| Entry |
|
| Name |
myosin ATPase
|
| Class |
Hydrolases;
Acting on acid anhydrides;
Acting on acid anhydrides to facilitate cellular and subcellular movement
 |
| Sysname |
ATP phosphohydrolase (actin-translocating)
|
| Reaction(IUBMB) |
ATP + H2O = ADP + phosphate [RN: R00086]
|
| Reaction(KEGG) |
|
| Substrate |
|
| Product |
|
| Comment |
Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15-27 kDa). The head region of the heavy chain contains actin- and ATP-binding sites. ATP hydrolysis provides energy for actomyosin contraction.
|
| Pathway |
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| Orthology |
|
| Genes |
 |
| Reference |
|
| Authors |
Rayment I. |
| Title |
The structural basis of the myosin ATPase activity. |
| Journal |
J. Biol. Chem. 271 (1996) 15850-3. |
| Organism |
Dictyostelium discoideum [GN: ddi] |
| Reference |
|
| Authors |
Hasson T, Mooseker MS. |
| Title |
Vertebrate unconventional myosins. |
| Journal |
J. Biol. Chem. 271 (1996) 16431-4. |
| Organism |
Homo sapiens [GN: hsa], Mus musculus [GN: mmu], Rattus norvegicus [GN: rno], Gallus gallus [GN: gga] |
| Reference |
|
| Authors |
Murphy CT, Spudich JA. |
| Title |
The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity. |
| Journal |
Biochemistry. 38 (1999) 3785-92. |
| Organism |
Gallus gallus [GN: gga], Oryctolagus cuniculus, Dictyostelium sp. |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |