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
Pretraga
PMCčlanci
PubMedčlanci
NCBIproteini

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] ⇌ {\displaystyle \rightleftharpoons } 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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
  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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
  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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
  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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
  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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
  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. CS1 одржавање: Вишеструка имена: списак аутора (веза)

Literatura

  • Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097. 

Spoljašnje veze

  • Myosin-light-chain+kinase на US National Library of Medicine Medical Subject Headings (MeSH)
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(1) Serin/treonin-specifične proteinske kinaze (EC 2.7.11.1-EC 2.7.11.20)
Nespecifična serin/treonin proteinske kinaze (EC 2.7.11.1)
LATS1, LATS2, MAST1, MAST2, STK38, STK38L, CIT, ROCK1, SGK, SGK2, SGK3, Proteinska kinaza B (AKT1, AKT2, AKT3), Ataksija telangiektazija mutirani, Sisarski cilj rapamicina, EIF-2 kinaze (PKR, HRI), Wee1 (WEE1)
Piruvat dehidrogenazna kinaza (EC 2.7.11.2)
Defosfo-(reduktaza kinaza) kinaza (EC 2.7.11.3)
AMP-activated protein kinase,
(3-metil-2-oksobutanoat dehidrogenaza (prenos acetila)) (EC 2.7.11.4)
BCKDK, BCKDHA, BCKDHB
(izocitrat dehidrogenaza (NADP+)) kinaza (EC 2.7.11.5)
IDH2, IDH3A, IDH3B, IDH3G
tirozin 3-monooksigenazna kinaza (EC 2.7.11.6)
Miozin-teški-lanac kinaza (EC 2.7.11.7)
Aurora kinaza (Aurora A kinaza, Aurora B kinaza)
Fas-aktivirana serin/treoninska kinaza (EC 2.7.11.8)
Goodpasture-antigen-vezujuća proteinska kinaza (EC 2.7.11.9)
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IκB kinaza (EC 2.7.11.10)
CHUK, IKK2, TBK1, IKBKE, IKBKG, IKBKAP
cAMP-zavisna proteinska kinaza (EC 2.7.11.11)
Proteinska kinaza A, PRKACG, PRKACB, PRKACA, PRKY
cGMP-zavisna proteinska kinaza (EC 2.7.11.12)
Protein kinaza C (EC 2.7.11.13)
Protein kinaza C, Protein kinaza Cζ, PKC alfa, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, PRKCQ, Proteinska zavisna proteinska N1, PKN2, PKN3,
Rodopsinska kinaza (EC 2.7.11.14)
Beta adrenergički receptor kinaza (EC 2.7.11.15)
Beta adrenergički receptor kinaza, Beta adrenergički receptor kinaza-2
G protein spregnuti receptor kinaza (EC 2.7.11.16)
GRK4, GRK5, GRK6
Ca2+/kalmodulin-zavisna (EC 2.7.11.17)
BRSK2, CAMK1, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMK4, MLCK, CASK, CHEK1, CHEK2, DAPK1, DAPK2, DAPK3, STK11, MAPKAPK2, MAPKAPK3, MAPKAPK5, MARK1, MARK2, MARK3, MARK4, MELK, MKNK1, MKNK2, NUAK1, NUAK2, OBSCN, PASK, PHKG1, PHKG2, PIM1, PIM2, PKD1, PRKD2, PRKD3, PSKH1, SNF1LK2, KIAA0999, STK40, SNF1LK, SNRK, SPEG, TSSK2, Kalirin, TRIB1, TRIB2, TRIB3, TRIO, Titin, DCLK1
Miozin laki-lanac kinaza (EC 2.7.11.18)
MYLK, MYLK2, MYLK3, MYLK4
Fosforilazna kinaza (EC 2.7.11.19)
PHKA1, PHKA2, PHKB, PHKG1, PHKG2
Faktor elongacije 2 kinaza (EC 2.7.11.20)
Polo kinaza (EC 2.7.11.21)
PLK1, PLK2, PLK3, PLK4
(2) Serin/treonin-specifične proteinske kinaze (EC 2.7.11.21-EC 2.7.11.30)
Polo kinaza (EC 2.7.11.21)
PLK1, PLK2, PLK3, PLK4
Ciklin-zavisna kinaza (EC 2.7.11.22)
CDK1, CDK2, CDKL2, CDK3, CDK4, CDK5, CDKL5, CDK6, CDK7, CDK8, CDK9, CDK10, CDC2L5, CRKRS, PCTK1, PCTK2, PCTK3, PFTK1, CDC2L1
(RNK-polimerazna)-podjedinica kinaza (EC 2.7.11.23)
RPS6KA5, RPS6KA4, P70S6 kinaza, P70-S6 kinaza 1, RPS6KB2, RPS6KA2, RPS6KA3, RPS6KA1, RPS6KC1
Mitogenom-aktivirana proteinska kinaza (EC 2.7.11.24)
Ekstracelularnim signalom regulisane (MAPK1, MAPK3, MAPK4, MAPK6, MAPK7, MAPK12, MAPK15), C-Jun N-terminal (MAPK8, MAPK9, MAPK10), P38 mitogenom-aktivirani protein (MAPK11, MAPK13, MAPK14)
MAP3K (EC 2.7.11.25)
MAP kinaza kinaza kinaze (MAP3K1, MAP3K2, MAP3K3, MAP3K4, MAP3K5, MAP3K6, MAP3K7, MAP3K8) RAFs (ARAF, BRAF, KSR1, KSR2), MLK (MAP3K12, MAP3K13, MAP3K9, MAP3K10, MAP3K11, MAP3K7, ZAK), CDC7, MAP3K14
Tau-proteinska kinaza (EC 2.7.11.26)
TPK1, TTK, GSK-3
acetil-CoA karboksilazna kinaza] (EC 2.7.11.27)
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Tropomiozinska kinaza (EC 2.7.11.28)
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Receptor lipoproteina-niske-gustine kinaza (EC 2.7.11.29)
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Receptor protein serin/treonin kinaza (EC 2.7.11.30)
Koštani morfogenetski proteinski receptori (BMPR1, BMPR1A, BMPR1B, BMPR2), ACVR1, ACVR1B, ACVR1C, ACVR2A, ACVR2B, ACVRL1, Anti-Mulerianski hormonski receptor
(3) Kinaze dualne-specifičnosti (EC 2.7.12)
MAP2K
MAP2K1, MAP2K2, MAP2K3, MAP2K4, MAP2K5, MAP2K6, MAP2K7
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
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Teme
Tipovi
  • 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
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