Literature summary extracted from

Rivera-Nieves, J.; Thompson, W.C.; Levine, R.L.; Moss, J.
Thiols mediate superoxide-dependent NADH modification of glyceraldehyde-3-phosphate dehydrogenase (1999), J. Biol. Chem., 274, 19525-19531.

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.2.1.12	Oryctolagus cuniculus	-	-	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
1.2.1.12	additional information	posttranslational modification of the enzyme with NADH is stimulated by thiols, possibly through superoxide, and is independent of NO	Oryctolagus cuniculus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.2.1.12	muscle	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

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

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.2.1.12	NAD+	-	Oryctolagus cuniculus

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Release 2023.1 (January 2023)