Lizofosfolipaza
(Preusmjereno sa stranice EC 3.1.1.5)
Lizofosfolipaza | |||||||||
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Identifikatori | |||||||||
EC broj | 3.1.1.5 | ||||||||
CAS broj | 9001-85-8 | ||||||||
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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Lizofosfolipaza (EC 3.1.1.5, lecitinaza B, lizolecitinaza, fosfolipaza B, lizofosfatidaza, lecitolipaza, fosfatidaza B, lizofosfatidilholinska hidrolaza, lizofosfolipaza A1, lizofofolipaza L2, lizofosfolipaza transacilaza, neuropatična ciljna esteraza, NTE, NTE-LysoPLA, NTE-lizofosfolipaza) je enzim sa sistematskim imenom 2-lisofosfatidilholin acilhidrolaza.[1][2][3][4][5][6][7][8][9][10][11] Ovaj enzim katalizuje sledeću hemijsku reakciju
- 2-lizofosfatidilholin + H2O glicerofosfoholin + karboksilat
Reference[uredi | uredi kod]
- ↑ Abe, M., Ohno, K. and Sato, R. (1974). „Possible identity of lysolecithin acyl-hydrolase with lysolecithin-lysolecithin acyl-transferase in rat-lung soluble fraction”. Biochim. Biophys. Acta 369: 361-370.
- ↑ Contardi, A. and Ercoli, A. (1933). „The enzymic cleavage of lecithin and lysolecithin”. Biochem. Z. 261: 275-302.
- ↑ Dawson, R.M.C. (1958). „Studies on the hydrolysis of lecithin by Penicillium notatum phospholipase B preparation”. Biochem. J. 70: 559-570. PMID 13607409.
- ↑ Fairbairn, D. (1948). „The preparation and properties of a lysophospholipase from Penicillium notatum”. J. Biol. Chem. 173: 705-714.
- ↑ Shapiro, B. (1953). „Purification and properties of a lysolecithinase from pancreas”. Biochem. J. 53: 663-666. PMID 13032127.
- ↑ van den Bosch, H., Aarsman, A.J., De Jong, J.G.N. and van Deenen, L.L.M. (1973). „Studies on lysophospholipases. I. Purification and some properties of a lysophospholipase from beef pancreas”. Biochim. Biophys. Acta 296: 94-104. PMID 4693514.
- ↑ van den Bosch, H., Vianen, G.M. and van Heusden, G.P.H. (1981). „Lysophospholipase-transacylase from rat lung”. Methods Enzymol. 71: 513-521. PMID 7278668.
- ↑ van Tienhoven, M., Atkins, J., Li, Y. and Glynn, P. (2002). „Human neuropathy target esterase catalyzes hydrolysis of membrane lipids”. J. Biol. Chem. 277: 20942-20948. PMID 11927584.
- ↑ Quistad, G.B., Barlow, C., Winrow, C.J., Sparks, S.E. and Casida, J.E. (2003). „Evidence that mouse brain neuropathy target esterase is a lysophospholipase”. Proc. Natl. Acad. Sci. USA 100: 7983-7987. PMID 12805562.
- ↑ Lush, M.J., Li, Y., Read, D.J., Willis, A.C. and Glynn, P. (1998). „Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man”. Biochem. J. 332: 1-4. PMID 9576844.
- ↑ Winrow, C.J., Hemming, M.L., Allen, D.M., Quistad, G.B., Casida, J.E. and Barlow, C. (2003). „Loss of neuropathy target esterase in mice links organophosphate exposure to hyperactivity”. Nat. Genet. 33: 477-485. PMID 12640454.
Literatura[uredi | uredi kod]
- 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.