EC |
5.6.1.8 |
Accepted name: |
myosin ATPase |
Reaction: |
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1 |
Systematic name: |
ATP phosphohydrolase (actin-translocating) |
Comments: |
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. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Rayment, I. The structural basis of myosin ATPase activity. J. Biol. Chem. 271 (1996) 15850–15853. [DOI] [PMID: 8663496] |
2. |
Hasson, T. and Mooseker, M.S. Vertebrate unconventional myosins. J. Biol. Chem. 271 (1996) 16431–16434. [DOI] [PMID: 8690736] |
3. |
Murphy, C.T. and Spudich, J.A. 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 (1999) 3785–3792. [DOI] [PMID: 10090768] |
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[EC 5.6.1.8 created 1984 as EC 3.6.1.32, transferred 2000 to EC 3.6.4.1, transferred 2018 to EC 5.6.1.8] |
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