Miozin laki lanac kinaza
| Miozin laki lanac kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.7.11.18 | ||||||||
| CAS broj | 51845-53-5 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Miozin laki lanac kinaza (EC 2.7.11.18, (miozin-laki-lanac) kinaza, ATP:miozin-laki-lanac O-fosfotransferaza, kinaza kalcium/kalmodulin-zavisnog miozinskog lakog lanaca, MLCK, MLCKaza, miozinska kinaza, kinaza miozinskog lakog lanca, proteinska kinaza miozinskog lakog lanca, kinaza miozinskog lakog-lanca (fosforilacija), kinaza glatko mišičnog miozina lakog-lanca, STK18) je enzim sa sistematskim imenom ATP:(miozin laki lanac) O-fosfotransferaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + [miozin laki lanac] ADP + [miozin laki lanac] fosfat
Za rad ovog enzima je neophodan jon Ca2+ i kalmodulin.
Reference
- ↑ Adelstein, R.S. and Klee, C.B. (1981). „Purification and characterization of smooth muscle myosin light chain kinase”. J. Biol. Chem. 256: 7501-7509. PMID 6894756.
- ↑ Hathaway, D.R. and Adelstein, R.S. (1979). „Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity”. Proc. Natl. Acad. Sci. USA 76: 1653-1657. PMID 156362.
- ↑ Pires, E., Perry, S.V. and Thomas, M.A.W. (1974). „Myosin light-chain kinase, a new enzyme from striated muscle”. FEBS Lett. 41: 292-296. PMID 4853304.
- ↑ Nunnally, M.H., Rybicki, S.B. and Stull, J.T. (1985). „Characterization of chicken skeletal muscle myosin light chain kinase. Evidence for muscle-specific isozymes”. J. Biol. Chem. 260: 1020-1026. PMID 3881420.
- ↑ Edelman, A.M., Takio, K., Blumenthal, D.K., Hansen, R.S., Walsh, K.A., Titani, K. and Krebs, E.G. (1985). „Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase”. J. Biol. Chem. 260: 11275-11285. PMID 3897230.
- ↑ Mal, T.K., Skrynnikov, N.R., Yap, K.L., Kay, L.E. and Ikura, M. (2002). „Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR”. Biochemistry 41: 12899-12906. PMID 12390014.
- ↑ Sobieszek, A. (1999). „Enzyme kinetic characterization of the smooth muscle myosin phosphorylating system: activation by calcium and calmodulin and possible inhibitory mechanisms of antagonists”. Biochim. Biophys. Acta 1450: 77-91. PMID 10231558.
- ↑ Sobieszek, A., Borkowski, J. and Babiychuk, V.S. (1997). „Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex”. J. Biol. Chem. 272: 7034-7041. PMID 9054394.
- ↑ Fujita, K., Ye, L.H., Sato, M., Okagaki, T., Nagamachi, Y. and Kohama, K. (1999). „Myosin light chain kinase from skeletal muscle regulates an ATP-dependent interaction between actin and myosin by binding to actin”. Mol. Cell. Biochem. 190: 85-90. PMID 10098974.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Myosin-light-chain+kinase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
