d(-)-Lactate dehydrogenase from Allomyces

Summary d(-)-lactate dehydrogenase from hybrid male strain of Allomyces has been partially purified.The enzyme shows multiple binding sites for NADH. It obeys Michaelis-Menten kinetics for pyruvate. The inhibition of the enzyme activity by ATP is of mixed type. ADP is not an allosteric inhibitor of the enzyme. AMP and cyclic 3,5-AMP do not affect the enzyme. NAD⁺ acts as a product inhibitor.