Lizofosfolipaza
(Preusmjereno sa stranice EC 3.1.1.5)
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
| Lizofosfolipaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
- 2-lizofosfatidilholin + H2O glicerofosfoholin + karboksilat
Reference uredi
- ↑ 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
- 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.