The Enzyme Database

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Accepted name: myosin-heavy-chain kinase
Reaction: ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
Other name(s): ATP:myosin-heavy-chain O-phosphotransferase; calmodulin-dependent myosin heavy chain kinase; MHCK; MIHC kinase; myosin heavy chain kinase; myosin I heavy-chain kinase; myosin II heavy-chain kinase; [myosin-heavy-chain] kinase; myosin heavy chain kinase A; STK6
Systematic name: ATP:[myosin heavy-chain] O-phosphotransferase
Comments: The enzyme from Dictyostelium sp. (slime moulds) brings about phosphorylation of the heavy chains of Dictyostelium myosin, inhibiting the actin-activated ATPase activity of the myosin. One threonine residue in each heavy chain acts as acceptor. While the enzyme from some species is activated by actin, in other cases Ca2+/calmodulin are required for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64763-54-8
1.  Côté, G.P. and Bukiejko, U. Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum. J. Biol. Chem. 262 (1987) 1065–1072. [PMID: 3027076]
2.  Hammer, J.A., 3rd, A lbanesi, J.P. and Korn, E.D. Purification and characterization of a myosin I heavy chain kinase from Acanthamoeba castellanii. J. Biol. Chem. 258 (1983) 10168–10175. [PMID: 6309772]
3.  Rieker, J.P., Swanljung-Collins, H. and Collins, J.H. Purification and characterization of a calmodulin-dependent myosin heavy chain kinase from intestinal brush border. J. Biol. Chem. 262 (1987) 15262–15268. [PMID: 2822719]
4.  Ravid, S. and Spudich, J.A. Myosin heavy chain kinase from developed Dictyostelium cells. Purification and characterization. J. Biol. Chem. 264 (1989) 15144–15150. [PMID: 2549052]
5.  Brzeska, H., Lynch, T.J., Martin, B., Corigliano-Murphy, A. and Korn, E.D. Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides. J. Biol. Chem. 265 (1990) 16138–16144. [PMID: 2168881]
6.  Ravid, S. and Spudich, J.A. 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 (1992) 5877–5881. [PMID: 1321427]
7.  Futey, L.M., Medley, Q.G., Côté, G.P. and Egelhoff, T.T. 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 (1995) 523–529. [PMID: 7822274]
8.  Szczepanowska, J., Zhang, X., Herring, C.J., Qin, J., Korn, E.D. and Brzeska, H. 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 (1998) 4146–4151. [PMID: 9539704]
9.  Egelhoff, T.T., Croft, D. and Steimle, P.A. 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 (2005) 2879–2887. [PMID: 15545285]
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