirects glucose toward pentose phosphate pathway (PPP) and NADPH production. Tyr-Asp supplementation improves the growth performance of both Arabidopsis and tobacco seedlings subjected to oxidative stress conditions. Neither the combination of Tyr and Asp nor the two other tested dipeptides, Ser-Leu and Gly-Pro, exhibit the bioactivity of Tyr-Asp. Tyr-Asp treatment, but neither the combination of amino acids nor the two other tested dipeptides improves plant performance under stress conditions. Tyr-Asp supplementation increases biomass of catechin-treated wild-type seedlings. The Tyr-Asp-associated stress tolerance is dependent on the inhibition of the GAPC1 and GAPC2 activities. Proteome characterization of the Tyr-Asp feeding experiment revealed changes in protein and redox metabolism consistent with the Tyr-Asp protein interactions beyond that with GAPC, Tyr-Asp affects redox and protein metabolism, phenotypes, overview
malfunction
when the cell is exposed to high levels of H2O2, GAPDH is irreversibly inhibited presumably by the formation of sulphenic acid in the active site cysteine, becoming a switch that balances the equilibrium between the glycolytic cycle and the pentose phosphate metabolic pathway and promoting the formation of NADPH to combat ROS-produced cell stress
malfunction
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RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. Genetic manipulation of gapdh1 and gapdh2 affects the biomass and total fatty acid of Mortierella alpina through an altered NADPH/NADP ratio
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malfunction
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RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. MA-RGAPDH2 is found to strengthen the metabolic flux of dihydroxyacetone phosphate to glycerol-3-phosphate. Genetic manipulation of gapdh1 and gapdh2 affects the biomass and total fatty acid of Mortierella alpina through an altered NADPH/NADP ratio
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malfunction
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knockout or overexpression of GAPC isozymes causes significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Two double knockout seeds show over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
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malfunction
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FAO hepatoma cells with mutations of all 4 lysine residues (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state show reduced GAPDH glycolytic activity and glycolytic flux and increased gluconeogenic GAPDH activity and glucose production. Hepatic expression of mutant 4K-R-GAPDH in mice increases GAPDH gluconeogenic activity and the contribution of gluconeogenesis to endogenous glucose production in the unfed state. Consistent with the increased reliance on the energy-consuming gluconeogenic pathway, plasma free fatty acids and ketones are elevated inmice expressing 4K-RGAPDH, suggesting enhanced lipolysis and hepatic fatty acid oxidation. GAPDH acetylation is reduced in obese and type 2 diabetic db/db mice
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malfunction
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TDH3 deletion or overexpression does not affect overall cellular NAD+ levels, but affects nuclear NAD+ levels in yeast
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metabolism
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GAPDH is not involved in the control of the glycolytic flux. A strain overproducing GAPDH shows a high NADH-to-NAD+ ratio, but no significant differences in growth rate when grown on glucose or lactose
metabolism
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replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase by Clostridium acetobutylicum GapC glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.9 results in significant reduction of flux through the pentose phosphate pathway. Recombinant strains display increased NADPH availability, and consistently higher productivity than parent strains
metabolism
the enzyme is involved in glycolysis
metabolism
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a key enzyme of glycolysis, catalyses the oxidative phosphorylation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate using NAD+ as the co-enzyme
metabolism
GAPCp might be an important metabolic connector of glycolysis with other pathways, such as the phosphorylated pathway of serine biosynthesis, the ammonium assimilation pathway, or the metabolism of gamma-aminobutyrate, which in turn affect plant development
metabolism
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GAPDH is a component of a multiprotein complex that repairs DNA lesions through the base excision repair pathway
metabolism
GAPDH not only catalyses the sixth step of glycolysis, but is also implicated in multiple nonmetabolic processes. Glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes. Astrocytic energy metabolism controls D-serine production, thereby influencing glutamatergic neurotransmission in the hippocampus, overview. Involvement of glycolysis in modulating D-serine levels
metabolism
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glyceraldehyde-3-phosphate dehydrogenase, GAPDH, is a key enzyme of glycolysis
metabolism
plastidial isozyme GAPCp might be an important metabolic connector of glycolysis with other pathways, such as the phosphorylated pathway of serine biosynthesis, the ammonium assimilation pathway, or the metabolism of gamma-aminobutyrate, which in turn affect plant development
metabolism
the EMP pathway can be controlled through the glyceraldehyde 3-phosphate node by NAD+-GAPDH activity, recombinant NADP+-GAPDH heterologous activity can also exert a similar response, which modulates the glucose uptake and also the acetic acid production rate
metabolism
the enzyme is involved in glycolysis catalyzing a key reaction
metabolism
the enzyme is involved in glycolysis, the glycolytic conversion of glucose to pyruvic acid
metabolism
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anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
metabolism
different roles of GAPDH1 and GAPDH2 in lipid biosynthesis in Mortierella alpina
metabolism
different roles of GAPDH1 and GAPDH2 in lipid biosynthesis in Mortierella alpina. The GAPDH2 might be a moonlighting protein
metabolism
enzyme GAPDHS is essential in glycolysis
metabolism
glyceraldehyde 3-phosphate dehydrogenase (FgGAPDH) is a key enzyme of the glycolytic pathway
metabolism
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate
metabolism
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is the sixth enzyme in the glycolytic pathway, in which it converts D-glyceraldehyde 3-phosphate (D-G3P) to 1,3-bisphosphoglycerate and consumes inorganic phosphate using NAD+ as a coenzyme
metabolism
glyceraldehyde-3-phosphate dehydrogenase is a critical metabolic enzyme in the stony coral Acropora millepora
metabolism
in the cytosol, two different GAPDHs are involved in glycolysis, the phosphorylating NAD+-dependent GAPDH (GAPC1 and GAPC2, EC 1.2.1.12) and the non-phosphorylating, NADP+-dependent GAPDH (GAPN, EC 1.2.1.9). GAPN irreversibly oxidizes G3P to 3-phosphoglycerate (3PGA) and has no homology to GAPC. Besides their role in carbon assimilation and partitioning, phosphorylating GAPDHs (particularly, GAPC1 and GAPA1) have additional moonlighting functionalities
metabolism
in the cytosol, two different GAPDHs are involved in glycolysis, the phosphorylating NAD+-dependent GAPDH (GAPC1 and GAPC2; EC 1.2.1.12) and the non-phosphorylating, NADP+-dependent GAPDH (GAPN, EC 1.2.1.9). GAPN irreversibly oxidizes G3P to 3-phosphoglycerate (3PGA) and has no homology to GAPC. Besides their role in carbon assimilation and partitioning, phosphorylating GAPDHs (particularly, GAPC1 and GAPA1) have additional moonlighting functionalities
metabolism
in the cytosol, two different GAPDHs are involved in glycolysis, the phosphorylating NAD+-dependent GAPDH (GAPC1 and GAPC2; EC 1.2.1.12) and the non-phosphorylating, NADP+-dependent GAPDH (GAPN, EC 1.2.1.9). GAPN irreversibly oxidizes G3P to 3-phosphoglycerate (3PGA) and has no homology to GAPC. Besides their role in carbon assimilation and partitioning, phosphorylating GAPDHs (particularly, GAPC1 and GAPA1) have additional moonlighting functionalities
metabolism
mechanism of NADH-channeling from D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to L-lactate dehydrogenase (LDH). Enzyme kinetics studies show that LDH activity with free NADH and GAPDH-NADH complex always take place in parallel. The channeling is observed only in assays that mimic cytosolic conditions where free NADH concentration is negligible and the GAPDH-NADH complex is dominant. Molecular dynamics and protein-protein interaction studies show that LDH and GAPDH can form a leaky channeling complex only at the limiting NADH concentrations. Surface calculations show that positive electric field between the NAD(H) binding sites on LDH and GAPDH tetramers can merge in the LDH-GAPDH complex. NAD(H)-channeling within the LDH-GAPDH complex can be an extension of NAD(H)-channeling within each tetramer. In the case of a transient LDH-(GAPDH-NADH) complex, the relative contribution from the channeled and the diffusive paths depends on the overlap between the off-rates for the LDH-(GAPDH-NADH) complex and the GAPDH-NADH complex. The GAPDH complex can be observed in cell extracts, and with purified proteins in conditions that mimic high protein concentrations in cytosol
metabolism
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the enzyme is important in the carbon metabolism in plant leaves, overview
metabolism
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is the sixth enzyme in the glycolytic pathway, in which it converts D-glyceraldehyde 3-phosphate (D-G3P) to 1,3-bisphosphoglycerate and consumes inorganic phosphate using NAD+ as a coenzyme
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metabolism
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different roles of GAPDH1 and GAPDH2 in lipid biosynthesis in Mortierella alpina
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metabolism
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different roles of GAPDH1 and GAPDH2 in lipid biosynthesis in Mortierella alpina. The GAPDH2 might be a moonlighting protein
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metabolism
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the enzyme is involved in glycolysis catalyzing a key reaction
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metabolism
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the enzyme is involved in glycolysis
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metabolism
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a key enzyme of glycolysis, catalyses the oxidative phosphorylation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate using NAD+ as the co-enzyme
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metabolism
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glyceraldehyde-3-phosphate dehydrogenase, GAPDH, is a key enzyme of glycolysis
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metabolism
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is the sixth enzyme in the glycolytic pathway, in which it converts D-glyceraldehyde 3-phosphate (D-G3P) to 1,3-bisphosphoglycerate and consumes inorganic phosphate using NAD+ as a coenzyme
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physiological function
a GAPDH-deficient mutant can still grow in medium with glucose or other sugars as the sole carbon source, and no phosphofructokinase activity is detectable.The mutant can not utilize pyruvate as sole carbon source, whereas the wild-type can. Inactivation of GAPDH results in impairment of bacterial growth and virulence in the host plant, and reduction of intracellular ATP and extracellularpolysaccharide
physiological function
double mutants lacking both plastidial isoforms gapcp1 and gapcp2 display a drastic phenotype of arrested root development, dwarfism, and sterility. In spite of their low gene expression level, GAPCp down-regulation leads to altered gene expression and to drastic changes in the sugar and amino acid balance of the plant. GAPCps are important for the synthesis of serine in roots. Serine supplementation to the growth medium rescues root developmental arrest and restores normal levels of carbohydrates and sugar biosynthetic activities in gapcp double mutants
physiological function
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downregulation of GAPDH using siRNA reduces both macrophage colony stimulating factor CSF-1 mRNA and protein levels, through destabilizing CSF-1 mRNA. CSF-1 mRNA half-lives are decreased by 50% in the presence of GAPDH siRNA. GAPDH associates with a large AU-rich containing regionof CSF-1
physiological function
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gapc-1 null mutant line shows a delay in growth, morpholigical alterations in siliques, and low seed number. Embryo development is altered, showing abortions and empty embryonic sacs in basal and apical siliques, respectively. Mutant shows a decrease in ATP levels and reduced respiratory rate as well as a decrease in the expression and activity of aconitase and succinate dehydrogenase and reduced levels of pyruvate and several Krebs cycle intermediates, and increased reactive oxygen species levels
physiological function
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GAPDH controls generation of H2O2 by the proapoptotic family member Bax and heat shock, which in turn suppresses cell death in yeast and plant cells
physiological function
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GAPDH is a translational suppressor of angiotensin II type 1 receptor expression and mediates the effect of H2O2 on angiotensin II type 1 receptor mRNA
physiological function
GAPDH physically associates with DNA repair enzyme APE1. This interaction allows GAPDH to convert the oxidized species of APE1 to the reduced form, thereby reactivating its endonuclease activity to cleave abasic sites
physiological function
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interaction of GAPDH with Porphyromonas gingivalis major fimbrae plays an important role in Porphyromonas gingivalis colonization. Amino acid residues 166 to 183 of Streptococcus oralis GAPDH exhibit the strongest binding activity toward rFimA, and the synthetic peptide corresponding to amino acid residues 166 to 183 of GAPDH, peptide DNFGVVEGLMTTIHAYTG inhibits Streptococcus oralis-Porphyromonas gingivalis biofilm formation in a dose-dependent manner. The peptide inhibits interbacterial biofilm formation by several oral streptococci and Porphyromonas gingivalis strains with different types of FimA
physiological function
reduction of transcription by 41% and 67% using RNAi leads to transformants with sluggish motility and less active than wild-type
physiological function
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the adhesion mechanism of the lactobacilli is in part due to GAPDH binding to human ABO-type blood group antigens expressed on human colonic mucin. After periodate oxidation of colonic mucin, adhesion of Lactobacillus plantarum LA 318 bacterial cells significantly decreases compared to normal human colonic mucin. High binding is observed to A and B group antigens, while binding to H group antigen is lower. No interaction is observed between GAPDH and various monosaccharides. GAPDH binding to the B-trisaccharide biotinyl polymer probe [Gala1-3 (Fuca1-2) Gal-] is significantly higher as compared to B-disaccharide, Lewis D-trisaccharide, 3-fucosyl-N-acetylglucosamine and a-N-acetylneuraminic acid biotinyl polymer-probes
physiological function
the GAPDH gene product is a heat shock protein which might be involved in the developmental phase of the Lentinus polychrous
physiological function
cadmium-induced stress in seedlings roots induces nitric oxide accumulation, cytosolic oxidation, activation of the GAPC1 promoter, GAPC1 protein accumulation in enzymatically inactive form, and strong relocalization of GAPC1 to the nucleus. All the effects are detected in the same zone of the root tip. In vitro, GAPC1 is inactivated by either nitric oxide donors or hydrogen peroxide, but no inhibition is directly provided by cadmium
physiological function
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deletion mutants of isoforms TDH1, TDH2, TDH3 show decreased enzymic activity following the trend ?tdh3>?tdh2>?tdh1 in both YEPD or YEPE medium. TDH3 encodes the major GAPDH isoenzyme. The GAPDH total activity is significantly lower in all genotypes grown on ethanol in comparison with the activity on glucose. A downregulation of GAPDH activity does not contribute to improved performance of engineered Saccharomyces cerevisiae on pentose substrates
physiological function
enzyme shows high affinity for Porphyromonas gingivalis proteins tonB-dependent receptor protein RagA4, 4-hydroxybutyryl-coenzyme A dehydratase AbfD, GAPDH, NAD-dependent glutamate dehydrogenase GDH, and malate dehydrogenase MDH. tonB-Dependent receptor protein RagA4, 4-hydroxybutyryl-coenzyme A dehydratase AbfD and NAD-dependent glutamate dehydrogenase GDH enhance coaggregation, whereas GAPDH and malate dehydrogenase inhibite coaggregation
physiological function
Q81X74, YP_027084
human plasminogen predominantly interacts with the GapA isoform at physiological concentrations and the interaction is lysine dependent
physiological function
knockout or overexpression of isoforms GapC1 and GapC2 causes significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Double knockout seeds have about 3% of dry weight decrease in oil content compared with wild type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild type and the fatty acid composition is altered. These transgenic lines exhibit decreased fertility. Seed-specific overexpression lines have more than 3% increase in seed oil without compromised seed yield or fecundity
physiological function
when endogenous phosphorylating NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Corynebacterium glutamicum is replaced by nonphosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (GapN) from Clostridium acetobutylicum, this NADPH-generating glycolytic pathway does not allow for the growth of Corynebacterium glutamicum with glucose as the sole carbon source. Heterologous expression of udhA encoding soluble transhydrogenase from Escherichia coli partly restores growth
physiological function
plastidial isozymes GAPCps are critical for primary root growth and essential for microspore development. Plastidial isozyme GAPCp1 is not functionally important in photosynthetic cells but plays a fundamental role in roots and in heterotrophic cells of the aerial part. GAPCp1 expression in reproductive organs is necessary for Arabidopsis fertility. GAPCp activity may be required in root meristems and the root cap for normal primary root growth. GAPCp might be an important metabolic connector of glycolysis with other pathways, such as the phosphorylated pathway of serine biosynthesis, the ammonium assimilation pathway, or the metabolism of gamma-aminobutyrate, which in turn affect plant development. Isozymes GAPCp1 and GAPCp2 are redundant to one another
physiological function
the plastidial GAPCps are critical for primary root growth and essential for microspore development. Plastidial isozyme GAPCp might be an important metabolic connector of glycolysis with other pathways, such as the phosphorylated pathway of serine biosynthesis, the ammonium assimilation pathway, or the metabolism of gamma-aminobutyrate, which in turn affect plant development. Isozymes GAPCp1 and GAPCp2 are redundant to one another
physiological function
apurinic/apyrimidinic (AP) sites are some of the most frequent DNA damages and the key intermediates of base excision repair. Certain proteins can interact with the deoxyribose of the AP site to form a Schiff base, which can be stabilized by NaBH4 treatment. The enzyme interacts with single-stranded AP DNA and AP DNA duplex with both 5' and 3' dangling ends. The protein forming this adduct is an isoform of glyceraldehyde-3-phosphate dehydrogenase called uracil-DNA glycosylase. GAPDH, at least partially, is covalently linked with the AP site by a mechanism other than the Schiff base formation. In spite of the ability to form a Schiff-base intermediate with the deoxyribose of the AP site, GAPDH does not display the AP lyase activity. In addition, along with the borohydride-dependent adducts with AP DNAs containing single-stranded regions, GAPDH was also shown to form the stable borohydride-independent crosslinks with these AP DNAs. GAPDH crosslinks preferentially to AP DNAs cleaves via the beta-elimination mechanism (spontaneously or by AP lyases) as compared to DNAs containing the intact AP site. The level of GAPDH-AP DNA adduct formation depends on oxidation of the protein SH-groups. Disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA
physiological function
apurinic/apyrimidinic (AP) sites are some of the most frequent DNA damages and the key intermediates of base excision repair. Certain proteins can interact with the deoxyribose of the AP site to form a Schiff base, which can be stabilized by NaBH4 treatment. The enzyme interacts with single-stranded AP DNA and AP DNA duplex with both 5' and 3' dangling ends. The protein forming this adduct is an isoform of glyceraldehyde-3-phosphate dehydrogenase called uracil-DNA glycosylase. GAPDH, at least partially, is covalently linked with the AP site by a mechanism other than the Schiff base formation. In spite of the ability to form a Schiff-base intermediate with the deoxyribose of the AP site, GAPDH does not display the AP lyase activity. In addition, along with the borohydride-dependent adducts with AP DNAs containing single-stranded regions, GAPDH was also shown to form the stable borohydride-independent crosslinks with these AP DNAs. GAPDH crosslinks preferentially to AP DNAs cleaves via the beta-elimination mechanism (spontaneously or by AP lyases) as compared to DNAs containing the intact AP site. The level of GAPDHAP DNA adduct formation depends on oxidation of the protein SH-groups. Disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA
physiological function
cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a phylogenetically conserved, ubiquitous enzyme that plays an indispensable role in energy metabolism. The extracellular GAPDH in human serum is a multimeric, high-molecular-weight, yet glycolytically active enzyme, the enzymatic function of serum GAPDH remained unaffected by the multimers
physiological function
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diverse functions of GAPDH, including roles in membrane trafficking, apoptosis, and autophagy in addition to GAPDH's canonical role within the glycolytic and gluconeogenic pathways. In this capacity it converts D-glyceraldehyde-3-phosphate and NAD+ to 1,3-bisphosphoglycerate and NADH in the glycolytic pathway, or the reverse reaction in the gluconeogenic pathway. GAPDH plays a central role in carbohydrate metabolismin ground squirrels, which typically shift to non-carbohydrate fuels during winter hibernation, stable suppression of GAPDH (possibly by some reversible posttranslational modification) during ground squirrel torpor, which likely contributes to the overall reduction in carbohydrate metabolism when these animals switch to lipid fuels during dormancy. GAPDH regulation by reversible phosphorylation
physiological function
enzyme Gapdh is likely to have multiple nonglycolytic functions in the parasite in additon to its function in glycolysis. During intra-erythrocytic phage of its life cycle in humans, the parasite solely relies on glycolysis for its energy needs
physiological function
enzyme Gapdh is likely to have multiple nonglycolytic functions in the parasite in additon to its function in glycolysis. During intra-erythrocytic phage of its life cycle in humans, the parasite solely relies on glycolysis for its energy needs. PfGapdh appearing on the parasite cell surface can bind to extracellular proteins for moonlighting functions due to its specific interactions with with Pfeno, plasminogen, alpha-tubulin and lysozyme
physiological function
enzyme GAPDH plays a key role in glycolysis and gluconeogenesis by catalyzing the reversible oxidative phosphorylation of D-glyceraldehyde 3-phosphate to the energy-rich intermediate glyceraldehyde 1,3-bisphosphate
physiological function
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GAPDH is required for the efficient repair of DNA lesions in Escherichia coli. Interaction occur between GAPDH and enzymes of the base excision repair pathway, namely the AP-endonuclease Endo IV and uracil DNA glycosylase. GAPDH is a component of a protein complex dedicated to the maintenance of genomic DNA integrity. Interaction of GAPDH with the single-stranded DNA binding protein may recruit GAPDH to the repair sites and implicates GAPDH in DNA repair pathways activated by profuse DNA damage, such as homologous recombination or the SOS response.
physiological function
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GAPDH plays essential role in glycolysis and gluconeogenesis as a housekeeping enzyme. Cyclic adenosine diphosphoribose (cADPR), an endogenous nucleotide derived from NAD+, mobilizes Ca2+ release from endoplasmic reticulum via ryanodine receptors (RyRs). cADPR interacts directly with enzyme GAPDH and induces the transient interaction between GAPDH and RyRs in vivo, without cADPR the interaction is weak. GAPDH is required for cADPR-mediated Ca2+ mobilization from endoplasmic reticulum via RyRs. cADPR-mediated Ca2+ signaling pathway is involved in a wide variety of cellular processes,1 e.g. abscisic acid signaling, calorie restriction in gut stem cell, circadian clock in plants, and long-term synaptic depression in hippocampus
physiological function
glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses one of the two steps in glycolysis which generate the reduced coenzyme NADH. This reaction precedes the two ATP generating steps
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 NADH are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme of the glycolytic pathway, reversibly catalyzing the sixth step of glycolysis and concurrently reducing the coenzyme NAD+ to NADH
physiological function
glyceraldehyde-3-phosphate dehydrogenase is an essential enzyme in the glycolytic pathway. GAPDH also displays a range of other functions unrelated to its glycolytic function. GAPDH is a 3'-AU-rich element-binding protein, it can selectively bind to AU-rich +element, RNA recognition mechanism, overview. NAD1 inhibition for GAPDH3 RNA binding capability indicates that GAPDH3 likely binds to the AU-rich or polyadenosine RNA substrates through its NAD+-binding domain in vitro
physiological function
glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, GAPDHS, is a sperm-specific glycolytic enzyme involved in energy production during spermatogenesis and sperm motility
physiological function
glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, GAPDHS, is a sperm-specific glycolytic enzyme involved in energy production during spermatogenesis and sperm motility
physiological function
glycolytic flux controls D-serine synthesis through glyceraldehyde-3-phosphate dehydrogenase in astrocytes. D-Serine production in astrocytes is modulated by the interaction between the D-serine synthetic enzyme serine racemase (SRR) and a glycolytic enzyme, glyceraldehyde 3-phosphate dehydrogenase (GAPDH). In primary cultured astrocytes, glycolysis activity is negatively correlated with D-serine level. SRR interacts directly with GAPDH, and activation of glycolysis augments this interaction. GAPDH suppresses SRR activity by direct binding to GAPDH and through NADH, a product of GAPDH. NADH allosterically inhibits the activity of SRR by promoting the disassociation of ATP from SRR
physiological function
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plastidial glyceraldehyde-3-phosphate dehydrogenase GAPCp is not functionally significant in photosynthetic cells, but GAPCp activity expression in root tips is necessary for primary root growth, its expression in heterotrophic cells of aerial parts and roots is necessary for plant growth and development. GAPCp is an important metabolic connector of carbon and nitrogen metabolism through the phosphorylated pathway of serine biosynthesis, role of the pathway in the control of plant growth and development, overview. 3-Phospho-D-glyceroyl phosphate is converted into acetyl-coA in plastids, which is used for the biosynthesis of fatty acids
physiological function
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possible role of NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase in growth promotion of Arabidopsis seedlings by low levels of selenium. The pro-growth effect of selenium arises enhancing mitochondrial performance in a GSH-dependent manner, in which NAD-GAPDH may serve as a key regulator
physiological function
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reversible post-translational modification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), particularly acetylation, contributes to the reciprocal regulation of glycolysis/gluconeogenesis. Lysine post-translational modification of glyceraldehyde-3-phosphate dehydrogenase regulates hepatic and systemic metabolism
physiological function
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Tdh3, an NAD+-binding protein, influences nuclear NAD+ levels. Tdh3 links nuclear Sir2 with NAD+ from the cytoplasm
physiological function
the C-terminal domain of human host cell glyceraldehyde 3-phosphate dehydrogenase plays an important role in suppression of tRNALys3 packaging into human immunodeficiency virus type-1 particles. Human immunodeficiency virus type-1 (HIV-1) requires the packaging of human tRNALys3 as a primer for effective viral reverse transcription. The binding of human GAPDH to Pr55gag is important for the suppression mechanism, and residues Asp256, Lys260, Lys263 and Glu267 of GAPDH are essential for the suppression of tRNALys3 packaging. The C-terminal domain of GAPDH (151-335) interacts with both the matrix region (MA, 1-132) and capsid N-terminal domain (CANTD, 133-282)
physiological function
the enzyme inhibits complement function as measured by haemolytic assay and membrane attack complex (MAC) formation, C3-binding property of Haemonchus contortus GAPDH is an additional function of the enzyme, and it represents another entity of complement-binding protein. Key role of the protein in immune modulation
physiological function
the enzyme is involved in glycolysis, the pathway plays an important role in tumor cells
physiological function
the enzyme of the human pathogen binds hemoglobin and heme, it is a heme-binding protein and might be playing a dynamic role in the success of the invasive and infective processes of this pathogen
physiological function
the enzyme plays a central role in glycolysis, and nonglycolytic processes such as nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis
physiological function
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the significance of D-glyceraldehyde-3-phosphate dehydrogenase is not restricted to its pivotal glycolytic function. GAPDH localized in the nucleus can be involved in numerous processes: regulation of the length of telomeres, DNA repair, gene expression, and regulation of cyclin functions. GAPDH may act as a specific scaffold for cytoskeleton-associated proteins independently of its catalytic activity
physiological function
two cytosolic GAPC isozymes play important roles in cellular metabolism and seed oil accumulation. GAPC levels play important roles in the overall cellular production of reductants, energy, and carbohydrate metabolites, and GAPC levels are directly correlated with seed oil accumulation
physiological function
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a 13C signal (i.e. systematic 13C/12C variation) at tree-ring glucose C-4 signal seems to be introduced by glyceraldehyde-3-phosphate dehydrogenases in the cytosol of leaves, which means commitment of glyceraldehyde 3-phosphate to 3-phosphoglycerate versus fructose 1,6-bisphosphate metabolism, and the contribution of non-phosphorylating versus phosphorylating glyceraldehyde-3-phosphate dehydrogenase to catalysing the glyceraldehyde 3-phosphate to 3-phosphoglycerate forward reaction of glycolysis. Modelling of the cytosolic oxidation-reduction (COR) cycle, a carbon-neutral mechanism supplying NADPH at the expense of ATP and NADH, which may help to maintain leaf-cytosolic redox balances. Carbon isotope fractionation by glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is modelled. A positive correlation between air vapour pressure deficit and 13C discrimination at glucose C-4 is observed
physiological function
apart from its glycolytic function, GAPDH displays a battery of moonlighting activities. Primary location of the tetrameric GAPDH is in the cytoplasm, where it conducts its canonical role in glycolysis
physiological function
cytosolic glyceraldehyde-3-phosphate dehydrogenase (NAD-GAPDH) is involved in a critical energetic step of glycolysis and also has many important functions besides its enzymatic activity. NAD-GAPDH enzyme catalyzes the phosphorylating-coupled oxidation of glyceraldehyde 3-phosphate. Its catalytic role in glycolysis is based on a highly reactive catalytic cysteine that is often target of oxidative modifications that blocks its enzymatic activity and in turns trigger other moonlighting non-glycolytic roles. NAD-GAPDH is phosphorylated in vivo, the enzyme depicts different activity, abundance and phosphorylation profiles during development of seeds that mainly accumulate lipids (castor oil seed). In castor oil seed, the activity slightly increased and total protein levels do not significantly change in the first half of seed development but both abruptly decreases in the second part of development, when triacylglycerol synthesis and storage begin
physiological function
cytosolic glyceraldehyde-3-phosphate dehydrogenase (NAD-GAPDH) is involved in a critical energetic step of glycolysis and also has many important functions besides its enzymatic activity. NAD-GAPDH enzyme catalyzes the phosphorylating-coupled oxidation of glyceraldehyde 3-phosphate. Its catalytic role in glycolysis is based on a highly reactive catalytic cysteine that is often target of oxidative modifications that blocks its enzymatic activity and in turns trigger other moonlighting non-glycolytic roles. NAD-GAPDH is phosphorylated in vivo, the enzyme depicts different activity, abundance and phosphorylation profiles during development of seeds that mainly accumulate starch (wheat). NAD-GAPDH activity gradually increases along wheat seed development, but protein levels and phosphorylation status exhibit only slight changes
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyses the conversion of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate using NAD+ as a cofactor. It is a moonlighting enzyme playing multiple roles in the regulation of mRNA stability, intracellular membrane trafficking, iron uptake and transport, DNA replication and repair, and nuclear RNA transport
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme, whose main role is to provide energy for different cellular functions. Also the enzyme appears to be involved in numerous cell processes that have no relation to glycolysis
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional enzyme that plays critical roles in bacterial pathogenesis in some pathogenic bacteria
physiological function
in Fasciola gigantica, the glyceraldehyde 3-phosphate dehydrogenase (FgGAPDH) is a key enzyme of the glycolytic pathway and catalyzes the reversible oxidative phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate, with the simultaneous reduction of NAD+ to NADH. The enzyme has various roles in the parasite
physiological function
isozyme GAPDH1 contributes to NADPH supply and lipid accumulation in Mortierella alpina, and has a distinct role from isozyme GAPDH2. Transcriptional analysis of genes gapdh1 and gapdh2 shows that they have opposing roles during lipid accumulation. GAPDH1 possesses a stronger catalyzing ability than GAPDH2
physiological function
Mycobacterium tuberculosis relocates several housekeeping proteins to the cell surface for capture and internalization of host iron carrier protein transferrin. One of the identified receptors is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Mycobacterium tuberculosis glyceraldehyde-3-phosphate dehydrogenase (GAPDH) functions as a receptor for human lactoferrin. Human lactoferrin is sequestered at the bacterial surface by GAPDH. The enzyme is a virulence factor in the bacterium. Iron is chelated by the siderophore and transported via specific iron regulated transporters
physiological function
sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDHS) switches glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate by coupling with the reduction of NAD+ to NADH. The sperm-specific glycolysis enzyme is regulated by transcription factor SOX10 to promote uveal melanoma (UM) tumorigenesis. GAPDHS, which is regulated by SOX10, controls glycolysis and contributes to UM tumorigenesis. GAPDHS is involved in regulating the Warburg effect in UM cells. GAPDHS serves as a functional target gene in SOX10-mediated tumor proliferation and glycolysis in UM
physiological function
the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
physiological function
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the adhesion mechanism of the lactobacilli is in part due to GAPDH binding to human ABO-type blood group antigens expressed on human colonic mucin. After periodate oxidation of colonic mucin, adhesion of Lactobacillus plantarum LA 318 bacterial cells significantly decreases compared to normal human colonic mucin. High binding is observed to A and B group antigens, while binding to H group antigen is lower. No interaction is observed between GAPDH and various monosaccharides. GAPDH binding to the B-trisaccharide biotinyl polymer probe [Gala1-3 (Fuca1-2) Gal-] is significantly higher as compared to B-disaccharide, Lewis D-trisaccharide, 3-fucosyl-N-acetylglucosamine and a-N-acetylneuraminic acid biotinyl polymer-probes
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physiological function
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the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
-
physiological function
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional enzyme that plays critical roles in bacterial pathogenesis in some pathogenic bacteria
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physiological function
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isozyme GAPDH1 contributes to NADPH supply and lipid accumulation in Mortierella alpina, and has a distinct role from isozyme GAPDH2. Transcriptional analysis of genes gapdh1 and gapdh2 shows that they have opposing roles during lipid accumulation. GAPDH1 possesses a stronger catalyzing ability than GAPDH2
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physiological function
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the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
-
physiological function
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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 NADH are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
-
physiological function
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glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, GAPDHS, is a sperm-specific glycolytic enzyme involved in energy production during spermatogenesis and sperm motility
-
physiological function
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two cytosolic GAPC isozymes play important roles in cellular metabolism and seed oil accumulation. GAPC levels play important roles in the overall cellular production of reductants, energy, and carbohydrate metabolites, and GAPC levels are directly correlated with seed oil accumulation
-
physiological function
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Mycobacterium tuberculosis relocates several housekeeping proteins to the cell surface for capture and internalization of host iron carrier protein transferrin. One of the identified receptors is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Mycobacterium tuberculosis glyceraldehyde-3-phosphate dehydrogenase (GAPDH) functions as a receptor for human lactoferrin. Human lactoferrin is sequestered at the bacterial surface by GAPDH. The enzyme is a virulence factor in the bacterium. Iron is chelated by the siderophore and transported via specific iron regulated transporters
-
physiological function
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reversible post-translational modification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), particularly acetylation, contributes to the reciprocal regulation of glycolysis/gluconeogenesis. Lysine post-translational modification of glyceraldehyde-3-phosphate dehydrogenase regulates hepatic and systemic metabolism
-
physiological function
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the GAPDH gene product is a heat shock protein which might be involved in the developmental phase of the Lentinus polychrous
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physiological function
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Mycobacterium tuberculosis relocates several housekeeping proteins to the cell surface for capture and internalization of host iron carrier protein transferrin. One of the identified receptors is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Mycobacterium tuberculosis glyceraldehyde-3-phosphate dehydrogenase (GAPDH) functions as a receptor for human lactoferrin. Human lactoferrin is sequestered at the bacterial surface by GAPDH. The enzyme is a virulence factor in the bacterium. Iron is chelated by the siderophore and transported via specific iron regulated transporters
-
physiological function
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glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
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physiological function
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Tdh3, an NAD+-binding protein, influences nuclear NAD+ levels. Tdh3 links nuclear Sir2 with NAD+ from the cytoplasm
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physiological function
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the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
-
physiological function
-
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional enzyme that plays critical roles in bacterial pathogenesis in some pathogenic bacteria
-
physiological function
-
the protein CbbG is a glyceraldehyde-3-phosphate (Ga3P) dehydrogenase (Ga3PDHase) catalyzing the reversible oxidation of Ga3P to 1,3-bis-phospho-glycerate (1,3bisPGA), using specifically NAD+/NADH as cofactor. CbbG seems to be the only Ga3PDHase present in Nitrosomonas europaea, which is involved in reducing triose phosphate during autotrophic carbon fixation. Otherwise, in cells grown under conditions deprived of ammonia and oxygen, the enzyme can catalyze the glycolytic step of Ga3P oxidation producing NADH
-
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 NADH are generated at this enzymatic reaction with the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate
-
physiological function
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enzyme Gapdh is likely to have multiple nonglycolytic functions in the parasite in additon to its function in glycolysis. During intra-erythrocytic phage of its life cycle in humans, the parasite solely relies on glycolysis for its energy needs. PfGapdh appearing on the parasite cell surface can bind to extracellular proteins for moonlighting functions due to its specific interactions with with Pfeno, plasminogen, alpha-tubulin and lysozyme
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additional information
comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
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detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
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detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
importance of Phe34 in NAD+ binding, Phe34 is stabilized in the presence of NAD+ but displays greater mobility in its absence. The oxidative state of the active site Cys149 residue is regulated by NAD+ binding, because this residue is found oxidized in the absence of dinucleotide. The distance between Cys149 and His176 decreases upon NAD binding and Cys149 remains in a reduced state when NAD+ is bound, cofactor binding and active site structures, catalytic mechanism, overview
additional information
kinetic and chemical mechanism of Mtb-GAPDH, overview. C158 is the active site nucleophile reacting with the aldehyde group of D-glyceraldehyde 3-phosphate to generate the thiohemiacetal and H185 is additionally required to either stabilize thiolate anion formation or act as a catalytic acid/base group
additional information
molecular docking simulation
additional information
molecular modeling of FhGAPDH monomer, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers
additional information
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molecular modeling of FhGAPDH monomer, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers
additional information
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possible existence of actin/active GAPDH dimer complexes similar to 3-phosphoglycerate kinase/active GAPDH dimer complexes
additional information
sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS, is stabilized by additional proline residues and an interdomain salt bridge. Residues P164, P326, and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at expense of the catalytic activity. Comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS, is stabilized by additional proline residues and an interdomain salt bridge. Residues P164, P326, and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at expense of the catalytic activity. Comparison of the sequences of muscle GAPD and sperm GAPDS isozymes reveals seven additional proline residues in the catalytic part of GAPDS
additional information
the enzyme's catalytic domain interrupts interacting sites in the NAD+-binding domain of GAPDH
additional information
the phosphate group of the substrate is bound to the phosphate site in all four subunits, adenosyl binding pocket structure, comparison of group B Streptococcus ternary complex of enzyme with substrate and cofactor with human structure, comparative structure-function analysis of GBS GAPDH and hGAPDH, conformational changes upon ligand binding, overview. The active site residue Cys152 is positioned between the nicotinamide moiety of NAD+ and the side chain of active site residue His179
additional information
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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
denatured GAPDH, in contrast to the native enzyme, interacts with the bacterial chaperonin GroEL and beta-amyloid peptide 1-42
additional information
-
denatured GAPDH, in contrast to the native enzyme, interacts with the bacterial chaperonin GroEL and beta-amyloid peptide 1-42
additional information
docking analysis of cofactor NAD+ and substrate glyceraldehyde 3-phosphate, identification and structure analysis of the binding sites, overview. Enzyme structure homology modeling using the structure of NAD+ bound BmGAPDH from Brugia malayi (PDB ID 4K9D) as template
additional information
-
docking analysis of cofactor NAD+ and substrate glyceraldehyde 3-phosphate, identification and structure analysis of the binding sites, overview. Enzyme structure homology modeling using the structure of NAD+ bound BmGAPDH from Brugia malayi (PDB ID 4K9D) as template
additional information
docking and molecular dynamics simulations of the interaction between rabbit muscle GAPDH and rabbit muscle or porcine heart LDH, structure analysis and calculation of the rm(ph)LDH-rmGAPDH complex, overview. Multiscale MD calculations and molecular docking studies showed that rmLDH and rmGAPDH can form a dynamic complex facing each other with their NAD(H) binding sites. The complex breaks apart when the two enzymes are saturated with NAD(H) molecules. The complex breaks apart when the two enzymes are saturated with NAD(H) molecules. When rmLDH and rmGAPDH form a complex, the positive cavities on the surface of each enzyme merge to form a central positive cavity under the protein surface. The cavity connects four NAD(H) binding sites with an average separation of 2.9 nm between the adjacent sites. Thus, NADH channeling within the rmLDH-rmGAPDH complex can be an extension of NADH channeling between the two adjacent monomers in rmLDH and rmGAPDH tetramers. Analysis of interaction between phLDH and byGAPDH by analytical ultracentrifugation, on velocity experiments for detection of interaction between phLDH and byGAPDH. It is a transient protein-protein interactions and NADH channeling in cells
additional information
each GAPDH monomer contains a molecule of glyceraldehyde-3 phosphate in a non-previously identified site. The catalytic Cys149 is covalently attached to an about 300 Da molecule, possibly glutathione. This modification alters the conformation of an adjacent alpha-helix in the catalytic domain, right opposite to the NAD+ binding site. The conformation of the alpha-helix is stabilized after soaking the crystals with NAD+. Enzyme structure analysis, structure modeling, detailed overview
additional information
phosphate ion-binding sites structure analysis. Superimposition of GBS GAPDH and a ternary complex of GBS GAPDH (PDB ID 5jya), structure comparisons of ligand-binding state and of ternary complex enzyme and apoenzyme, implications for the catalytic mechanism, overview
additional information
proteogenic dipeptides act as evolutionarily conserved small-molecule regulators at the nexus of stress, protein degradation, and metabolism
additional information
proteogenic dipeptides act as evolutionarily conserved small-molecule regulators at the nexus of stress, protein degradation, and metabolism
additional information
proteogenic dipeptides act as evolutionarily conserved small-molecule regulators at the nexus of stress, protein degradation, and metabolism
additional information
proteogenic dipeptides act as evolutionarily conserved small-molecule regulators at the nexus of stress, protein degradation, and metabolism
additional information
structure homology modeling of GAPDH using the tetrameric GAPDH structure from Bacillus stearothermophilus (PDB ID 1GD1) as template. The glycine-valine-asparagine tripeptide sequence (at positions 140, 141, and 142 respectively) is highly conserved in several GAPDH homologues
additional information
the GAPDH enzyme from the reef-building stony coral Acropora millepora is a rather typical eukaryotic GAPDH, comprising an N-terminal NAD+-binding Rossman fold and a catalytic domain that provides important active site residues
additional information
the S-loop of GAPDH is required for interaction of the enzyme with its cofactor and with other proteins. NAD+-bound GAPDH S-loop fixation occurs by the formation of a complex with the coenzyme NAD+. The structure of trehalose-bound ecGAPDH is compared with the structures of both NAD+-free and NAD+-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD+-free ecGAPDH structure and a 3.1° rotation compared with the NAD+-bound ecGAPDH structure
additional information
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the S-loop of GAPDH is required for interaction of the enzyme with its cofactor and with other proteins. NAD+-bound GAPDH S-loop fixation occurs by the formation of a complex with the coenzyme NAD+. The structure of trehalose-bound ecGAPDH is compared with the structures of both NAD+-free and NAD+-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD+-free ecGAPDH structure and a 3.1° rotation compared with the NAD+-bound ecGAPDH structure
additional information
three-dimensional structure analysis of EcGAPDH1 compared with the structures of HuGAPDH and MrsaGAPDH shows that the main difference is the loop conformation, especially the S-loop
additional information
-
three-dimensional structure analysis of EcGAPDH1 compared with the structures of HuGAPDH and MrsaGAPDH shows that the main difference is the loop conformation, especially the S-loop
additional information
-
phosphate ion-binding sites structure analysis. Superimposition of GBS GAPDH and a ternary complex of GBS GAPDH (PDB ID 5jya), structure comparisons of ligand-binding state and of ternary complex enzyme and apoenzyme, implications for the catalytic mechanism, overview
-
additional information
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kinetic and chemical mechanism of Mtb-GAPDH, overview. C158 is the active site nucleophile reacting with the aldehyde group of D-glyceraldehyde 3-phosphate to generate the thiohemiacetal and H185 is additionally required to either stabilize thiolate anion formation or act as a catalytic acid/base group
-
additional information
-
structure homology modeling of GAPDH using the tetrameric GAPDH structure from Bacillus stearothermophilus (PDB ID 1GD1) as template. The glycine-valine-asparagine tripeptide sequence (at positions 140, 141, and 142 respectively) is highly conserved in several GAPDH homologues
-
additional information
-
structure homology modeling of GAPDH using the tetrameric GAPDH structure from Bacillus stearothermophilus (PDB ID 1GD1) as template. The glycine-valine-asparagine tripeptide sequence (at positions 140, 141, and 142 respectively) is highly conserved in several GAPDH homologues
-
additional information
-
phosphate ion-binding sites structure analysis. Superimposition of GBS GAPDH and a ternary complex of GBS GAPDH (PDB ID 5jya), structure comparisons of ligand-binding state and of ternary complex enzyme and apoenzyme, implications for the catalytic mechanism, overview
-
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heteromer
-
GAPDH-AnBn heteromer of GapA and GapB subunits
heterotetramer
-
A2B2-GAPDH, light conformation, B subunits are almost identical to A subunits, expect for the presence of a C-terminal extension containing a pair of cysteines, which is the target of TRX regulation
multimer
-
A8B8-GAPDH, dark conformation, B subunits are almost identical to A subunits, expect for the presence of a C-terminal extension containing a pair of cysteines, which is the target of TRX regulation
octamer
-
8 * 43000, pentalenolactone-insensitive enzyme, gel filtration
?
-
x * 37600, calculated and SDS-PAGE
?
Q81X74, YP_027084
x * 40000, SDS-PAGE
?
-
x * 35500 + x * 37000, SDS-PAGE
?
-
x * 35000, high speed equilibrium sedimentation after treatment with 5 M guanidine hydrochloride containing 0.01 M dithiothreitol
?
x * 36446, calculated from amino acid sequence
?
x * 36446, calculated, x * 38000, SDS-PAGE
?
x * 14000, SDS-PAGE, probably truncated form, x * 37000, native enzyme, SDS-PAGE, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 35470, apo-form of GADPH isozyme uracil-DNA glycosylase, mass spectrometry
?
x * 75000, about, recombinant enzyme, SDS-PAGE, x * 45000-50000, native enzyme, SDS-PAGE
?
x * 75000, about, recombinant enzyme, SDS-PAGE, x * 45000-50000, native enzyme, SDS-PAGE
?
-
x * 75000, about, recombinant enzyme, SDS-PAGE, x * 45000-50000, native enzyme, SDS-PAGE
-
?
-
x * 36000, about, sequence determination and analysis
?
-
x * 36000, about, sequence determination and analysis
-
?
x * 27000 + x * 37000 + x * 51000, SDS-PAGE
?
-
x * 27000 + x * 37000 + x * 51000, SDS-PAGE
-
?
x * 35914, calculated from sequence
?
-
x * 36100, calculated
-
?
-
x * 14000 + x * 37000, SDS-PAGE
?
x * 37600, calculated, x * 37500, SDS-PAGE
?
-
x * 37600, calculated, x * 37500, SDS-PAGE
-
dimer
-
x-ray crystallography
dimer
2 * 37000, about, sequence calculation, ligands bound
dimer
-
1 * 58000 + 1 * 61000, enzyme form E6.6, SDS-PAGE
dimer
-
the final crystallographic model consists of a dimer
homodimer
2 * 36200, recombinant enzyme, SDS-PAGE
homodimer
-
2 * 36200, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 36200, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 36200, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 36200, recombinant enzyme, SDS-PAGE
-
homotetramer
-
homotetramer
-
GAPDH-A4, homotetramer GapA subunits
homotetramer
4 * 36000, SDS-PAGE
homotetramer
-
4 * 37000, SDS-PAGE
homotetramer
-
4 * 36500, non-denaturing PAGE
homotetramer
x-ray crystallography
homotetramer
4 * 37000, recombinant His-tagged enzyme, SDS-PAGE
homotetramer
4 * 38000, SDS-PAGE
homotetramer
4 * 40000, N-terminally truncated enzyme after trypsin treatment, SDS-PAGE
homotetramer
4 * 37672, MALDI-TOF mass spectrometry
homotetramer
4 * 37000, about, SDS-PAGE
homotetramer
4 * 37000, about, SDS-PAGE
homotetramer
-
4 * 37000, about
homotetramer
-
4 * 37000, SDS-PAGE
homotetramer
4 * 36000, SDS-PAGE
homotetramer
-
4 * 36000, SDS-PAGE
-
homotetramer
-
4 * 36000, SDS-PAGE
-
homotetramer
-
4 * 50000, SDS-PAGE
homotetramer
-
4 * 51000, native PAGE slab gels with varying acrylamide concentrations of 5-10% (w/v) in the absence of SDS
homotetramer
-
4 * 50000, SDS-PAGE
-
homotetramer
-
4 * 51000, native PAGE slab gels with varying acrylamide concentrations of 5-10% (w/v) in the absence of SDS
-
homotetramer
4 * 37000, SDS-PAGE
homotetramer
4 * 36636, wild-type enzyme, sequence calculation, 4 * 40000, about, recombinant N-terminally prolongated enzyme, SDS-PAGE, 4 * 40355, recombinant N-terminally prolongated enzyme, sequence calculation
homotetramer
4 * 37000, SDS-PAGE
homotetramer
SDS-PAGE and gel filtration
homotetramer
-
4 * 37000, denaturing SDS-PAGE
homotetramer
-
4 * 38500, non-denaturing PAGE
homotetramer
-
GAPDH-A4, homotetramer GapA subunits
homotetramer
functional GAPDH is a homotetramer, with each monomer composed of two domains: the N-terminal coenzyme binding domain and the C-terminal catalytic domain. The catalytic domain contains the Ps and Pi sites, which bind the C(3) phosphate of the substrate and the inorganic phosphate ion, respectively, during the phosphorylation step carried out by the enzyme. The S-loop folds over in close proximity to the bound cofactor, modelling
homotetramer
x-ray crystallography
homotetramer
-
x-ray crystallography
homotetramer
-
x-ray crystallography
-
homotetramer
a dimer of dimers, 4 * 44000, about, SDS-PAGE
homotetramer
4 * 36830, MALDI-TOF mass spectrometry
homotetramer
-
4 * 36830, MALDI-TOF mass spectrometry
-
homotetramer
4 * 37000, SDS-PAGE
monomer
1 * 36000, SDS-PAGE
monomer
1 * 45000, SDS-PAGE, isozyme uracil-DNA glycosylase, enzyme as adduct with AP DNA
monomer
-
1 * 36000, SDS-PAGE
monomer
1 * 45000, SDS-PAGE, isozyme uracil-DNA glycosylase
monomer
1 * 38000, SDS-PAGE, 1 * 38760, mass spectrometry
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
-
4 * 36000, SDS-PAGE
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
4 * 38500, SDS-PAGE
tetramer
-
4 * 36000, SDS-PAGE
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
4 * 32400, engineered recombinant enzyme, SDS-PAGE, 4 * 35500, non-modified wild-type enzyme, SDS-PAGE
tetramer
each of the subunits can be divided into two domains: the N-terminal NAD+-binding domain and the C-terminal catalytic domain. The NAD+-binding domain is typically a Rossman fold containing eight beta-strands, namely beta1 (Lys3-Asn7), beta2 (Asp28-Asn33), beta3 (Val58-Phe60), beta4 (Ser64-Val67), beta5 (Lys70-Tyr75), beta6 (Ile92-Glu95), beta7 (Lys116-Ile119) and beta8 (Ile144-Ser146). The strands are connected by either helices or short loops. beta3 and beta5 are antiparallel to the other six parallel beta-strands. There are four alpha-helices in this domain: alpha1 (Gly10-Val23), alpha2 (Ser37-His47), alpha3 (Ser102-Ser106) and alpha4 (Gln107-Ala112). The catalytic domain contains eight mixed beta-sheets, beta9 (Ile168-Ala178), beta10 (Ile205-His207), beta11 (Leu226-Val231), beta12 (Ser239-Leu247), beta13 (Phe270-Thr273), beta14 (Ser289-Asp292), beta15 (Glu297-Val301) and beta16 (Leu304-Tyr313), and three long alpha-helices, alpha5 (Ser149-Gly167), alpha6 (Thr252-Thr264) and alpha7 (Gln317-Lys332). The catalytically active residues Cys150 and His177 are situated in alpha5 and beta9, respectively
tetramer
-
4 * 37000, SDS-PAGE
tetramer
4 * 37000, about, sequence calculation and modeling
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
-
4 * 36000, SDS-PAGE
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
-
4 * 38000, cetyltrimethyl ammonium bromide PAGE
tetramer
-
4 * 38000, cetyltrimethyl ammonium bromide PAGE
-
tetramer
-
4 * 36000, SDS-PAGE
tetramer
-
4 * 29500, enzyme form E8.5, SDS-PAGE
tetramer
-
x * 36000 + x * 38000, enzyme form E6.8, SDS-PAGE
tetramer
-
4 * 33000, enzyme form E9.5, SDS-PAGE
tetramer
N-terminally truncated mutant, crystallization data
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
-
determined by gel filtration
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
-
sedimentation analysis
tetramer
-
4 * 36000-37000, SDS-PAGE
tetramer
4 * 37000, SDS-PAGE
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
-
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
-
tetramer
4 * 41000, SDS-PAGE
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
4 * 35000, SDS-PAGE
tetramer
4 * 37000, dimer of dimer, SDS-PAGE
tetramer
-
4 * 37000, dimer of dimer, SDS-PAGE
-
tetramer
-
4 * 37000, dimer of dimer, SDS-PAGE
-
tetramer
-
4 * 43000, pentalenolactone-sensitive enzyme, gel filtration
tetramer
-
4 * 38000, SDS-PAGE
tetramer
-
4 * 38000, glyoxysomal enzyme, SDS-PAGE
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
4 * 36000, SDS-PAGE
tetramer
-
4 * 33500, SDS-PAGE
tetramer
-
4 * 33700, SDS-PAGE
tetramer
-
4 * 33700, SDS-PAGE
-
tetramer
-
4 * 38000, GAPDH I and GAPDH II, SDS-PAGE
tetramer
-
4 * 38000, glyoxysomal enzyme, SDS-PAGE
tetramer
-
4 * 33500, cytosolic enzyme, SDS-PAGE
tetramer
-
4 * 36000, SDS-PAGE
tetramer
-
4 * 36000, SDS-PAGE
-
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
4 * 40000-42000, SDS-PAGE
additional information
enzyme can bind top a partial gene sequence of NADP-dependent malated dehydrogenase EC 1.2.1.37
additional information
enzyme can bind top a partial gene sequence of NADP-dependent malated dehydrogenase EC 1.2.1.37
additional information
-
enzyme can bind top a partial gene sequence of NADP-dependent malated dehydrogenase EC 1.2.1.37
additional information
structure analysis, overview. Dual side-chain conformations are observed in Ser207 in subunits of O, Q, and R of the bGAPDH(NAD)3
additional information
purified recombinant FhGAPDH is a mixture of homodimers and tetramers, as judged by protein-protein crosslinking and analytical gel filtration. The addition of either NAD+ or glyceraldehyde 3-phosphate shifts this equilibrium towards a compact dimer, that is more stable than the unliganded one. Molecular modeling of FhGAPDH monomer, and of the enzyme as a tetramer, the quaternary structure is shown as a dimer of dimers arrangement, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers
additional information
-
purified recombinant FhGAPDH is a mixture of homodimers and tetramers, as judged by protein-protein crosslinking and analytical gel filtration. The addition of either NAD+ or glyceraldehyde 3-phosphate shifts this equilibrium towards a compact dimer, that is more stable than the unliganded one. Molecular modeling of FhGAPDH monomer, and of the enzyme as a tetramer, the quaternary structure is shown as a dimer of dimers arrangement, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers
additional information
dimers generated from the tetrameric enzyme are inactive but exhibit cooperativity in NAD+ binding
additional information
-
dimers generated from the tetrameric enzyme are inactive but exhibit cooperativity in NAD+ binding
additional information
isolation of a truncated form of the protein from the excretory-secretory products of the parasite worms using C3-affinity chromatography, and identification by mass spectroscopy as glyceraldehyde-3-phosphate dehydrogenase, GAPDH
additional information
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isolation of a truncated form of the protein from the excretory-secretory products of the parasite worms using C3-affinity chromatography, and identification by mass spectroscopy as glyceraldehyde-3-phosphate dehydrogenase, GAPDH
additional information
-
recombinant GAPDH binds directly with high affinity to a single-stranded oligonucleotide comprising three telomeric DNA repeats. Nucleotides T1, G5, and G6 of the TTAGGG repeat are essential for binding.The stoichiometry of the interaction is 2:1 DNA:GAPDH, and GAPDH appears to form a high-molecular-weight complex when bound to the oligonucleotide
additional information
-
recombinant glyceraldehyde 3-phosphate dehydrogenase binds to hepatitis B virus regulatory element RNA in vitro and inhibits hepatitis B virus regulatory element function. Overexpression of glyceraldehyde 3-phosphate dehydrogenase depresses the expression of hepatitis B virus antigen
additional information
GAPDH is composed of two folding domains, an NAD+-binding domain (residues 2-150) and a catalytic domain (residues 155-312)
additional information
high-molecular-weight multimers of serum GAPDH, multiple protein bands (about 25, and 50-75 kDa) along with some proteins with weak signals in albumin-depleted serum samples, SDS-PAGE and mass spectrometry. The enzymatic function of serum GAPDH remained unaffected by the multimers
additional information
molecular docking simulation
additional information
the residues P164 (beta-turn), P326 (first position of alpha-helix), and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at the expense of the catalytic activity. The N-terminal domain is hidden inside the cytoskeleton structures and does not interact with the catalytic part of the enzyme
additional information
the residues P164 (beta-turn), P326 (first position of alpha-helix), and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at the expense of the catalytic activity. The N-terminal domain is hidden inside the cytoskeleton structures and does not interact with the catalytic part of the enzyme
additional information
three GAPDS-specific salt bridges, E96-H394 and D311-H124 connect the NAD+-binding and the catalytic domains within a single subunit, while E244-R320 is formed between two different subunits
additional information
three GAPDS-specific salt bridges, E96-H394 and D311-H124 connect the NAD+-binding and the catalytic domains within a single subunit, while E244-R320 is formed between two different subunits
additional information
human GAPDH identified by peptide mass fingerprinting and mass spectrometric analysis
additional information
-
human GAPDH identified by peptide mass fingerprinting and mass spectrometric analysis
additional information
-
peptide mapping, mass spectrometry, overview
additional information
-
enzyme exists as an equilibrium mixture of different oligomeric states. Rapid equilibrium between monomer - dimer - tetramer, the tetramer is inactive
additional information
-
non-native forms of GAPDH obtained by cold denaturation, oxidation of the enzyme, or its unfolding in guanidine hydrochloride efficiently bind to soluble amyloid-beta peptide (1-42) yielding a stable complex. Native tetrameric GAPDH does not interact with soluble amyloid-beta peptide (1-42), neither non-native forms of GAPDH interact with aggregated amyloid-beta peptide (1-42)
additional information
-
the CgGAP protein consists of an N-terminal NAD+-binding domain and a central catalytic domain
additional information
-
the CgGAP protein consists of an N-terminal NAD+-binding domain and a central catalytic domain
additional information
-
the CgGAP protein consists of an N-terminal NAD+-binding domain and a central catalytic domain
-
additional information
the 51 kDa enzyme form is present only in the soluble fraction of the cell extract
additional information
-
the 51 kDa enzyme form is present only in the soluble fraction of the cell extract
additional information
-
the 51 kDa enzyme form is present only in the soluble fraction of the cell extract
-
additional information
-
subunit interactions are involved in regulation of activity
additional information
-
immobilized enzyme can exist as a trimer
additional information
quarternary structure analysis and comparisons, overview
additional information
-
quarternary structure analysis and comparisons, overview
additional information
subunits of the dimers form the major interface P, overview. The second largest interface, the R interface, includes residues in the N-terminal domain that interact with NAD+ and loop residues 181-206 in the C-terminal domain of subunit pairs A, C and B, D. The smallest interface, the Q interface, shows limited interactions between residues in the ranges 43-53 and 274-291 of adjacent subunits A, D and B, C
additional information
the enzyme crystal structure contains an asymmetric mixed holo tetramer (four copies of the GAPDH molecule in one asymmetric unit that form a tetramer or two dimers, namely the A-B dimer and the C-D dimer), with two NAD+ ligands bound to two protomers. The asymmetric dimers A-B of both structures can be aligned nearly perfectly, while the asymmetric dimers C-D are in very different conformations because of the different NAD+ binding states of the molecules. The molecular interfaces within both tetramers are essentially the same. Overall, the two tetramers are in different conformations owing to the different ligand-binding states of the four promoters
additional information
-
the enzyme crystal structure contains an asymmetric mixed holo tetramer (four copies of the GAPDH molecule in one asymmetric unit that form a tetramer or two dimers, namely the A-B dimer and the C-D dimer), with two NAD+ ligands bound to two protomers. The asymmetric dimers A-B of both structures can be aligned nearly perfectly, while the asymmetric dimers C-D are in very different conformations because of the different NAD+ binding states of the molecules. The molecular interfaces within both tetramers are essentially the same. Overall, the two tetramers are in different conformations owing to the different ligand-binding states of the four promoters
-
additional information
-
the enzyme crystal structure contains an asymmetric mixed holo tetramer (four copies of the GAPDH molecule in one asymmetric unit that form a tetramer or two dimers, namely the A-B dimer and the C-D dimer), with two NAD+ ligands bound to two protomers. The asymmetric dimers A-B of both structures can be aligned nearly perfectly, while the asymmetric dimers C-D are in very different conformations because of the different NAD+ binding states of the molecules. The molecular interfaces within both tetramers are essentially the same. Overall, the two tetramers are in different conformations owing to the different ligand-binding states of the four promoters
-
additional information
-
interaction of GAPDH with Porphyromonas gingivalis major fimbrae plays an important role in Porphyromonas gingivalis colonization. Amino acid residues 166 to 183 of Streptococcus oralis GAPDH exhibit the strongest binding activity toward rFimA, and the synthetic peptide corresponding to amino acid residues 166 to 183 of GAPDH, peptide DNFGVVEGLMTTIHAYTG inhibits Streptococcus oralis-Porphyromonas gingivalis biofilm formation in a dose-dependent manner. The peptide inhibits interbacterial biofilm formation by several oral streptococci and Porphyromonas gingivalis strains with different types of FimA
additional information
enzyme modeling
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C155S
nuclear relocalization of GAPC1 under cadmium-induced oxidative stress is stimulated, rather than inhibited, by mutation of the catalytic cysteine C155
C159S
the mutant C159S of the isozyme GapC2 shows decreased specific activity
D32A
-
activity of mutant enzyme D32A with NAD+ is equal to that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 3% of the activity with NAD+
D32A/L187N
-
wild-type enzyme has no activity with NADP+, the mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+
L187N
-
activity of mutant L187N with NAD+ is higher than that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 7% of the activity with NAD+
D35G
-
mutation enables GAPDH to accept both NAD and NADP
-
D35G/L36R/P192S
-
mutant accepts both Nad AND nadp WITH SIMILAR EFFICINCY
-
D35G/L36T/T37K
-
catalytic efficiency with NADP is about 10fold hihger than with NAD
-
D35G/L36T/T37K/P192S
-
Mutant shows the highest catalytic efficiency with NADP while the catalytic efficiency with NAD also increases
-
L36T
-
mutation enables GAPDH to accept both NAD and NADP
-
C153A
-
site-directed mutagenesis
N313T/Y317G
dissociation constant for NAD+ is 300times higher than that of the wild-type enzyme. Conformational equilibrium between the syn and the anti forms with a preference for the anti conformer
Y317A
dissociation constant for NAD+ is 5times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged
Y317G
dissociation constant for NAD+ is 13times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged
C149A
mutant enzyme displays no significant dehydrogenase activity
C149S
low but significant phosphorylating dehydrogenase activity
C149selenocysteine
-
mutant enzyme has selenoperoxidase activity
D186G
behavior in NAD+ binding is similar to that of the wild type enzyme
D186G/E276G
positive cooperativity in binding the coenzyme NAD+
D282G
-
enzyme exists as dimer and tetramer, the tetramer is inactive, the dimer is slightly active, 650fold decrease in turnover number for NAD+, 5.8fold increase in Km-value for NAD+ compared to wild-type enzyme
E276G
behavior in NAD+ binding is similar to that of the wild type enzyme
L187A/P188S
-
the mutant is catalytically active not only with NAD+, as the wild-type enzyme, but also with NADP+
N313T
-
mutant enzyme with a drastic decrease in thermostability, weakening of cooperative interactions between the catalytic and the cofactor domains and an inefficient binding of NAD+, mutant enzyme exists only as tetramer, 65fold decrease in turnover number for NAD+, 50fold increase in Km-value for NAD+ compared to wild-type enzyme
T34Q/T39S/L43Q
-
drastic decrease in thermostability, inefficient NAD+ binding, enzyme exists as dimer and tetramer, the tetramer is inactive, the dimer is slightly active, 650fold decrease in turnover number for NAD+, 4fold increase in Km-value for NAD+ compared to wild-type enzyme
W310F
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mutant enzyme with a drastic decrease in thermostability, mutant enzyme exists only as tetramer, 2fold increase of Km-value for NAD+, 1.3fold decrease in turnover number compared to wild-type enzyme
W84F
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slightly lower Km-values for NAD+ and glyceraldehyde 3-phosphate, slightly higher Km-value for phosphate. The construction of the mutant permitts the identification of the individual fluorescence and phosphorescence characteristics of the two Trp residues W84 and W310 in the native enzyme
Y283V
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mutant enzyme with a drastic decrease in thermostability, dimeric form is inactive, KM-value and turnover-number of tetramer are nearly identical to that of the wild-type
Y46G
behavior in NAD+ binding is similar to that of the wild type enzyme
Y46G/R52G
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inactive mutant enzyme, only exists as dimer
C149A
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mutant has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition
C152G
mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1
C156G
mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1
D234A
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site-directed mutagenesis
D256R/K260E
site-directed mutagenesis, the double mutation of GAPDH results in loss of detectable binding activity to wild-type capsid N-terminal domain
D256R/K260E/K263E/E267R
site-directed mutagenesis, multiple-substituted GAPDH mutant D256R/K260E/K263E/E267R retains the oligomeric formation with wild-type GAPDH in HIV-1 producing cells, but the incorporation level of the hetero-oligomer is decreased in viral particles. The viruses produced from cells expressing the D256R/K260E/K263E/E267R mutant restores tRNALys3 packaging efficiency because the mutant exerts a dominant negative effect by preventing wild-type GAPDH from binding to matrix region and capsid N-terminal domain and improves the reverse transcription
D256R/K260E/Q264A
site-directed mutagenesis, the mutant lacks the ability to bind to the wild-type capsid N-terminal domain
D256R/K260E/Q264A/E267R
site-directed mutagenesis, the mutant lacks the binding ability to the wild-type capsid N-terminal domain
D32A
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mutant is unable to bind NAD+, is enzymatically inactive and has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition
D356R
site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region
E267R
site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region
H179A
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site-directed mutagenesis, the KD value of cADPR to GAPDHHis179Ala mutant protein is markedly increased compared to wild-type GAPDH enzyme
K263E
site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region
P111A
site-directed mutagenesis, mutation at first position of alpha-helix
P157A
site-directed mutagenesis, mutation at first position of alpha-helix
P164A
site-directed mutagenesis, mutation at beta-turn, the mutant shows reduced thermostability and reduced resistance against guanidine hydrochloride. The Tm value of the heat-absorption curve decreases by 3.3°C compared to the wild-type protein
P197A
site-directed mutagenesis, mutation at beta-turn
P213A
site-directed mutagenesis, mutation at beta-turn
P326A
site-directed mutagenesis, mutation at first position of alpha-helix, the mutant shows reduced thermostability and reduced resistance against guanidine hydrochloride. The Tm value of the heat-absorption curve decreases by 6.0°C compared to the wild-type protein
A229V
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exhibits 50-55% residual activity in blood compared to the wild type enzyme
C281W
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exhibits 50-55% residual activity in blood compared to the wild type enzyme
G166D
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exhibits 50-55% residual activity in blood compared to the wild type enzyme
I308S
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exhibits 50-55% residual activity in blood compared to the wild type enzyme
V239I
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exhibits 50-55% residual activity in blood compared to the wild type enzyme
Y327N
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exhibits 50-55% residual activity in blood compared to the wild type enzyme
C158A
site-directed mutagenesis, inactive mutant
C162A
site-directed mutagenesis, the mutant exhibits a comparable Vmax to the wild-type enzyme and only a 2fold increased Km value for D-glyceraldehyde 3-phosphate
H185A
site-directed mutagenesis, inactive mutant
N142S
naturally occuring mutation, resulting in a non-significant structural change, since Ser at position 142 also shows a similar characteristic to the wild-type residues N142, experimentally the mutation results in a loss of enzyme activity
P295L
naturally occuring mutation
N142S
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naturally occuring mutation, resulting in a non-significant structural change, since Ser at position 142 also shows a similar characteristic to the wild-type residues N142, experimentally the mutation results in a loss of enzyme activity
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P295L
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naturally occuring mutation
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C158A
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site-directed mutagenesis, inactive mutant
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C162A
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site-directed mutagenesis, the mutant exhibits a comparable Vmax to the wild-type enzyme and only a 2fold increased Km value for D-glyceraldehyde 3-phosphate
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H185A
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site-directed mutagenesis, inactive mutant
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N142S
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naturally occuring mutation, resulting in a non-significant structural change, since Ser at position 142 also shows a similar characteristic to the wild-type residues N142, experimentally the mutation results in a loss of enzyme activity
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P295L
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naturally occuring mutation
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C149S
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treatment of with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide at 0.1 mM leads to low levels of aggregation (5% of wild type)
C149S/C281S
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mutant shows a complete absence of aggregation in the presence of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide
C153S
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aggregation can be detected at low concentrations of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (0.001 mM) and is enhanced at higher concentrations
C244A
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aggregation can be detected at low concentrations of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (0.001 mM) and is enhanced at higher concentrations
C281S
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the levels of aggregation in C281S are reduced to 45% of wild type at 0.1 mM (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide
F37G
the mutant shows strongly reduced kcat values compared to the wild type enzyme
F37L
the mutant shows strongly reduced kcat values compared to the wild type enzyme
F37T
the mutant shows strongly reduced kcat values compared to the wild type enzyme
F37G
substitution of residue F37 with Gly, Thr or Leu leads to 6- to 9fold increase in Km value for cofactor NAD+ or NADG, with only slight increase for substrates D- glyceraldehyde 3-phosphate or 3-phospho-D-glyceroyl phosphate
F37L
substitution of residue F37 with Gly, Thr or Leu leads to 6- to 9fold increase in Km value for cofactor NAD+ or NADG, with only slight increase for substrates D-glyceraldehyde 3-phosphate or 3-phospho-D-glyceroyl phosphate
F37T
substitution of residue F37 with Gly, Thr or Leu leads to 6- to 9fold increase in Km value for cofactor NAD+ or NADG, with only slight increase for substrates D-glyceraldehyde 3-phosphate or 3-phospho-D-glyceroyl phosphate
T227A
mutation at site of O-GlcNAcylation. Mutation induces the cytoplasmic accumulation of glyceraldehyde 3-phosphate dehydrogenase
C151/H178N
the rate of the forward reaction is decreased by 47000 times compared to the wild type enzyme with similar affinity for the substrate and the coenzyme
C151G
the mutant is completely inactive
C151S
the mutant shows drastically reduced kcat values compared to the wild type enzyme
H178N
the mutant shows no significant difference in the Km values of D-glyceraldehyde 3-phosphate, phosphate, and NAD+ compared to the wild type enzyme, however, the mutation results in the reduction of kcat of oxidative phosphorylation by 1400times
C151/H178N
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the rate of the forward reaction is decreased by 47000 times compared to the wild type enzyme with similar affinity for the substrate and the coenzyme
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C151G
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the mutant is completely inactive
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C151S
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the mutant shows drastically reduced kcat values compared to the wild type enzyme
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H178N
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the mutant shows no significant difference in the Km values of D-glyceraldehyde 3-phosphate, phosphate, and NAD+ compared to the wild type enzyme, however, the mutation results in the reduction of kcat of oxidative phosphorylation by 1400times
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C152S
site-directed mutagenesis, mutation of the catalytic residue inactivates the enzyme
S124A
site-directed mutagenesis, the mutant is phosphorylated in a similar way like the wild-type enzyme, but shows highly reduced activity
S205A
site-directed mutagenesis, the mutant is poorly or not phosphorylated, the mutant shows similar affinity for both substrates but near half of the Vmax compared to wild-type
S205D
site-directed mutagenesis, the mutant enzyme (mimicking the phosphorylated form) exhibits a sstrong decrease in activity but similar affinity toward substrates compared to wild-type. The catalytic efficiency is 330 and 410fold lower with NAD+ and Ga3P, respectively
S66A
site-directed mutagenesis, the mutant is phosphorylated in a similar way like the wild-type enzyme, the mutant shows similar affinity for both substrates but near half of the Vmax compared to wild-type
C149S
the mutant shows 92% activity compared to the wild type enzyme
C149S
about 1% of wild-type activity, residue Cys149 is both essential for catalysis and the only accessible cysteine
C153S
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mutant, having only one cysteine in the catalytic site, is oxidized and glutathionylated similarly to the wild-type enzyme
C153S
the mutant shows 0.7% activity compared to the wild type enzyme
C153S
residue Cys153 has apparently no role in catalysis, in spite of the proximity in space with catalytic Cys149
D35G
mutation enables GAPDH to accept both NAD and NADP
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
mutant accepts both Nad AND nadp WITH SIMILAR EFFICINCY
D35G/L36R/P192S
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
D35G/L36T/T37K
catalytic efficiency with NADP is about 10fold hihger than with NAD
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
Mutant shows the highest catalytic efficiency with NADP while the catalytic efficiency with NAD also increases
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
mutation enables GAPDH to accept 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+
C153S
about 450fold decrease in activity
C153S
the specific activity of the mutant enzyme is approximately 450fold lower than that of the wild type enzyme
C149A
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site-directed mutagenesis
C149A
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mutation abolishes NAD+-dependent ADP-ribosylation of the enzyme
Y46G/S48G
positive cooperativity in binding the coenzyme NAD+
Y46G/S48G
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inactive mutant enzyme, only exists as dimer
D311N
site-directed mutagenesis, the mutation breaks the salt bridge between the catalytic and NAD+-binding domains, mutant dN-GAPDS D311N binds NAD+ noncooperatively
D311N
site-directed mutagenesis, the mutation breaks the salt bridge between the catalytic and NAD+-binding domains, the inactivation rate constant in the presence of GdnHCl increases 6fold, and the value of GdnHCl concentration corresponding to the protein half-denaturation decreases from 1.83 to 1.35 M. The mutation D311N enhances the enzymatic activity of the protein 2fold
E244Q
site-directed mutagenesis, mutation at the interdomain salt bridge
E244Q
site-directed mutagenesis, mutation at the interdomain salt bridge, the E244Q substitution does not alter the NAD+-binding significantly. The mutant protein exhibits a well-pronounced positive cooperativity in coenzyme binding
E96Q
site-directed mutagenesis, mutation at the interdomain salt bridge
E96Q
site-directed mutagenesis, mutation at the interdomain salt bridge, the E96Q substitution does not alter the NAD+-binding significantly. The mutant protein exhibits a well-pronounced positive cooperativity in coenzyme binding
C150G
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the Tdh3 mutation eliminates catalytic activity, the mutant is defective in silencing and deficient in NAD+ binding
C150G
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the Tdh3 mutation eliminates catalytic activity, the mutant is defective in silencing and deficient in NAD+ binding
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additional information
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recombinant expression of Gapdh from Thermoanaerobacterium saccharolyticum in Clostridium thermocellum improves the growth rates of the cells in presence of ethanol compared to wild-type
additional information
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GAPC-1 antisense line shows a delay in growth, morpholigical alterations in siliques, and low seed number. Embryo development is altered, showing abortions and empty embryonic sacs in basal and apical siliques, respectively. Mutant shows a decrease in the expression and activity of aconitase and succinate dehydrogenase and reduced levels of pyruvate and several Krebs cycle intermediates, and increased reactive oxygen species levels
additional information
construction of enzyme gapcp double mutants, gapcp1gapcp2, under the control of photosynthetic (Rubisco small subunit RBCS2B [RBCS]) or heterotrophic (phosphate transporter PHT1.2 [PHT]) cell-specific promoters
additional information
construction of enzyme gapcp double mutants, gapcp1gapcp2, under the control of photosynthetic (Rubisco small subunit RBCS2B [RBCS]) or heterotrophic (phosphate transporter PHT1.2 [PHT]) cell-specific promoters
additional information
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construction of glyceraldehyde-3-phosphate dehydrogenase double mutant gapcp1gapcp2. GAPCp expression in photosynthetic cells of gapcp1-gapcp2 does not complement the growth arrest of the aerial parts of the mutant plants, the lack of GAPCp activity in epidermal cells restricts leaf growth
additional information
knockout or overexpression of GAPC isozymes in Arabidopsis thaliana causing significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Construction of two double knockout seeds by T-DNA insertion showing over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
additional information
knockout or overexpression of GAPC isozymes in Arabidopsis thaliana causing significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Construction of two double knockout seeds by T-DNA insertion showing over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
additional information
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knockout or overexpression of GAPC isozymes in Arabidopsis thaliana causing significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Construction of two double knockout seeds by T-DNA insertion showing over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
additional information
generation of a gapc1/gapc2 double mutant that is entirely devoid of the cytosolic GAPC activity and insensitive to Tyr-Asp inhibition of GAPC activity
additional information
generation of a gapc1/gapc2 double mutant that is entirely devoid of the cytosolic GAPC activity and insensitive to Tyr-Asp inhibition of GAPC activity
additional information
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knockout or overexpression of GAPC isozymes in Arabidopsis thaliana causing significant changes in the level of intermediates in the glycolytic pathway and the ratios of ATP/ADP and NAD(P)H/NAD(P). Construction of two double knockout seeds by T-DNA insertion showing over 3% of dry weight decrease in oil content compared with that of the wild-type. In transgenic seeds under the constitutive 35S promoter, oil content is increased up to 42% of dry weight compared with 36% in the wild-type and the fatty acid composition is altered. The transgenic lines exhibit decreased fertility. Seed-specific overexpression lines show over 3% increase in seed oil without compromised seed yield or fecundity, phenotypes, overview
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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
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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
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replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase by Clostridium acetobutylicum GapC glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.9 results in significant reduction of flux through the pentose phosphate pathway. Recombinant strains display increased NADPH availability, and consistently higher productivity than parent strains
additional information
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construction of a gapA-deficient strain MC4100 DELTAgapA
additional information
the gapA gene from Escherichia coli strain MG1655 is replaced by the gene gapN from Streptococcus mutans, EC 1.2.1.9, UniProt ID Q59931. The specific NADP+-GAPDH activity of the strain MG1655DgapA::gapN is 4.6times lower relative to strain MG1655DELTAgapA::gapN/pTrcgapN and no NAD+-GAPDH activity is detected. The specific NADP+-GAPDH activity levels in the derivative strain reveal that growth rate and glucose uptake differences are attributable to gapN expression level. The NADH/NAD+ ratio in the strain MG1655DELTAgapA::gapN/pTrcgapN decreases by 25% as compared to wild-type strain. In contrast, the NADPH/NADP+ ratio increases 2times indicating that the alteration in the turnover of NAD(P)H via glyceraldehyde 3-phosphate oxidation affects the redox levels of the strain MG1655DELTAgapA::gapN/pTrcgapN, which increases 2.8times the NADPH/NADH ratio
additional information
generation of an engineered synthetic Escherichia coli codon optimized sequence of a human gene that codifies for a 32.4 kDa protein for recombinant expression
additional information
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mutant htt shows co-localization of GAPDH with N-terminus of huntingtin aggregates
additional information
expression of a highly soluble form of GAPDS truncated at the N-terminus, amino acids 69398. Mutant displays a 3fold increase in catalytic efficiency and shows homotetrameric structure
additional information
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expression of a highly soluble form of GAPDS truncated at the N-terminus, amino acids 69398. Mutant displays a 3fold increase in catalytic efficiency and shows homotetrameric structure
additional information
construction of a plasmid encoding truncated GAPDS lacking 68 N-terminal amino acids (dN-GAPDS)
additional information
construction of a plasmid encoding truncated GAPDS lacking 68 N-terminal amino acids (dN-GAPDS)
additional information
construction of a plasmid encoding truncated GAPDS lacking 68 N-terminal amino acids (dN-GAPDS). The recombinant GAPDS without the N-terminal sequence (dN-GAPDS) is soluble in contrast to the wild-type
additional information
construction of a plasmid encoding truncated GAPDS lacking 68 N-terminal amino acids (dN-GAPDS). The recombinant GAPDS without the N-terminal sequence (dN-GAPDS) is soluble in contrast to the wild-type
additional information
construction of three deletion mutants of GAPDH that lack different lengths in their C-terminal regions (GAPDH1-106, GAPDH1-176, and GAPDH1-230). Among these three mutants, GAPDH1-106 shows an affinity with SRR, whereas GAPDH1-176 and GAPDH1-230 do not, suggesting that the catalytic domain interrupts interacting sites in the NAD+-binding domain of GAPDH
additional information
viral mutations R58E, Q59A or Q63A in the matrix region, and E76R or R82E in the capsid N-terminal domain abrogate the interaction with the C-terminal domain of enzyme GAPDH. SAccharomyces cerevisiae two-hydrib interaction analysis between enzyme GAPDH wild-type and mutants with HIV-1 wild-type and mutant matrix region and capsid N-terminal domain, overview
additional information
knockdown of GAPDHS in uveal melanoma (UM) cell lines hinders glycolysis by decreasing glucose uptake, lactate production, ATP generation, cell growth and proliferation. Conversely, overexpression of GAPDHS promotes glycolysis, cell growth and proliferation. Transcription factor SOX10 knockdown reduces the activation of GAPDHS, leading to an attenuated malignant phenotype, and SOX10 overexpression promotes the activation of GAPDHS, leading to an enhanced malignant phenotype
additional information
GAPDH1 gene silencing using Agrobacterium tumefaciens strain AGL-1-mediated transformation o the cells with siRNA. RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. MA-RGAPDH2 is found to strengthen the metabolic flux of dihydroxyacetone phosphate to glycerol-3-phosphate
additional information
GAPDH1 gene silencing using Agrobacterium tumefaciens strain AGL-1-mediated transformation o the cells with siRNA. RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. MA-RGAPDH2 is found to strengthen the metabolic flux of dihydroxyacetone phosphate to glycerol-3-phosphate
additional information
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GAPDH1 gene silencing using Agrobacterium tumefaciens strain AGL-1-mediated transformation o the cells with siRNA. RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. MA-RGAPDH2 is found to strengthen the metabolic flux of dihydroxyacetone phosphate to glycerol-3-phosphate
additional information
GAPDH1 gene silencing using Agrobacterium tumefaciens strain AGL-1-mediated transformation of the cells with siRNA. RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate
additional information
GAPDH1 gene silencing using Agrobacterium tumefaciens strain AGL-1-mediated transformation of the cells with siRNA. RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate
additional information
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GAPDH1 gene silencing using Agrobacterium tumefaciens strain AGL-1-mediated transformation of the cells with siRNA. RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate
additional information
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GAPDH1 gene silencing using Agrobacterium tumefaciens strain AGL-1-mediated transformation of the cells with siRNA. RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate
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additional information
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GAPDH1 gene silencing using Agrobacterium tumefaciens strain AGL-1-mediated transformation o the cells with siRNA. RNA interference of isozymes GAPDH1 and GAPDH2 (MA-RGAPDH1 and MA-RGAPDH2) greatly reduced the biomass of the fungus. The lipid content of MA-RGAPDH2 is about 23% higher than that of the control. Both of the lipid-increasing transformants show a higher NADPH/NADP ratio. Analysis of metabolite and enzyme expression levels reveals that the increased lipid content of MA-GAPDH1 is due to enhanced flux of glyceraldehyde-3-phosphate to glycerate-1,3-biphosphate. MA-RGAPDH2 is found to strengthen the metabolic flux of dihydroxyacetone phosphate to glycerol-3-phosphate
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additional information
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mutants Gapdhm1Neu (Y91stop truncated protein of 89 amino acids), Gapdhm2Neu (truncated/altered protein of 9 amino acids), and Gapdhm8Neu (truncated/altered protein of 73 amino acids) exhibit 50-55% residual activity in blood compared to the wild type enzyme
additional information
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generation of FAO hepatoma cells with mutations of all 4 lysine residues K115, K160, K225, and K252 (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state reduces GAPDH glycolytic activity and glycolytic flux and increases gluconeogenic GAPDH activity and glucose production, phenotype overview
additional information
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generation of FAO hepatoma cells with mutations of all 4 lysine residues K115, K160, K225, and K252 (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state reduces GAPDH glycolytic activity and glycolytic flux and increases gluconeogenic GAPDH activity and glucose production, phenotype overview
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additional information
generation of a gapc1/gapc2 double mutant that is entirely devoid of the cytosolic GAPC activity and insensitive to Tyr-Asp inhibition of GAPC activity
additional information
generation of a gapc1/gapc2 double mutant that is entirely devoid of the cytosolic GAPC activity and insensitive to Tyr-Asp inhibition of GAPC activity
additional information
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a downregulation of GAPDH activity does not contribute to improved performance of engineered Saccharomyces cerevisiae on pentose substrates
additional information
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nuclear export sequences are fused to the 3' end of gene TDH3 by transforming a DNA fragment with 3' homology to the TDH3 ORF, the nuclear export sequence, and an hphMX4 sequence into the appropriate yeast strain. Strains lacking both TDH3 and specific NAD+ biosynthetic genes are generated by crossing Dtdh3 strain YSH969 with selected strains from the yeast deletion collection. Identification of sporulation haploid strains
additional information
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nuclear export sequences are fused to the 3' end of gene TDH3 by transforming a DNA fragment with 3' homology to the TDH3 ORF, the nuclear export sequence, and an hphMX4 sequence into the appropriate yeast strain. Strains lacking both TDH3 and specific NAD+ biosynthetic genes are generated by crossing Dtdh3 strain YSH969 with selected strains from the yeast deletion collection. Identification of sporulation haploid strains
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