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2976283 
Journal Article 
Oxidative deamination of epsilon-N-acetylthialysine and epsilon-N-acetylselenalysine by snake venom L-aminoacid oxidase 
Cini, C; De Marco, C 
1979 
Yes 
Italian Journal of Biochemistry
ISSN: 0021-2938 
28 
3 
221-231 
English 
121995 
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.