EC 2.7.11.7 - Myosin-heavy-chain kinase

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IntEnz Enzyme Nomenclature
EC 2.7.11.7

Names

Accepted name:
myosin-heavy-chain kinase
Other names:
ATP:myosin-heavy-chain O-phosphotransferase
[myosin-heavy-chain] kinase
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 A
STK6
Systematic name:
ATP:[myosin heavy-chain] O-phosphotransferase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00100 , PROSITE:PDOC51158
Structural data: CSA , EC2PDB
Gene Ontology: GO:0016905
CAS Registry Number: 64763-54-8
UniProtKB/Swiss-Prot:

References

  1. Côté, G.P. and Bukiejko, U.
    Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum.
    J. Biol. Chem. 262: 1065-1072 (1987). [PMID: 3027076]
  2. Hammer, J.A., 3rd, Albanesi, J.P. and Korn, E.D.
    Purification and characterization of a myosin I heavy chain kinase from Acanthamoeba castellanii.
    J. Biol. Chem. 258: 10168-10175 (1983). [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: 15262-15268 (1987). [PMID: 2822719]
  4. Ravid, S. and Spudich, J.A.
    Myosin heavy chain kinase from developed Dictyostelium cells. Purification and characterization.
    J. Biol. Chem. 264: 15144-15150 (1989). [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: 16138-16144 (1990). [PMID: 2168881]
  6. Ravid, S., 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: 5877-5881 (1992). [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: 523-529 (1995). [PMID: 7822274]
  8. Szczepanowska, J., Ramachandran, U., Herring, C.J., Gruschus, J.M., 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: 4146-4151 (1998). [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: 2879-2887 (2005). [PMID: 15545285]

[EC 2.7.11.7 created 1990 as EC 2.7.1.129, transferred 2005 to EC 2.7.11.7]