In enzymology, a tau-protein kinase (EC 2.7.11.26) is an enzyme that catalyzes the chemical reaction
tau-protein kinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.11.26 | ||||||||
CAS no. | 111694-09-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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- ATP + tau protein ADP + O-phospho-tau-protein
Thus, the two substrates of this enzyme are ATP and tau protein, whereas its two products are ADP and O-phospho-tau-protein.
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). This enzyme participates in 14 metabolic pathways: erbb signaling pathway, cell cycle, wnt signaling pathway, hedgehog signaling pathway, axon guidance, focal adhesion, b cell receptor signaling pathway, insulin signaling pathway, melanogenesis, alzheimer's disease, colorectal cancer, endometrial cancer, prostate cancer, and basal cell carcinoma.
Nomenclature edit
The systematic name of this enzyme class is ATP:[tau-protein] O-phosphotransferase. Other names in common use include ATP:tau-protein O-hosphotransferase, brain protein kinase PK40erk, cdk5/p20, CDK5/p23, glycogen synthase kinase-3beta, GSK, protein tau kinase, STK31, tau kinase, [tau-protein] kinase, tau-protein kinase I, tau-protein kinase II, tau-tubulin kinase, TPK, TPK I, TPK II, and TTK.
Structural studies edit
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2JDO, 2JDR, and 2UW9.
Examples edit
Human genes encoding proteins with Tau-protein kinase activity include:
References edit
- Ishiguro K, Ihara Y, Uchida T, Imahori K (September 1988). "A novel tubulin-dependent protein kinase forming a paired helical filament epitope on tau". J. Biochem. 104 (3). Tokyo: 319–21. doi:10.1093/oxfordjournals.jbchem.a122465. PMID 2467901.
- Lund ET, McKenna R, Evans DB, Sharma SK, Mathews WR (2001). "Characterization of the in vitro phosphorylation of human tau by tau protein kinase II (cdk5/p20) using mass spectrometry". J. Neurochem. 76 (4): 1221–32. doi:10.1046/j.1471-4159.2001.00130.x. PMID 11181841. S2CID 24005862.
- Takashima A; Mercken, M; Murayama, M; Noguchi, K; Ishiguro, K; Imahori, K; Takashima, A (1998). "Characterization of tau phosphorylation in glycogen synthase kinase-3beta and cyclin dependent kinase-5 activator (p23) transfected cells". Biochim. Biophys. Acta. 1380 (2): 177–82. doi:10.1016/s0304-4165(97)00139-6. PMID 9565682.
- Sugio S, Kohno T, Matsuzaki T (November 2000). "Expression, purification and crystallization of human tau-protein kinase I/glycogen synthase kinase-3beta". Acta Crystallogr. D. 56 (Pt 11): 1464–5. doi:10.1107/S0907444900010386. PMID 11053853.