Molecular architecture of mammalian pyruvate dehydrogenase complex

被引：0
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作者：
Maofei Chen [1 ,2 ]
Yutong Song [1 ,3 ]
Sensen Zhang [1 ,2 ]
Yitang Zhang [1 ,2 ]
Xudong Chen [1 ,2 ]
Minghui Zhang [4 ]
Meng Han [5 ]
Xin Gao [6 ,7 ]
Sai Li [1 ,3 ]
Maojun Yang [1 ,2 ,8 ,9 ]
机构：
[1] Tsinghua-Peking Center for Life Sciences, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua University
[2] Ministry of Education Key Laboratory of Protein Science, Tsinghua University
[3] State Key Laboratory of Membrane Biology, Tsinghua University
[4] Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Shenzhen University Health Science Center
[5] Protein Research Technology Center, Protein Chemistry and Omics Platform, School of Life Sciences, Tsinghua University
[6] Computer Science Program, Computer, Electrical and Mathematical Sciences and Engineering Division, King Abdullah University of Science and Technology (KAUST)
[7] Computational Bioscience Research Center, King Abdullah University of Science and Technology
[8] Cryo-EM Facility Center, Southern University of Science and Technology
[9] Beijing Life Science
来源：
Protein & Cell | 2025年 / 16卷 / 01期
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Q55 [酶];
学科分类号：
摘要：
<正>Dear Editor,Pyruvate dehydrogenase complex(PDHc) is a large multienzyme assembly(Mr = 4–10 million Daltons) consisting of three essential components: pyruvate dehydrogenase(E1p), dihydrolipoyl transacetylase(E2p), and dihydrolipoyl dehydrogenase(E3). These three enzymes perform distinct functions sequentially to catalyze the oxidative decarboxylation of pyruvate with formation of nicotinamide adenine dinucleotide(NADH) and acetyl-coenzyme A(Patel and Roche, 1990).
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页码：72 / 78
页数：7
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