ROLE OF EXCESS LIPOYL DEHYDROGENASE IN RECONSTITUTED ALPHA-KETOGLUTARATE DEHYDROGENASE COMPLEX OF ESCHERICHIA-COLI

被引：7
|
作者：
WAGENKNECHT, T
FRANCIS, N
DEROSIER, D
机构：
[1] BRANDEIS UNIV, ROSENSTIEL BASIC MED SCI RES CTR, WALTHAM, MA 02254 USA
[2] BRANDEIS UNIV, DEPT BIOL, WALTHAM, MA 02254 USA
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1986年 / 135卷 / 03期
关键词：
D O I：
10.1016/0006-291X(86)90999-X
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 .alpha.-ketoglutarate dehydrogenase complex of Escherichia coli can bind up to 12 dimers of dihydrolipoyl dehydrogenase (E3) besides those already present. Maximal activity does not increase, however, when surplus E3 is present. This observation was previously interpreted to mean that the excess enzyme is inactive. We have now determined that if the reactions catalyzed by E3 are made rate-limiting, the excess E3 functions equivalently to that in the native complex.
引用
收藏
页码：802 / 807
页数：6
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