Myosin-heavy-chain kinase

In enzymology, a myosin-heavy-chain kinase (EC 2.7.11.7) is an enzyme that catalyzes the chemical reaction

ATP + [myosin heavy-chain] ${\displaystyle \rightleftharpoons }$ ADP + [myosin heavy-chain] phosphate

Thus, the two substrates of this enzyme are ATP and myosin heavy-chain, whereas its two products are ADP and myosin heavy-chain phosphate.

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:[myosin heavy-chain] O-phosphotransferase. Other names in common use include

• 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.

References

• Cote GP, Bukiejko U (1987). "Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum". J. Biol. Chem. 262 (3): 1065–72. doi:10.1016/S0021-9258(19)75750-0. PMID 3027076.
• Hammer JA III, Albanesi JP, Korn ED (1983). "Purification and characterization of a myosin I heavy chain kinase from Acanthamoeba castellanii". J. Biol. Chem. 258 (16): 10168–75. doi:10.1016/S0021-9258(17)44620-5. PMID 6309772.
• Rieker JP, Swanljung-Collins H, Collins JH (1987). "Purification and characterization of a calmodulin-dependent myosin heavy chain kinase from intestinal brush border". J. Biol. Chem. 262 (31): 15262–8. doi:10.1016/S0021-9258(18)48169-0. PMID 2822719.
• Ravid S, Spudich JA (1989). "Myosin heavy chain kinase from developed Dictyostelium cells Purification and characterization". J. Biol. Chem. 264 (25): 15144–50. doi:10.1016/S0021-9258(18)63823-2. PMID 2549052.
• Brzeska H, Lynch TJ, Martin B, Corigliano-Murphy A, Korn ED (1990). "Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides". J. Biol. Chem. 265 (27): 16138–44. doi:10.1016/S0021-9258(17)46199-0. PMID 2168881.
• Ravid S, Spudich JA (1992). "Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally regulated substrate-specific member of the protein kinase C family". Proc. Natl. Acad. Sci. U.S.A. 89 (13): 5877–81. Bibcode:1992PNAS...89.5877R. doi:10.1073/pnas.89.13.5877. PMC 49400. PMID 1321427.
• Futey LM, Medley QG, Cote GP, Egelhoff TT (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 beta-subunit of heterotrimeric G proteins". J. Biol. Chem. 270 (2): 523–9. doi:10.1074/jbc.270.2.523. PMID 7822274.
• Korn ED, 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. U.S.A. 95 (8): 4146–51. Bibcode:1998PNAS...95.4146S. doi:10.1073/pnas.95.8.4146. PMC 22456. PMID 9539704.
• Egelhoff TT, Croft D, Steimle PA (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 (4): 2879–87. doi:10.1074/jbc.M410803200. PMID 15545285.