Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.5.1.11 extracted from

  • Schrimsher, J.L.; Taylor, K.B.
    Octopine dehydrogenase from Pecten maximus: steady-state mechanism (1984), Biochemistry, 23, 1348-1353.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
5-Guanidinopentanoate
-
Pecten maximus
L-Arg substrate inhibition Pecten maximus
propanoate
-
Pecten maximus
pyruvate substrate inhibition 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+ NADH binds to the enzyme first followed by L-Arg and pyruvate, which bind randomly Pecten maximus
N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+ in the direction of octopine oxidation NAD binds to the enzyme before octopine in a rapid equilibrium fashion. The products L-Arg and pyruvate are released in a random fashion Pecten maximus

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
NADH
-
Pecten maximus