Kinaza teškog lanca miozina
(Preusmjereno sa stranice MIHC kinaza)
Kinaza teškog lanca miozina | |||||||||
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Identifikatori | |||||||||
EC broj | 2.7.11.7 | ||||||||
CAS broj | 64763-54-8 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Kinaza teškog lanca miozina (EC 2.7.11.7, ATP:miozin-teški lanac O-fosfotransferaza, kalmodulin-zavisni miozin teški lanac kinaza, MHCK, MIHC kinaza, miozin teški lanac kinaza, miozin I teški-lanac kinaza, miozin II teški-lanac kinaza, (miozin-teški-lanac) kinaza, miozin teški lanac kinaza A, STK6) je enzim sa sistematskim imenom ATP:(miozin teškog lanca) O-fosfotransferaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
Enzim iz Dictyostelium sp. (sluzave plesni) fosforiliše teške lance Dictyostelium miozin, čime inhibira aktinom aktiviranju ATPaznu aktivnost miozina.
- ↑ Côté, G.P. and Bukiejko, U. (1987). „Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum”. J. Biol. Chem. 262: 1065-1072. PMID 3027076.
- ↑ Hammer, J.A., 3rd, A lbanesi, J.P. and Korn, E.D. (1983). „Purification and characterization of a myosin I heavy chain kinase from Acanthamoeba castellanii”. J. Biol. Chem. 258: 10168-10175. PMID 6309772.
- ↑ Rieker, J.P., Swanljung-Collins, H. and Collins, J.H. (1987). „Purification and characterization of a calmodulin-dependent myosin heavy chain kinase from intestinal brush border”. J. Biol. Chem. 262: 15262-15268. PMID 2822719.
- ↑ Ravid, S. and Spudich, J.A. (1989). „Myosin heavy chain kinase from developed Dictyostelium cells. Purification and characterization”. J. Biol. Chem. 264: 15144-15150. PMID 2549052.
- ↑ Brzeska, H., Lynch, T.J., Martin, B., Corigliano-Murphy, A. and Korn, E.D. (1990). „Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides”. J. Biol. Chem. 265: 16138-16144. PMID 2168881.
- ↑ Ravid, S. and Spudich, J.A. (1992). „Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally regulated substrate-specific member of the protein kinase C family”. Proc. Natl. Acad. Sci. USA 89: 5877-5881. PMID 1321427.
- ↑ Futey, L.M., Medley, Q.G., Côté, G.P. and Egelhoff, T.T. (1995). „Structural analysis of myosin heavy chain kinase A from Dictyostelium. Evidence for a highly divergent protein kinase domain, an amino-terminal coiled-coil domain, and a domain homologous to the β-subunit of heterotrimeric G proteins”. J. Biol. Chem. 270: 523-529. PMID 7822274.
- ↑ Szczepanowska, J., Zhang, X., Herring, C.J., Qin, J., Korn, E.D. and Brzeska, H. (1998). „Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain of Acanthamoeba myosin I heavy chain kinase”. Proc. Natl. Acad. Sci. USA 95: 4146-4151. PMID 9539704.
- ↑ Egelhoff, T.T., Croft, D. and Steimle, P.A. (2005). „Actin activation of myosin heavy chain kinase A in Dictyostelium: a biochemical mechanism for the spatial regulation of myosin II filament disassembly”. J. Biol. Chem. 280: 2879-2887. PMID 15545285.
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