(S)-2-hidroksipropilfosfonska kiselina epoksidaza
(Preusmjereno sa stranice HppE)
(S)-2-hidroksipropilfosfonska kiselina epoksidaza (EC 1.14.19.7, HPP epoksidaza, HppE, 2-hidroksipropilfosfonic kiselina epoksidaza, Fom4, (S)-2-hidroksipropilfosfonat epoksidaza) je enzim sa sistematskim imenom (S)-2-hidroksipropilfosfonat,NADH:kiseonik epoksidaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| (S)-2-hidroksipropilfosfonska kiselina epoksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.19.7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- (S)-2-hidroksipropilfosfonat + NADH + H+ + O2 (1R,2S)-epoksipropilfosfonat + NAD+ + 2H2O
Ovaj enzim sadrži u svakom monomeru jedan center gvožđa koje nije vezano za hem.
Reference
uredi- ↑ Munos, J.W., Moon, S.J., Mansoorabadi, S.O., Chang, W., Hong, L., Yan, F., Liu, A. and Liu, H.W. (2008). „Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae”. Biochemistry 47: 8726-8735. PMID 18656958.
- ↑ Yan, F., Moon, S.J., Liu, P., Zhao, Z., Lipscomb, J.D., Liu, A. and Liu, H.W. (2007). „Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analogues”. Biochemistry 46: 12628-12638. PMID 17927218.
- ↑ Hidaka, T., Goda, M., Kuzuyama, T., Takei, N., Hidaka, M. and Seto, H. (1995). „Cloning and nucleotide sequence of fosfomycin biosynthetic genes of Streptomyces wedmorensis”. Mol. Gen. Genet. 249: 274-280. PMID 7500951.
- ↑ Liu, P., Mehn, M.P., Yan, F., Zhao, Z., Que, L., Jr. and Liu, H.W. (2004). „Oxygenase activity in the self-hydroxylation of (S)-2-hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis”. J. Am. Chem. Soc. 126: 10306-10312. PMID 15315444.
- ↑ Higgins, L.J., Yan, F., Liu, P., Liu, H.W. and Drennan, C.L. (2005). „Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme”. Nature 437: 838-844. PMID 16015285.
- ↑ Cameron, S., McLuskey, K., Chamberlayne, R., Hallyburton, I. and Hunter, W.N. (2005). „Initiating a crystallographic analysis of recombinant (S)-2-hydroxypropylphosphonic acid epoxidase from Streptomyces wedmorensis”. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61: 534-536. PMID 16511089.
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.