EC 2.7.11.4 - [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase

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IntEnz Enzyme Nomenclature
EC 2.7.11.4

Names

Accepted name:
[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase
Other names:
branched-chain 2-oxo acid dehydrogenase kinase
branched-chain α-ketoacid dehydrogenase kinase
branched-chain keto acid dehydrogenase kinase
branched-chain oxo acid dehydrogenase kinase (phosphorylating)
BCK
BCKD kinase
BCODH kinase
STK2
Systematic name:
ATP:[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphotransferase

Reaction

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 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC50109
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047323
CAS Registry Number: 82391-38-6
UniProtKB/Swiss-Prot:

References

  1. Paxton, R. and Harris, R.A.
    Isolation of rabbit liver branched chain α-ketoacid dehydrogenase and regulation by phosphorylation.
    J. Biol. Chem. 257: 14433-14439 (1982). [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: 30512-30519 (2000). [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: 36905-36908 (2002). [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: 105-111 (1997). [PMID: 9344245]

[EC 2.7.11.3 created 1986 as EC 2.7.1.115, transferred 2005 to EC 2.7.11.3]