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Literature summary for 1.2.1.12 extracted from

  • Marin, P.; Maus, M.; Bockaert, J.; Glowinski, J.; Premont, J.
    Oxygen free radicals enhance the nitric oxide-induced covalent NAD(+)-linkage to neuronal glyceraldehyde-3-phosphate dehydrogenase (1995), Biochem. J., 309, 891-898.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
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 Mus musculus
NO inactivation by induction of a covalent binding of NAD+ to the enzyme Mus musculus
sodium nitroprusside the NO-generating compound inactivates by induction of a covalent binding of NAD+ to the enzyme Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Mus musculus 5829
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
neuron striatal Mus musculus
-

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
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Mus musculus