Medda R, Padiglia A, Lorrai A, De Marco C, Floris G
Institute of Biological Chemistry, University of Cagliari, Italy.
Biochem Mol Biol Int. 1997 Feb;41(2):395-405. doi: 10.1080/15216549700201411.
Cysteamine is oxidatively deaminated by lentil amine oxidase. It shows saturation kinetic K(m) = 9 x 10(-4) M like other substrates, but the aldehyde produced leads to loss of enzyme activity, which is restored by dialysis. When putrescine is the substrate of the amine oxidase cysteamine behaves like a competitive inhibitor, and shows Ki = 5 x 10(-5) M. The possible involvement of the oxidation of cysteamine and the inhibitory effects of thioacetaldehyde in the cystamine oxidation by amine oxidase is discussed.