Kinetic study of the inhibition of rat liver ornithine decarboxylase by diamines; considerations on the mechanism of interaction between enzyme and inhibitor.

1. Partially purified rat liver ornithine decarboxylase is inhibited by several diamines including putrescine, 1,3-diaminopropane, cadaverine and p-phenylenediamine. 2. The inhibition is dependent on pH, being strong at pH above 8 and negligible below pH 6.5. 3. The kinetic study of the inhibition showed that while the aromatic diamine behaved as a simple competitive inhibitor, the aliphatic diamines presented a more complex pattern of inhibition in which two molecules of inhibitor might bind to the enzyme active site. 4. The Ki values for the different inhibitors were calculated and the degree of affinity for the enzyme was p-phenylenediamine greater than putrescine greater than cadaverine greater than 1,3-diaminopropane. 5. A molecular mechanism explaining how one or two molecules of inhibitor can bind to the enzyme is proposed.