Multiple forms of octopine dehydrogenase in Strombus luhuanus (mollusca, gastropoda, strombidae): genetic basis of polymorphism, properties of the enzymes, and relationship between the octopine dehydrogenase phenotype and the accumulation of anaerobic end products during exercise.
Octopine dehydrogenase (ODH) is electrophoretically polymorphic in the gastropod mollusk Strombus luhuanus. The frequencies of the six electrophoretic phenotypes in the Heron Island population, together with the molecular weight values of 38,000 obtained for each of the three forms of the enzyme, demonstrate that the monomeric enzyme is encoded by three codominant alleles at a single locus. The purified allozymes are indistinguishable in terms of Km values for substrates, product inhibition by octopine and NAD, pH optima, and substrate inhibition by pyruvate. No statistically significant correlations were found between the ODH phenotype and the maximum activities of ODH or alanopine dehydrogenase, the capacity for anaerobic muscle work, or the accumulation of octopine or strombine/alanopine during exercise. It would appear that the ODH allozymes may be functionally equivalent both in vitro and in vivo.
D000483:Alleles; D000594:Amino Acid Oxidoreductases / Q000235:genetics*; D000818:Animals; D005075:Biological Evolution; D007700:Kinetics; D008974:Mollusca / Q000201:enzymology*; D009132:Muscles / Q000201:enzymology; D009243:NAD / Q000378:metabolism; D005082:Physical Exertion; D011110:Polymorphism, Genetic
D009243:NAD; D000594:Amino Acid Oxidoreductases; C021903:D-octopine dehydrogenase