Difference between revisions of "Polo kinase"

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Latest revision as of 17:58, 26 December 2007

In enzymology, a polo kinase (EC is an enzyme that catalyzes the chemical reaction

ATP + a protein ADP + a phosphoprotein

Thus, the two substrates of this enzyme are ATP and protein, whereas its two products are ADP and phosphoprotein.

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:protein phosphotransferase (spindle-pole-dependent). Other names in common use include Cdc5, Cdc5p, Plk, PLK, Plk1, Plo1, POLO kinase, polo serine-threonine kinase, polo-like kinase, polo-like kinase 1, serine/threonine-specific Drosophila kinase polo, and STK21. This enzyme participates in 3 metabolic pathways: cell cycle, cell cycle - yeast, and progesterone-mediated oocyte maturation.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2OGQ, 2OJS, 2OJX, 2OU7, and 2OWB.


  • IUBMB entry for
  • BRENDA references for (Recommended.)
  • PubMed references for
  • PubMed Central references for
  • Google Scholar references for
  • C, Karess RE, Glover DM, Sunkel CE (1991). "polo encodes a protein kinase homolog required for mitosis in Drosophila". Genes. Dev. 5: 2153&ndash, 65. PMID 1660828.
  • Golsteyn RM, Mundt KE, Fry AM, Nigg EA (1995). "Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function". J. Cell. Biol. 129: 1617&ndash, 28. PMID 7790358.
  • Mulvihill DP, Hyams JS (2002). "Cytokinetic actomyosin ring formation and septation in fission yeast are dependent on the full recruitment of the polo-like kinase Plo1 to the spindle pole body and a functional spindle assembly checkpoint". J. Cell. Sci. 115: 3575&ndash, 86. PMID 12186944.
  • Ohkura H (2003). "Phosphorylation: polo kinase joins an elite club". Curr. Biol. 13: R912&ndash, 4. PMID 14654016.

External links