Myosin-heavy-chain kinase
| myosin heavy chain kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.11.7 | ||||||||
| CAS no. | 64763-54-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a myosin-heavy-chain kinase (EC 2.7.11.7) is an enzyme that catalyzes the chemical reaction
- ATP + [myosin heavy-chain] 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
[edit]- 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.
