title: Oxidative deamination of epsilon-N-acetylthialysine and epsilon-N-acetylselenalysine by snake venom L-aminoacid oxidase.
abstract: 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.
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D000641:Ammonia / Q000378:metabolism; D000818:Animals; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D003641:Deamination; D066298:In Vitro Techniques; D007651:Keto Acids / Q000096:biosynthesis; D007700:Kinetics; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism; D010101:Oxygen Consumption; D012910:Snake Venoms; D012911:Snakes; D013379:Substrate Specificity
chemical_list: D007651:Keto Acids; D012910:Snake Venoms; C028077:epsilon-N-acetylthialysine; C028078:epsilon-N-acetylselenalysine; D000641:Ammonia; D000594:Amino Acid Oxidoreductases; D008239:Lysine; D003545:Cysteine