The Enzyme Database

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Accepted name: [pyruvate dehydrogenase (acetyl-transferring)] kinase
Reaction: ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
Other name(s): PDH kinase; PDHK; PDK; PDK1; PDK2; PDK3; PDK4; pyruvate dehydrogenase kinase; pyruvate dehydrogenase kinase (phosphorylating); pyruvate dehydrogenase kinase activator protein; STK1
Systematic name: ATP:[pyruvate dehydrogenase (acetyl-transferring)] phosphotransferase
Comments: The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. Phosphorylation inactivates EC, pyruvate dehydrogenase (acetyl-transferring).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9074-01-5
1.  Linn, T.C., Pelley, J.W., Petit, F.H., Hucho, F., Randall, D.D. and Reed, L.J. α-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart. Arch. Biochem. Biophys. 148 (1972) 327–342. [DOI] [PMID: 4401694]
2.  Reed, L.J., Damuni, Z. and Merryfield, M.L. Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation. Curr. Top. Cell. Regul. 27 (1985) 41–49. [DOI] [PMID: 3004826]
3.  Tovar-Mendez, A., Hirani, T.A., Miernyk, J.A. and Randall, D.D. Analysis of the catalytic mechanism of pyruvate dehydrogenase kinase. Arch. Biochem. Biophys. 434 (2005) 159–168. [DOI] [PMID: 15629119]
4.  Bao, H., Kasten, S.A., Yan, X., Hiromasa, Y. and Roche, T.E. Pyruvate dehydrogenase kinase isoform 2 activity stimulated by speeding up the rate of dissociation of ADP. Biochemistry 43 (2004) 13442–13451. [DOI] [PMID: 15491151]
5.  Roche, T.E., Hiromasa, Y., Turkan, A., Gong, X., Peng, T., Yan, X., Kasten, S.A., Bao, H. and Dong, J. Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1. Eur. J. Biochem. 270 (2003) 1050–1056. [DOI] [PMID: 12631265]
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