| Entry |
|
| Name |
myosin-heavy-chain kinase;
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
|
| Class |
Transferases;
Transferring phosphorus-containing groups;
Protein-serine/threonine kinases
 |
| Sysname |
ATP:[myosin heavy-chain] O-phosphotransferase
|
| Reaction(IUBMB) |
ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate
|
| Reaction(KEGG) |
|
| Substrate |
ATP [CPD: C00002];
[myosin heavy-chain]
|
| Product |
|
| Comment |
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.
|
| Orthology |
| myosin-heavy-chain kinase |
|
| Genes |
TBR: | | TCR: | | LMA: | | LIF: | | LDO: | | LMI: | | LBZ: | |
 |
| Reference |
|
| Authors |
Cote GP, Bukiejko U. |
| Title |
Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum. |
| Journal |
J. Biol. Chem. 262 (1987) 1065-72. |
| Organism |
Dictyostelium discoideum [GN: ddi] |
| Reference |
|
| Authors |
Hammer JA 3rd, Albanesi JP, Korn ED. |
| Title |
Purification and characterization of a myosin I heavy chain kinase from Acanthamoeba castellanii. |
| Journal |
J. Biol. Chem. 258 (1983) 10168-75. |
| Organism |
Acanthamoeba castellanii |
| Reference |
|
| Authors |
Rieker JP, Swanljung-Collins H, Collins JH. |
| Title |
Purification and characterization of a calmodulin-dependent myosin heavy chain kinase from intestinal brush border. |
| Journal |
J. Biol. Chem. 262 (1987) 15262-8. |
| Organism |
|
| Reference |
|
| Authors |
Ravid S, Spudich JA. |
| Title |
Myosin heavy chain kinase from developed Dictyostelium cells. Purification and characterization. |
| Journal |
J. Biol. Chem. 264 (1989) 15144-50. |
| Organism |
Dictyostelium discoideum [GN: ddi] |
| Reference |
|
| Authors |
Brzeska H, Lynch TJ, Martin B, Corigliano-Murphy A, Korn ED. |
| Title |
Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides. |
| Journal |
J. Biol. Chem. 265 (1990) 16138-44. |
| Organism |
Acanthamoeba castellanii |
| Reference |
|
| Authors |
Ravid S, Spudich JA. |
| Title |
Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally regulated substrate-specific member of the protein kinase C family. |
| Journal |
Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 5877-81. |
| Organism |
Dictyostelium discoideum [GN: ddi] |
| Reference |
|
| Authors |
Futey LM, Medley QG, Cote GP, Egelhoff TT. |
| Title |
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. |
| Journal |
J. Biol. Chem. 270 (1995) 523-9. |
| Organism |
Dictyostelium discoideum [GN: ddi] |
| Reference |
|
| Authors |
Szczepanowska J, Ramachandran U, Herring CJ, Gruschus JM, Qin J, Korn ED, Brzeska H. |
| Title |
Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain of Acanthamoeba myosin I heavy chain kinase. |
| Journal |
Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 4146-51. |
| Organism |
Acanthamoeba castellanii |
| Reference |
|
| Authors |
Egelhoff TT, Croft D, Steimle PA. |
| Title |
Actin activation of myosin heavy chain kinase A in Dictyostelium: a biochemical mechanism for the spatial regulation of myosin II filament disassembly. |
| Journal |
J. Biol. Chem. 280 (2005) 2879-87. |
| Organism |
Dictyostelium discoideum [GN: ddi] |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 64763-54-8 |