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myosin heavy chain kinase
EC number
CAS number 64763-54-8
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures
Gene Ontology AmiGO / EGO

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

ATP + [myosin heavy-chain] \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.


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  • Hammer JA 3rd Albanesi JP, Korn ED (1983). "Purification and characterization of a myosin I heavy chain kinase from Acanthamoeba castellanii". J. Biol. Chem. 258: 10168–75. 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: 15262–8. PMID 2822719.  
  • Ravid S, Spudich JA (1989). "Myosin heavy chain kinase from developed Dictyostelium cells Purification and characterization". J. Biol. Chem. 264: 15144–50. 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: 16138–44. 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: 5877–81. doi:10.1073/pnas.89.13.5877. 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: 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: 4146–51. doi:10.1073/pnas.95.8.4146. 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: 2879–87. doi:10.1074/jbc.M410803200. PMID 15545285.  


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