Dual-specificity kinase

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In enzymology, a dual-specificity kinase (EC 2.7.12.1) is an enzyme that catalyzes the chemical reaction

ATP + a protein $\rightleftharpoons$ ADP + a phosphoprotein

on two different residues, most frequently on Ser or Thr residues, as in the case of MEK in the MAP kinase signaling pathway in mammalians, or phosphatidyl-(3,4,5)-inositol-3-kinase (PI3K). One example of a non-dual specificity kinase is the cAMP-dependent protein kinase, also known as PKA, which phosphorylates a serine in the context of a random-coiled recognition motif called kinase inducible domain (KID).

. The systematic name of this enzyme class is ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating). Other names in common use include ADK1, Arabidopsis dual specificity kinase 1, CLK1, dDYRK2, and Mps1p. This enzyme participates in cell cycle - yeast.

[edit] References

IUBMB entry for 2.7.12.1
BRENDA references for 2.7.12.1 (Recommended.)
PubMed references for 2.7.12.1
PubMed Central references for 2.7.12.1
Google Scholar references for 2.7.12.1
Ali N, Halfter U, Chua NH (1994). "Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine, and tyrosine". J. Biol. Chem. 269: 31626–9. PMID 7527390.
Lauze E, Stoelcker B, Luca FC, Weiss E, Schutz AR, Winey M (1995). "Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase". EMBO. J. 14: 1655–63. PMID 7737118.
Menegay HJ, Myers MP, Moeslein FM, Landreth GE (Pt 18). "Biochemical characterization and localization of the dual specificity kinase CLK1". J. Cell. Sci. 113: 3241–53. PMID 10954422.
Cleghon V (2003). "dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated kinase in Drosophila". Biochem. J. 374: 381–91. doi:10.1042/BJ20030500. PMID 12786602.