EC Number |
Reaction |
Reference |
---|
1.5.1.11 | 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 |
13311 |
1.5.1.11 | 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 |
13298 |
1.5.1.11 | N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+ |
kinetic mechanism |
13303 |
1.5.1.11 | 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 |
13298 |
1.5.1.11 | N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+ |
partially ordered mechanism. NADPH binds first followed by the random order, rapid-equilibrium-binding of Arg and pyruvate. Orn probably binds before pyruvate |
13319 |
1.5.1.11 | 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 |
13296 |
1.5.1.11 | N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+ |
substrates bind in an ordered sequential manner. First NADH binds to OcDH followed by L-arginine. The binding of the guanidinium headgroup of L-arginine induces a conformational change, resulting in the formation of the pyruvate binding site. The reduction of pyruvate can only occur in the presence of L-arginine, which than forms octopine and prevents lactate formation |
713370 |
1.5.1.11 | N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O = L-arginine + pyruvate + NADH + H+ |
the enzyme removes the pro-S hydrogen atom of the dihydronicotinamide ring with transfer of label to the solvent and to the product octopine (N-2-(1-carboxyethyl)-L-arginine ) |
13321 |