Nov 1, 1975

Investigations on the kinetic mechanism of octopine dehydrogenase. 1. Steady-state kinetics

European Journal of Biochemistry
M O Doublet, A Olomucki


The kinetic mechanism of action of octopine dehydrogenase was investigated. This enzyme catalyses the reversible dehydrogenation of D-octopine to L-arginine and pyruvate, in the presence of nicotinamide-adenine dinucleotide. Initial velocity and product inhibition studies were carried out in both directions. Most of the results are consistent with a bi-ter sequential mechanism where NAD+ binds first to the enzyme followed by D-octopine, and the products are released in the order L-arginine, pyruvate and NADH. Various kinetic parameters were determined for each reactant at 33 degrees C, at pH 9.6 for NAD reduction, at pH 6.6 for NADH oxidation.

Mentioned in this Paper

Pyruvate Measurement
Oxidoreductases Acting on CH-NH Group Donors
Binding (Molecular Function)
Metabolic Inhibition
Nadh Oxidation
Nicotinamide adenine dinucleotide (NAD)

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