Oxidative deamination of epsilon-N-acetylthialysine and epsilon-N-acetylselenalysine by snake venom L-aminoacid oxidase.

epsilon-N-acetylthialysine and epsilon-N-acetylselenalysine are oxidatively deaminated by Crotalus adamanteus l-aminoacid oxidase, giving rise to the corresponding alpha-ketoacids, identified by some chemical and chromatographic tests and by comparison with synthetic compounds. no cleavage of the C-S or C-Se bonds of the substrates occurs during the reaction. The enzyme acts as well on the epsilon-N-acetylderivatives of thialysine and selenalysine as on epsilon-N-acetyllysine. The substitution of the gamma methylene group of lysine by a sulfur or a selenium atom seems not to greatly affect the substrate specificity of the enzyme.