The Enzyme Database

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Accepted name: [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase
Reaction: ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] = ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
Other name(s): BCK; BCKD kinase; BCODH kinase; branched-chain α-ketoacid dehydrogenase kinase; branched-chain 2-oxo acid dehydrogenase kinase; branched-chain keto acid dehydrogenase kinase; branched-chain oxo acid dehydrogenase kinase (phosphorylating); STK2
Systematic name: ATP:[3-methyl-2-oxobutanoate 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 branched-chain 2-oxoacid dehydrogenase complex. Phosphorylation inactivates EC, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 82391-38-6
1.  Paxton, R. and Harris, R.A. Isolation of rabbit liver branched chain α-ketoacid dehydrogenase and regulation by phosphorylation. J. Biol. Chem. 257 (1982) 14433–14439. [PMID: 7142221]
2.  Wynn, R.M., Chuang, J.L., Cote, C.D. and Chuang, D.T. Tetrameric assembly and conservation in the ATP-binding domain of rat branched-chain α-ketoacid dehydrogenase kinase. J. Biol. Chem. 275 (2000) 30512–30519. [DOI] [PMID: 10903321]
3.  Chuang, J.L., Wynn, R.M. and Chuang, D.T. The C-terminal hinge region of lipoic acid-bearing domain of E2b is essential for domain interaction with branched-chain α-keto acid dehydrogenase kinase. J. Biol. Chem. 277 (2002) 36905–36908. [DOI] [PMID: 12189132]
4.  Popov, K.M., Hawes, J.W. and Harris, R.A. Mitochondrial α-ketoacid dehydrogenase kinases: a new family of protein kinases. Adv. Second Messenger Phosphoprotein Res. 31 (1997) 105–111. [PMID: 9344245]
[EC created 1986 as EC, transferred 2005 to EC]

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