INACTIVATION OF YEAST ALCOHOL DEHYDROGENASE BY N-ALKYLMALEIMIDES
INACTIVATION OF YEAST ALCOHOL DEHYDROGENASE BY N-ALKYLMALEIMIDES
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DOI：
10.1016/0003-9861(68)90271-3
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发表时间：
1968-01-01
影响因子：
3.9
通讯作者：
ANDERSON, BM
中科院分区：
文献类型：
--
作者：
HEITZ, JR;ANDERSON, CD;ANDERSON, BM
合成了七个N-烷基马来酰胺酸并通过加热转化为相应的N-烷基马来酰亚胺。不同链长的烷基马来酰亚胺在 pH 7.0 下可有效灭活酵母乙醇脱氢酶。研究了pH值对N-乙基马来酰亚胺水解速率的影响，pH范围为8.6至9.4，观察到反应的特定碱催化作用。酵母醇脱氢酶马来酰亚胺失活的二级速率常数随着马来酰亚胺衍生物烷基取代基链长的增加而增加。 N-乙基马来酰亚胺和N-庚基马来酰亚胺与半胱氨酸和谷胱甘肽的反应中没有观察到链长效应。酵母葡萄糖 6-磷酸脱氢酶对马来酰亚胺失活的敏感性低于酵母乙醇脱氢酶，它被 N-乙基和 N-庚基马来酰亚胺灭活，其速率表明没有明显的链长效应。
SevenN-alkylmaleamic acids were synthesized and converted through heating to the correspondingN-alkylmaleimides. Alkylmaleimides of varying chainlength were shown to effectively inactivate yeast alcohol dehydrogenase at pH 7.0. The effect of pH on the rate of hydrolysis ofN-ethylmaleimide was studied in the pH range from 8.6 to 9.4 where specific base catalysis of the reaction was observed.Second-order rate constants for maleimide inactivation of yeast alcohol dehydrogenase were shown to increase with increasing chainlength of the alkyl substituents of the maleimide derivatives. A chainlength effect was not observed in the reaction ofN-ethylmaleimide andN-heptylmaleimide with cysteine and glutathione. Yeast glucose 6-phosphate dehydrogenase, which is less sensitive to maleimide inactivation than is yeast alcohol dehydrogenase, was inactivated by bothN-ethyl andN-heptylmaleimide at rates indicating no appreciable chainlength effect.