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Literature summary for 1.5.1.11 extracted from

  • Doublet, M.O.; Olomucki, A.
    Investigations on the kinetic mechanism of octopine dehydrogenase (1975), Eur. J. Biochem., 59, 175-183.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
L-Arg noncompetitive with respect to D-octopine Pecten maximus
NAD+ noncompetitive with respect to pyruvate, uncompetitive with respect to L-Arg Pecten maximus
NEM competitive with respect to NAD+; non-competitive with respect to octopine Pecten maximus

Organism

Organism UniProt Comment Textmining
Pecten maximus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+ bi-ter sequential mechanism where NAD+ binds first to the enzyme followed by D-octopine, and the products are released in the order L-Arg, pyruvate and NADH Pecten maximus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Arg + pyruvate + NADH r Pecten maximus N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
?

Cofactor

Cofactor Comment Organism Structure
NADH
-
Pecten maximus