Evidence for an essential arginine residue in the substrate binding site of the mammalian succinate dehydrogenase.
Evidence for an essential arginine residue in the substrate binding site of the mammalian succinate dehydrogenase.
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哺乳动物琥珀酸脱氢酶底物结合位点中必需精氨酸残基的证据。
DOI：
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发表时间：
1984
期刊：
影响因子：
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通讯作者：
A. Vinogradov
中科院分区：
文献类型：
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作者：
A. Kotlyar;A. Vinogradov
苯乙二醛和2，3-丁二酮可迅速灭活膜结合或可溶性的牛心琥珀酸脱氢酶。这些试剂对酶的抑制完全可以通过饱和丙二酸浓度来防止。对氯汞苯甲酸酯修饰活性中心的巯基，降低了苯乙醛对酶的抑制速率，消除了丙二酸的保护作用。动力学数据表明，苯乙醛的失活是由于基本精氨酸残基(S)的修饰，该残基与二羧酸盐相互作用形成主要的酶-底物复合体。
Phenylglyoxal and 2,3-butanedione rapidly inactivate membrane-bound or soluble bovine heart succinate dehydrogenase. The inhibition of the enzyme by these reagents is completely prevented by saturating concentration of malonate. The modification of the active site sulfhydryl group by p-chloromercuribenzoate decreases the rate of the enzyme inhibition by phenylglyoxal and abolishes the protective effect of malonate. Kinetic data suggest that the inactivation by phenylglyoxal results from the modification of an essential arginine residue(s) which interacts with dicarboxylate to form the primary enzyme-substrate complex.