Polo kinase

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Polo kinase
Identifiers
EC number2.7.11.21
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

In enzymology, a polo kinase (EC 2.7.11.21) is a kinase enzyme i.e. one that catalyzes the chemical reaction

ATP + a protein ADP + a phosphoprotein

Thus, the two substrates of these enzymes are ATP and protein, whereas their two products are ADP and phosphoprotein.

These enzymes belong 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 [polo[-like] kinase] enzyme class is ATP:protein phosphotransferase (spindle-pole-dependent).

Examples and 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.

These enzymes participate in 3 metabolic pathways: cell cycle, cell cycle - yeast, and progesterone-mediated oocyte maturation.

Structural studies[edit]

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

References[edit]

  • Llamazares, Moreira, Tavares, et al. (1991). "polo encodes a protein kinase homolog required for mitosis in Drosophila". Genes Dev. 5 (12A): 2153–65. doi:10.1101/gad.5.12a.2153. PMID 1660828.
  • "Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila" 1993
  • 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 (6): 1617–28. doi:10.1083/jcb.129.6.1617. PMC 2291169. 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 (Pt 18): 3575–86. doi:10.1242/jcs.00031. PMID 12186944.
  • Ohkura H (2003). "Phosphorylation: polo kinase joins an elite club". Curr. Biol. 13 (23): R912–4. doi:10.1016/j.cub.2003.11.012. PMID 14654016.