Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1

Thomas E. Roche, Yasuaki Hiromasa, Ali Turkan, Xiaoming Gong, Tao Peng, Xiaohua Yan, Shane A. Kasten, Haiying Bao, Jianchun Dong

Research output: Contribution to journalShort survey

54 Citations (Scopus)

Abstract

Four pyruvate dehydrogenase kinase and two pyruvate dehydrogenase phosphatase isoforms function in adjusting the activation state of the pyruvate dehydrogenase complex (PDC) through determining the fraction of active (non-phosphorylated) pyruvate dehydrogenase component. Necessary adaptations of PDC activity with varying metabolic requirements in different tissues and cell types are met by the selective expression and pronounced variation in the inherent functional properties and effector sensitivities of these regulatory enzymes. This review emphasizes how the foremost changes in the kinase and phosphatase activities issue from the dynamic, effector-modified interactions of these regulatory enzymes with the flexibly held outer domains of the core-forming dihydrolipoyl acetyl transferase component.

Original languageEnglish
Pages (from-to)1050-1056
Number of pages7
JournalEuropean Journal of Biochemistry
Volume270
Issue number6
DOIs
Publication statusPublished - Mar 1 2003
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry

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