Literature summary for 1.2.1.12 extracted from

Ghosh, S.; Mukherjee, K.; Ray, M.; Ray, S.
Identification of a critical lysine residue at the active site in glyceraldehyde-3-phosphate dehydrogenase of Ehrlich ascites carcinoma cell. Comparison with the rabbit muscle enzyme (2001), Eur. J. Biochem., 268, 6037-6044.

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Inhibitors

Inhibitors	Comment	Organism	Structure
pyridoxal 5'-phosphate	inactivation with pseudo-first-order kinetics	Mus musculus
pyridoxal 5'-phosphate	-	Oryctolagus cuniculus
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	Mus musculus
Trinitrobenzenesulfonic acid	-	Oryctolagus cuniculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-
Oryctolagus cuniculus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
Ehrlich ascites carcinoma cell	-	Mus musculus	-
muscle	-	Mus musculus	-
muscle	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+	-	Mus musculus	3-phospho-D-glyceroyl phosphate + NADH	-	?
D-glyceraldehyde 3-phosphate + phosphate + NAD+	-	Oryctolagus cuniculus	3-phospho-D-glyceroyl phosphate + NADH	-	?

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Mus musculus
NAD+	-	Oryctolagus cuniculus

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Release 2023.1 (January 2023)