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Literature summary for 1.2.1.12 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.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
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

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
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Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Oryctolagus cuniculus