Oxidative deamination of epsilon-N-acetylthialysine and epsilon-N-acetylselenalysine by snake venom L-aminoacid oxidase.
Ital J Biochem, 1979/5-1979/6;28(3):221-31.
PMID: 121995
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
Amino Acid Oxidoreductases; Ammonia; Animals; Cysteine; Deamination; In Vitro Techniques; Keto Acids; Kinetics; Lysine; Oxygen Consumption; Snake Venoms; Snakes; Substrate Specificity
More resources
EndNote: Download