TRICARBALLYLATE AND HYDROXYCITRATE - SUBSTRATE AND INHIBITOR OF ATP - CITRATE OXALOACETATE LYASE

被引：225

作者：

WATSON, JA

FANG, M

LOWENSTEIN, JM

机构：

[1] Graduate Department of Biochemistry, Brandeis University, Waltham

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1969年 / 135卷 / 1-2期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/0003-9861(69)90532-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Citrate cleavage enzyme shows atypical kinetics at low chloride concentrations, but normal kinetics at high chloride concentrations. Tricarballylate is a substrate for citrate cleavage enzyme. The reaction with tricarballylate can be demonstrated both by the disappearance of CoA and, in the presence of hydroxylamine, by the appearance of a hydroxamate. This indicates that tricarballylyl-CoA is formed in the reaction. When hydroxamate formation is used to assay activity, the apparent Km for tricarballylate is about three times greater than that for citrate, while the maximum reaction velocity with tricarballylate is about 90% of that observed with citrate. One of the stereoisomers of hydroxycitrate is a powerful inhibitor of citrate cleavage enzyme. © 1969.

引用

页码：209 / +

页数：1

共 30 条

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