De Marco C, Rinaldi A, Dessi M R, Dernini S
Mol Cell Biochem. 1976 Aug 30;12(2):89-92. doi: 10.1007/BF01731554.
Se-Carboxymethyl-DL-selnocysteine (CMSeC) has been prepared in a pure crystalline form from selenocysteine and monochloracetic acid. It has been shown that CMSeC is a substrate for the L-aminoacid oxidase form snake venom and for the D-aspartate oxidase from beef kidney. Oxygen consumption and ammonia production indicate that only the L or the D form of CMSeC ar acted upon respectively by one or the other of the above enzymes. No noticeable differences were shown in the oxidation rate of CMSeC and S-carboxymethylcysteine, an indication that the substitution of a selenium for a sulfur atom in the molecule does not greatly affect the substrate specificity of the two enzymes. Data have been obtained suggesting that the product of the oxidative deamination of CMSeC Is Se-carboxymethyl-selenopyruvic acid.
硒代羧甲基-DL-硒代半胱氨酸（CMSeC）已由硒代半胱氨酸和一氯乙酸制备成纯结晶形式。研究表明，CMSeC是蛇毒L-氨基酸氧化酶和牛肾D-天冬氨酸氧化酶的底物。耗氧量和氨生成量表明，上述两种酶分别作用于CMSeC的L型或D型。CMSeC和S-羧甲基半胱氨酸的氧化速率没有明显差异，这表明分子中硒原子取代硫原子对这两种酶的底物特异性影响不大。已获得的数据表明，CMSeC氧化脱氨的产物是硒代羧甲基-硒代丙酮酸。
