Lipid-fosfatna fosfataza
(Preusmjereno sa stranice Lipid-fosfat fosfataza)
| Lipid-fosfatna fosfataza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.1.3.76 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Lipid-fosfatna fosfataza (EC 3.1.3.76, hidroksi masno kiselinska fosfataza, dihidroksi masno kiselinska fosfataza, hidroksi lipidna fosfataza, sEH, hidrolaza rastvornog epoksida) je enzim sa sistematskim imenom (9S,10S)-10-hidroksi-9-(fosfonooksi)oktadekanoat fosfohidrolaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (9S,10S)-10-hidroksi-9-(fosfonooksi)oktadekanoat + H2O (9S,10S)-9,10-dihidroksioktadekanoat + fosfat
Za rad ovog enzim je neophodan Mg2+.
Reference[uredi | uredi kod]
- ↑ Newman, J.W., Morisseau, C., Harris, T.R. and Hammock, B.D. (2003). „The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity”. Proc. Natl. Acad. Sci. USA 100: 1558-1563. PMID 12574510.
- ↑ Cronin, A., Mowbray, S., Dürk, H., Homburg, S., Fleming, I., Fisslthaler, B., Oesch, F. and Arand, M. (2003). „The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase”. Proc. Natl. Acad. Sci. USA 100: 1552-1557. PMID 12574508.
- ↑ Morisseau, C. and Hammock, B.D. (2005). „Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles”. Annu. Rev. Pharmacol. Toxicol. 45: 311-333. PMID 15822179.
- ↑ Tran, K.L., Aronov, P.A., Tanaka, H., Newman, J.W., Hammock, B.D. and Morisseau, C. (2005). „Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase”. Biochemistry 44: 12179-12187. PMID 16142916.
- ↑ Newman, J.W., Morisseau, C. and Hammock, B.D. (2005). „Epoxide hydrolases: their roles and interactions with lipid metabolism”. Prog. Lipid Res. 44: 1-51. PMID 15748653.
- ↑ Srivastava, P.K., Sharma, V.K., Kalonia, D.S. and Grant, D.F. (2004). „Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure”. Arch. Biochem. Biophys. 427: 164-169. PMID 15196990.
- ↑ Gomez, G.A., Morisseau, C., Hammock, B.D. and Christianson, D.W. (2004). „Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis”. Biochemistry 43: 4716-4723. PMID 15096040.
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.