Abstract
Chicken liver lactate dehydrogenase ( l-lactate : NAD + oxidoreductase, EC 1.1.1.27) irreversibly catalyses the oxidation of glyoxylate (hydrated form)(I) to oxalate ( pH = 9.6 ) and the reduction of (non-hydrated form) (II) to glycolate ( pH = 7.4 ). (I) attaches to the enzyme in the pyruvate binding site and (II) attaches to the enzyme at the l-lactate binding site. The oxidation of (I) ( pH = 9.6 ) is adapted to the following mechanism: The abortive complexes, E-NADH-I and E-NAD +-II, are responsible for the inhibition by excess substrate in the reduction and oxidation systems, respectively. When lactate dehydrogenase and NAD + are preincubated, E-NAD +NAD + appears and causes inhibition by excess NAD + in the glyoxylate-lactate dehydrogenase-NAD + and l-lactate-lactate dehydrogenase-NAD + systems; the second NAD + molecule attaches to the enzyme at the l-lactate binding site.
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