Leukotrien-A4 hidrolaza
(Preusmjereno sa stranice LTA4 hydrolase)
Leukotrien-A4 hidrolaza (EC 3.3.2.6, LTA4 hidrolaza, LTA4H, leukotrienska A4 hidrolaza) je enzim sa sistematskim imenom (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoksiikosa-7,9,11,14-tetraenoatna hidrolaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Leukotrien-A4 hidrolaza | |||||||||
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| Identifikatori | |||||||||
| EC broj | 3.3.2.6 | ||||||||
| CAS broj | 90119-07-6 | ||||||||
| 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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- leukotrien A4 + H2O leukotrien B4
Ova bifunkcionalna cinkova metaloproteaza deluje kao epoksidna hidrolaza i aminopeptidaza.
Reference uredi
- ↑ Evans, J.F., Dupuis, P. and Ford-Hutchinson, A.W. (1985). „Purification and characterisation of leukotriene A4 hydrolase from rat neutrophils”. Biochim. Biophys. Acta 840: 43-50. PMID 3995081.
- ↑ Minami, M., Ohno, S., Kawasaki, H., Rådmark, O., Samuelsson, B., Jörnvall, H., Shimizu, T., Seyama, Y. and Suzuki, K. (1987). „Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase - complete primary structure of an enzyme involved in eicosanoid synthesis”. J. Biol. Chem. 262: 13873-13876. PMID 3654641.
- ↑ Haeggström, J., Meijer, J. and Rådmark, O. (1986). „Leukotriene A4. Enzymatic conversion into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver cytosolic epoxide hydrolase”. J. Biol. Chem. 261: 6332-6337. PMID 3009453.
- ↑ 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.
- ↑ Fretland, A.J. and Omiecinski, C.J. (2000). „Epoxide hydrolases: biochemistry and molecular biology”. Chem. Biol. Interact. 129: 41-59. PMID 11154734.
- ↑ Orning, L., Gierse, J.K. and Fitzpatrick, F.A. (1994). „The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity”. J. Biol. Chem. 269: 11269-11267. PMID 8157657.
- ↑ Ohishi, N., Izumi, T., Minami, M., Kitamura, S., Seyama, Y., Ohkawa, S., Terao, S., Yotsumoto, H., Takaku, F. and Shimizu, T. (1987). „Leukotriene A4 hydrolase in the human lung. Inactivation of the enzyme with leukotriene A4 isomers”. J. Biol. Chem. 262: 10200-10205. PMID 3038871.
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.