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 cys
teamine behaves like a competitive inhibitor, and shows K-i = 5 x 10(-
5) M. The possible involvement of the oxidation of cysteamine and the
inhibitory effects of thioacetaldehyde in the cystamine oxidation by a
mine oxidase is discussed.