Myosin ATPase: Difference between revisions
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'''Myosin [[ATPase]]''' ({{EC number|3.6.4.1}}) is an [[enzyme]] with [[List of enzymes|systematic name]] ''ATP phosphohydrolase (actin-translocating)''.<ref>{{cite journal | vauthors = Rayment I | title = The structural basis of the myosin ATPase activity | journal = The Journal of Biological Chemistry | volume = 271 | issue = 27 | pages = 15850–3 | date = July 1996 | pmid = 8663496 | doi = 10.1074/jbc.271.27.15850 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Hasson T, Mooseker MS | title = Vertebrate unconventional myosins | journal = The Journal of Biological Chemistry | volume = 271 | issue = 28 | pages = 16431–4 | date = July 1996 | pmid = 8690736 | doi = 10.1074/jbc.271.28.16431 | doi-access = free }}</ref><ref>{{cite journal | vauthors = 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 | volume = 38 | issue = 12 | pages = 3785–92 | date = March 1999 | pmid = 10090768 | doi = 10.1021/bi9826815 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]] |
'''Myosin [[ATPase]]''' ({{EC number|3.6.4.1}}) is an [[enzyme]] with [[List of enzymes|systematic name]] ''ATP phosphohydrolase (actin-translocating)''.<ref>{{cite journal | vauthors = Rayment I | title = The structural basis of the myosin ATPase activity | journal = The Journal of Biological Chemistry | volume = 271 | issue = 27 | pages = 15850–3 | date = July 1996 | pmid = 8663496 | doi = 10.1074/jbc.271.27.15850 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Hasson T, Mooseker MS | title = Vertebrate unconventional myosins | journal = The Journal of Biological Chemistry | volume = 271 | issue = 28 | pages = 16431–4 | date = July 1996 | pmid = 8690736 | doi = 10.1074/jbc.271.28.16431 | doi-access = free }}</ref><ref>{{cite journal | vauthors = 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 | volume = 38 | issue = 12 | pages = 3785–92 | date = March 1999 | pmid = 10090768 | doi = 10.1021/bi9826815 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]: |
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: ATP + H<sub>2</sub>O <math>\rightleftharpoons</math> ADP + [[phosphate]] |
: ATP + H<sub>2</sub>O <math>\rightleftharpoons</math> ADP + [[phosphate]] |
Latest revision as of 03:03, 22 December 2023
Myosin ATPase | |||||||||
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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 | ||||||||
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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.
See also[edit]
References[edit]
- ^ 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.
- ^ 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.
- ^ 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.
External links[edit]
- Myosin+ATPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)