On the role of octopine dehydrogenase in cephalopod mantle muscle metabolism

Abstract

Octopine dehydrogenases from the mantle muscle of the squid, Symplectoteuthis oualaniensis, and of the octopus, Octopus ornatus, were kinetically characterized and compared. In the squid, the specific activity of the enzyme was about 110 μmol product formed per minute per gram wet weight; in the octopus that value was over 600. Both enzymes show similar pH dependence; in the direction of octopine formation the pH optimum was about 6.5, whereas in the direction of octopine oxidation it was about 8.5. The affinities for NADH, arginine, and pyruvate were similar (K_m values were about 0.04 mM, 7 mM, and 2 mM respectively). Increasing the concentration of either arginine or pyruvate increased the affinity for the cosubstrate (pyruvate or arginine), this mechanism being a means of regulating the enzyme activity in vivo. In the direction of octopine oxidation, the octopus enzyme showed a much higher affinity for octopine (K_m = 0.8 mM) than did the squid enzyme (K_m = 4.4 mM), suggesting that it may be better geared for reconverting octopine to arginine and pyruvate after anaerobic bursts of muscle activity.