CHARACTERIZATION OF THE INHIBITION OF ESCHERICHIA-COLI PYRUVATE-DEHYDROGENASE COMPLEX BY PYRUVATE

被引：6
|
作者：
DATTA, A [1 ]
机构：
[1] INST ENZYME RES,MADISON,WI 53705
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 176卷 / 01期
关键词：
D O I：
10.1016/0006-291X(91)90955-7
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：
The E. coli pyruvate dehydrogenase complex was inhibited by pyruvate in absence of its cofactor, NAD+. The inhibition was found to increase with pH and phosphate concentration of the buffer and decrease with its ionic strength. The inhibition profile was different with MOPS buffer. No radioactivity was found in the enzyme, when the latter was incubated with 2-14C-pyruvate. The results suggest that covalent adduct formation is not necessary for the observed inhibition. © 1991.
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页码：517 / 521
页数：5
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