Patel Mulchand S, Nemeria Natalia S, Furey William, Jordan Frank
From the Department of Biochemistry, School of Medicine and Biomedical Sciences, University at Buffalo, the State University of New York, Buffalo, New York 14214,
the Department of Chemistry, Rutgers, the State University of New Jersey, Newark, New Jersey 07102.
J Biol Chem. 2014 Jun 13;289(24):16615-23. doi: 10.1074/jbc.R114.563148. Epub 2014 May 5.
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.
所有已知生物体内的丙酮酸脱氢酶复合体（PDCs）都包含执行其功能的三个主要催化成分：E1和E2生成乙酰辅酶A，而依赖FAD/NAD(+)的E3进行氧化还原循环。在这里，我们比较了细菌（大肠杆菌）和人类的PDCs，因为它们代表了2-氧代酸脱氢酶复合体超家族的两大类，其组成成分的组装方式和相互作用各不相同。人类的PDC在E1处会被四种激酶磷酸化丝氨酸而失活，而两种磷酸酶的作用可使其失活逆转。本文综述了我们对这些在代谢中起重要作用的复合体的认识进展。
