Myosin ATPase
| Myosin ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.4.1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Myosin ATPase (EC 3.6.4.1) is an enzyme with systematic name ATP phosphohydrolase (actin-translocating).[1][2][3] This enzyme catalyses the following chemical reaction
- ATP + H2O ADP + phosphate
ATP hydrolysis provides energy for actomyosin contraction.
References
- ^ Rayment I (July 1996). "The structural basis of the myosin ATPase activity". The Journal of Biological Chemistry. 271 (27): 15850–3. doi:10.1074/jbc.271.27.15850. PMID 8663496.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Hasson T, Mooseker MS (July 1996). "Vertebrate unconventional myosins". The Journal of Biological Chemistry. 271 (28): 16431–4. doi:10.1074/jbc.271.28.16431. PMID 8690736.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Murphy CT, Spudich JA (March 1999). "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". Biochemistry. 38 (12): 3785–92. doi:10.1021/bi9826815. PMID 10090768.
See also
External links
- Myosin+ATPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)