Elongation factor 2 kinase

From Wikipedia, the free encyclopedia

In enzymology, an elongation factor 2 kinase (EC 2.7.11.20) is an enzyme that catalyzes the chemical reaction

ATP + [elongation factor 2] ADP + [elongation factor 2] phosphate

Thus, the two substrates of this enzyme are ATP and [[[elongation factor 2]]], whereas its two products are ADP and [[[elongation factor 2] phosphate]].

This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[elongation factor 2] phosphotransferase. Other names in common use include Ca/CaM-kinase III, calmodulin-dependent protein kinase III, CaM kinase III, eEF2 kinase, eEF2K, EF2K, and STK19.

[edit] References

• IUBMB entry for 2.7.11.20
• BRENDA references for 2.7.11.20 (Recommended.)
• PubMed references for 2.7.11.20
• PubMed Central references for 2.7.11.20
• Google Scholar references for 2.7.11.20
• Mitsui K, Brady M, Palfrey HC, Nairn AC (1993). "Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas". J. Biol. Chem. 268: 13422–33. PMID 8514778. 
• Hincke MT, Nairn AC (Pt 3). "Phosphorylation of elongation factor 2 during Ca(2+)-mediated secretion from rat parotid acini". Biochem. J. 282: 877–82. PMID 1372803. 
• Knebel A, Morrice N, Cohen P (2001). "A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta". EMBO. J. 20: 4360–9. doi:10.1093/emboj/20.16.4360. PMID 11500363. 
• Sans MD, Xie Q, Williams JA (2004). "Regulation of translation elongation and phosphorylation of eEF2 in rat pancreatic acini". Biochem. Biophys. Res. Commun. 319: 144–51. doi:10.1016/j.bbrc.2004.04.164. PMID 15158453. 
• Browne GJ, Finn SG, Proud CG (2004). "Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398". J. Biol. Chem. 279: 12220–31. doi:10.1074/jbc.M309773200. PMID 14709557. 
• Ryazanov AG (2002). "Elongation factor-2 kinase and its newly discovered relatives". FEBS. Lett. 514: 26–9. doi:10.1016/S0014-5793(02)02299-8. PMID 11904175. 

[edit] External links

• IUBMB entry for 2.7.11.20

• KEGG entry for 2.7.11.20

• BRENDA entry for 2.7.11.20

• NiceZyme view of 2.7.11.20

• EC2PDB: PDB structures for 2.7.11.20

• PRIAM entry for 2.7.11.20

• PUMA2 entry for 2.7.11.20

• IntEnz: Integrated Enzyme entry for 2.7.11.20

• MetaCyc entry for 2.7.11.20

• Atomic-resolution structures of enzymes belonging to this class
• MeSH Elongation+Factor+2+Kinase

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0004686: eukaryotic elongation factor-2 kinase

• AMIGO entry for GO code 0004686: eukaryotic elongation factor-2 kinase

v • d • e Kinases: Serine/threonine-specific protein kinases (primarily EC 2.7.11) 2.7.11 Pyruvate dehydrogenase kinase - Protein kinase A - Protein kinase G Protein kinase C (Protein kinase Mζ) G-protein coupled receptor kinases (Rhodopsin, Beta adrenergic receptor) Ca2+/calmodulin-dependent (Elongation factor 2 kinase, Myosin light-chain) Phosphorylase - Cyclin-dependent Mitogen-activated (Extracellular signal-regulated, C-Jun N-terminal (MAPK8, MAPK9), P38 mitogen-activated protein) MAP3K - GSK-3 - AMP-activated 2.7.12 MAP2K (1, 2, 3, 4, 5, 6, 7) 2.7.1.37, or unknown Anti-Mullerian hormone receptor - Ataxia telangiectasia mutated - Aurora (A, B) - Mammalian target of rapamycin - Bone morphogenetic protein receptors (1, 2) - CDKL5 - c-Raf - EIF-2 - Ribosomal s6 - Protein kinase B - PDK1