EC 2.7.11.2 - [pyruvate dehydrogenase (acetyl-transferring)] kinase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 2.7.11.2

Names

Accepted name:
[pyruvate dehydrogenase (acetyl-transferring)] kinase
Other names:
pyruvate dehydrogenase kinase
pyruvate dehydrogenase kinase (phosphorylating)
PDH kinase
PDHK
PDK
PDK1
PDK2
PDK3
PDK4
pyruvate dehydrogenase kinase activator protein
STK1
Systematic name:
ATP:[pyruvate 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 pyruvate dehydrogenase complex in mammals. Phosphorylation inactivates EC 1.2.4.1, pyruvate dehydrogenase (acetyl-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:0004740
CAS Registry Number: 9074-01-5
UniProtKB/Swiss-Prot: (20) [show] [UniProt]

References

  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: 327-342 (1972). [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: 41-49 (1985). [PMID: 3004826]
  3. Tovar-Méndez, A., Hirani, T.A., Miernyk, J.A. and Randall, D.D.
    Analysis of the catalytic mechanism of pyruvate dehydrogenase kinase.
    Arch. Biochem. Biophys. 434: 159-168 (2005). [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: 13442-13451 (2004). [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: 1050-1056 (2003). [PMID: 12631265]

[EC 2.7.11.2 created 1978 as EC 2.7.1.99, transferred 2005 to EC 2.7.11.2]