Amonijak monooksigenaza
Amonijak monooksigenaza (EC 1.14.99.39, AMO) je enzim.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Amonijak monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.99.39 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- amonijak + AH2 + O2 NH2OH + A + H2O
Ovaj enzim sadrži bakar i gvožđe nevezano za hem. Donor je vezan za membranu.
Reference uredi
- ↑ Hyman, M.R., Page, C.L. and Arp, D.J. (1994). „Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea”. Appl. Environ. Microbiol. 60: 3033-3035. PMID 8085841.
- ↑ Bergmann, D.J. and Hooper, A.B. (1994). „Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monoxygenase of Nitrosomonas europaea”. Biochem. Biophys. Res. Commun. 204: 759-762. PMID 7980540.
- ↑ Holmes, A.J., Costello, A., Lidstrom, M.E. and Murrell, J.C. (1995). „Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related”. FEMS Microbiol. Lett. 132: 203-208. PMID 7590173.
- ↑ Zahn, J.A., Arciero, D.M., Hooper, A.B. and DiSpirito, A.A. (1996). „Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea”. FEBS Lett. 397: 35-38. PMID 8941709.
- ↑ Moir, J.W., Crossman, L.C., Spiro, S. and Richardson, D.J. (1996). „The purification of ammonia monooxygenase from Paracoccus denitrificans”. FEBS Lett. 387: 71-74. PMID 8654570.
- ↑ Whittaker, M., Bergmann, D., Arciero, D. and Hooper, A.B. (2000). „Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea”. Biochim. Biophys. Acta 1459: 346-355. PMID 11004450.
- ↑ Arp, D.J., Sayavedra-Soto, L.A. and Hommes, N.G. (2002). „Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea”. Arch. Microbiol. 178: 250-255. PMID 12209257.
- ↑ Gilch, S., Meyer, O. and Schmidt, I. (2009). „A soluble form of ammonia monooxygenase in Nitrosomonas europaea”. Biol. Chem. 390: 863-873. PMID 19453274.
- ↑ Rasche, M.E., Hicks, R.E., Hyman, M.R. and Arp, D.J. (1990). „Oxidation of monohalogenated ethanes and n-chlorinated alkanes by whole cells of Nitrosomonas europaea”. J. Bacteriol. 172: 5368-5373. PMID 2394686.
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.