ミオシンATPアーゼ
- 関
- myosin
WordNet
- the commonest protein in muscle; a globulin that combines with actin to form actomyosin
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/11/23 22:39:00」(JST)
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Myosin ATPase |
Identifiers |
EC number |
3.6.4.1 |
Databases |
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IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
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KEGG |
KEGG entry |
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metabolic pathway |
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profile |
PDB structures |
RCSB PDB PDBe PDBsum |
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articles |
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proteins |
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Myosin ATPase (EC 3.6.4.1) is an enzyme with system 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[edit]
- ^ Rayment, I. (1996). "The structural basis of myosin ATPase activity". J. Biol. Chem. 271: 15850–15853. PMID 8663496.
- ^ Hasson, T. and Mooseker, M.S. (1996). "Vertebrate unconventional myosins". J. Biol. Chem. 271: 16431–16434. PMID 8690736.
- ^ Murphy, C.T. and Spudich, J.A. (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: 3785–3792. PMID 10090768.
See also[edit]
External links[edit]
- Myosin ATPase at the US National Library of Medicine Medical Subject Headings (MeSH)
UpToDate Contents
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English Journal
- Physicochemical properties of natural actomyosin from threadfin bream (Nemipterus spp.) induced by high hydrostatic pressure.
- Zhou A1, Lin L2, Liang Y2, Benjakul S3, Shi X2, Liu X2.
- Food chemistry.Food Chem.2014 Aug 1;156:402-7. doi: 10.1016/j.foodchem.2014.02.013. Epub 2014 Feb 12.
- Changes of physicochemical properties in natural actomyosin (NAM) from threadfin bream (Nemipterus spp.) induced by high hydrostatic pressure (200, 400, 600MPa for 10, 30, 50min) were studied. The increase in turbidity of NAM was coincidental with the decrease in protein solubility with increasing p
- PMID 24629987
- P115Pak1 is required to maintain ventricular Ca2+ homeostasis and electrophysiological stability through SERCA2a regulation in mice.
- Wang Y1, Tsui H1, Ke Y2, Terrar D1, Huang CL3, Solaro RJ2, Wang X4, Lei M1; ISHR.
- Cardiovascular research.Cardiovasc Res.2014 Jul 15;103 Suppl 1:S20. doi: 10.1093/cvr/cvu082.56. Epub 2014 Jun 27.
- PURPOSE: Impaired sarcoplasmic reticular (SR) Ca2+ uptake resulting from decreased SR Ca2+-ATPase type 2a (SERCA2a) expression or activity is characteristic of heart failure (HF) with its associated ventricular arrhythmias. Recent attempts at gene therapy of these conditions explored strategies enha
- PMID 25020537
- Gene-specific increase in the energetic cost of contraction in hypertrophic cardiomyopathy caused by thick filament mutations.
- Witjas-Paalberends ER1, Güçlü A2, Germans T3, Knaapen P3, Harms HJ4, Vermeer AM5, Christiaans I5, Wilde AA6, Dos Remedios C7, Lammertsma AA4, van Rossum AC3, Stienen GJ8, van Slegtenhorst M9, Schinkel AF10, Michels M10, Ho CY11, Poggesi C12, van der Velden J13.
- Cardiovascular research.Cardiovasc Res.2014 Jul 15;103(2):248-57. doi: 10.1093/cvr/cvu127. Epub 2014 May 16.
- AIMS: Disease mechanisms regarding hypertrophic cardiomyopathy (HCM) are largely unknown and disease onset varies. Sarcomere mutations might induce energy depletion for which until now there is no direct evidence at sarcomere level in human HCM. This study investigated if mutations in genes encoding
- PMID 24835277
Japanese Journal
- Molecular machines directly observed by high-speed atomic force microscopy
- Ando Toshio
- FEBS Letters 587(3), 997-1007, 2013-04-17
- … The captured images of myosin V, F1-ATPase, and bacteriorhodopsin have enabled their dynamic processes and structure dynamics to be revealed in great detail, giving unique and deep insights into their functional mechanisms. …
- NAID 120005304730
- Molecular machines directly observed by high-speed atomic force microscopy
- Ando Toshio
- FEBS Letters 587(8), 997-1007, 2013-04-17
- … The captured images of myosin V, F1-ATPase, and bacteriorhodopsin have enabled their dynamic processes and structure dynamics to be revealed in great detail, giving unique and deep insights into their functional mechanisms. …
- NAID 120005253832
- Myosin denaturation in heated myofibrils of scallop adductor muscle
- Satoh Aiko,Kinoshita Yasunori,Konno Kunihiko
- Fisheries Science 79(2), 341-347, 2013-03
- … Thermal inactivation of Ca2+-ATPase of scallop myofibrils (0.1 M KCl, pH 7.5) was unaffected by the presence of Ca2+. … Monomeric myosin and salt-solubility one decreased much faster than Ca2+-ATPase inactivation in both Ca-, and EDTA-media, which was well explained by the faster rod denaturation than subfragment-1 (S-1) denaturation. …
- NAID 120005228080
Related Links
- Myosin atpase Home » Myosin atpase myosin atpase (Science: enzyme) An enzyme that catalyses the hydrolysis of myosin aTP in the presence of actin to form myosin aDP ...
- Each myosin motor protein possesses ATPase activity and functions in a cyclical manner that couples ATP binding and hydrolysis to a conformational change in the protein. This process is known as the ‘powerstroke cycle’ (reviewed ...
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- 英
- myosin ATPase
- 関
- ミオシン
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- 同
- ATP hydrolase
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- アデノシン三リン酸