Literature summary for 1.2.1.12 extracted from

Eyschen, J.; Vitoux, B.; Marraud, M.; Cung, M.T.; Branlant, G.
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ nicotinamide but does not experience A-specific hydride transfer (1999), Arch. Biochem. Biophys., 364, 219-227.

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Protein Variants

Protein Variants	Comment	Organism
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	Escherichia coli
Y317A	dissociation constant for NAD+ is 5times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged	Escherichia coli
Y317G	dissociation constant for NAD+ is 13times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.045	-	NAD+	wild-type enzyme	Escherichia coli
0.05	-	NAD+	mutant Y317A	Escherichia coli
0.058	-	NAD+	mutant N313T/Y317G	Escherichia coli
0.19	-	NAD+	mutant N313T and Y317G	Escherichia coli
0.29	-	D-glyceraldehyde 3-phosphate	mutant N313T/Y317G	Escherichia coli
0.42	-	D-glyceraldehyde 3-phosphate	mutant N313T	Escherichia coli
0.53	-	phosphate	wild-type enzyme	Escherichia coli
0.88	-	D-glyceraldehyde 3-phosphate	mutant Y317A	Escherichia coli
0.89	-	D-glyceraldehyde 3-phosphate	wild-type enzyme	Escherichia coli
2.05	-	D-glyceraldehyde 3-phosphate	mutant Y317G	Escherichia coli
4.8	-	phosphate	mutant enzyme Y317A	Escherichia coli
6.9	-	phosphate	mutant enzyme N313T/Y317G	Escherichia coli
20	-	phosphate	mutant enzyme N313T	Escherichia coli
35.1	-	phosphate	mutant enzyme Y317G	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9B2	wild-type and mutant enzymes N313T, Y317A, Y317G and N313T/Y317G	-

Reaction

Reaction	Comment	Organism	Reaction ID
D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+	B-specific oxidoreductase	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+	-	Escherichia coli	3-phospho-D-glyceroyl phosphate + NADH	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Escherichia coli

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Release 2023.1 (January 2023)