硝基乙烷的碳负离子是黄素细胞色素b2[L-(+)-乳酸脱氢酶]的抑制剂，而非其底物。
The carbanion of nitroethane is an inhibitor of, and not a substrate for, flavocytochrome b2 [L-(+)-lactate dehydrogenase].
作者信息
Genet R, Lederer F
机构信息
Institut National de la Santé et de la Recherche Médicale Unité 25, Centre National de la Recherche Scientifique Unité Associëe 122, Hôpital Necker, Paris, France.
出版信息
Biochem J. 1990 Feb 15;266(1):301-4. doi: 10.1042/bj2660301.
Abstract
Although nitroethane does not bind to the active site of flavocytochrome b2, its anion, ethane nitronate, behaves as a competitive inhibitor, with a Ki of 2.2 mM. No electron transfer can be detected between the nitronate and the enzyme, in contrast with the observations of other workers on D-amino acid oxidase. Propionate is a competitive inhibitor, with a Ki of 28 mM. The significance of these results with respect to the proposed carbanion mechanism and the putative existence of a covalent enzyme-substrate intermediate is discussed.
摘要
尽管硝基乙烷不与黄素细胞色素b2的活性位点结合，但其阴离子乙烷硝酮却表现为竞争性抑制剂，抑制常数Ki为2.2 mM。与其他研究人员对D-氨基酸氧化酶的观察结果相反，在硝酮和该酶之间未检测到电子转移。丙酸盐是一种竞争性抑制剂，抑制常数Ki为28 mM。讨论了这些结果对于所提出的碳负离子机制以及共价酶-底物中间体可能存在的意义。
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