The Pyruvate Dehydrogenase Complexes: Structure-based Function and Regulation

被引:478
作者
Patel, Mulchand S. [1 ]
Nemeria, Natalia S. [2 ]
Furey, William [3 ,4 ]
Jordan, Frank [2 ]
机构
[1] SUNY Buffalo, Dept Biochem, Sch Med & Biomed Sci, Buffalo, NY 14214 USA
[2] Rutgers State Univ, Dept Chem, Newark, NJ 07102 USA
[3] Univ Pittsburgh, Sch Med, Dept Pharmacol & Chem Biol, Pittsburgh, PA 15261 USA
[4] Vet Affairs Med Ctr, Pittsburgh, PA 15240 USA
基金
美国国家卫生研究院;
关键词
THIAMIN DIPHOSPHATE ENZYMES; ACTIVE-CENTER COMMUNICATION; ESCHERICHIA-COLI; MULTIENZYME COMPLEX; E1; COMPONENT; DIHYDROLIPOAMIDE DEHYDROGENASE; CRYSTAL-STRUCTURE; PHOSPHATASE ISOFORM-1; MAMMALIAN PYRUVATE; LIPOYL DOMAIN-2;
D O I
10.1074/jbc.R114.563148
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 pyruvate dehydrogenase complexes (PDCs) from all known living organisms comprise three principal catalytic components for their mission: E1 and E2 generate acetyl-coenzyme A, whereas the FAD/NAD(+)-dependent E3 performs redox recycling. Here we compare bacterial (Escherichia coli) and human PDCs, as they represent the two major classes of the superfamily of 2-oxo acid dehydrogenase complexes with different assembly of, and interactions among components. The human PDC is subject to inactivation at E1 by serine phosphorylation by four kinases, an inactivation reversed by the action of two phosphatases. Progress in our understanding of these complexes important in metabolism is reviewed.
引用
收藏
页码:16615 / 16623
页数:9
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