Miozin laki lanac kinaza

Miozin laki lanac kinaza
Identifikatori
EC broj2.7.11.18
CAS broj51845-53-5
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum

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

  1. ^ Adelstein, R.S. & Klee, C.B. (1981). „Purification and characterization of smooth muscle myosin light chain kinase”. J. Biol. Chem. 256: 7501—7509. PMID 6894756. 
  2. ^ Hathaway, D.R. & 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. 
  3. ^ 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. 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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. 
  9. ^ 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

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