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Literature summary for 1.5.1.11 extracted from

  • Carvajal, N.; Kessi, E.
    Kinetic mechanism of octopine dehydrogenase from the muscle of the sea mollusc, Concholepas concholepas (1988), Biochim. Biophys. Acta, 953, 14-19.
No PubMed abstract available
Search for more literature for 1.5.1.11

Inhibitors

Inhibitors Comment Organism Structure
AMP dead-end inhibition Concholepas concholepas
L-Arg linear non-competitive inhibitors with respect to octopine Concholepas concholepas
NEM product inhibition Concholepas concholepas
pyruvate linear non-competitive inhibitors with respect to octopine Concholepas concholepas

Organism

Organism UniProt Comment Textmining
Concholepas concholepas
-
-
-

Reaction

Reaction Comment Organism Reaction ID
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+ partially random mechanism in which NADH is the obligatory first substrate, and Arg and pyruvate bind randomly to the enzyme-NADH complex. Ordered sequential addition of NAD+ and octopine in octopine oxidation Concholepas concholepas
a

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Concholepas concholepas