Dual-specificity kinase

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

ATP + a protein ADP + a phosphoprotein

on two different residues, most frequently on Ser or Thr residues, as in the case of MAP3Ks in the MAP kinase signaling pathway in mammals (while the proteins they phosphorylate, MEKs, are Ser/Tyr specific), 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). This enzyme participates in the yeast cell cycle.

Nomenclature

The systematic name of this enzyme class is ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating). Some common kinases with dual specificity include

• ADK1
• Arabidopsis dual specificity kinase 1
• CLK1
• dDYRK2
• Mps1p

References

• 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.