OXIDATION OF SE-CARBOXYMETHYL-SELENOCYSTEINE BY L-AMINOACID OXIDASE AND BY D-ASPARTATE OXIDASE
OXIDATION OF SE-CARBOXYMETHYL-SELENOCYSTEINE BY L-AMINOACID OXIDASE AND BY D-ASPARTATE OXIDASE
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DOI：
10.1007/bf01731554
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发表时间：
1976-01-01
影响因子：
4.3
通讯作者：
DERNINI, S
中科院分区：
文献类型：
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作者：
DEMARCO, C;RINALDI, A;DERNINI, S
Se-羧甲基-DL-硒代半胱氨酸（CMSeC）是由硒代半胱氨酸和一氯乙酸制备的纯晶体形式。已表明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。氧消耗和氨产生表明，只有L或D形式的CMSeC分别受到上述酶中的一种或另一种的作用。CMSeC和S-羧甲基半胱氨酸的氧化速率没有显着差异，表明分子中硒取代硫原子不会大大影响两种酶的底物特异性。已获得的数据表明，CMSeC的氧化脱氨基的产物是Se-羧甲基-硒丙酮酸。
Se-Carboxymethyl-DL-selenocysteine (CMSeC) has been prepared in a pure crystalline form from selenocysteine and monochloroacetic acid. It has been shown that CMSeC is a substrate for the L-aminoacid oxidase from 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 are 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.