Ammonia monooxygenase
| Ammonia monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.99.39 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Ammonia monooxygenase (EC 1.14.99.39, AMO) is an enzyme,[1][2][3][4][5][6][7][8][9] which catalyses the following chemical reaction
ammonia + AH2 + O2⇌displaystyle rightleftharpoonsNH2OH + A + H2O
Ammonia monooxygenase contains copper and possibly nonheme iron.
References
^ Hyman MR, Page CL, Arp DJ (August 1994). "Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea". Applied and Environmental Microbiology. 60 (8): 3033–5. PMC 201762. PMID 8085841..mw-parser-output cite.citationfont-style:inherit.mw-parser-output .citation qquotes:"""""""'""'".mw-parser-output .citation .cs1-lock-free abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-subscription abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registrationcolor:#555.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration spanborder-bottom:1px dotted;cursor:help.mw-parser-output .cs1-ws-icon abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center.mw-parser-output code.cs1-codecolor:inherit;background:inherit;border:inherit;padding:inherit.mw-parser-output .cs1-hidden-errordisplay:none;font-size:100%.mw-parser-output .cs1-visible-errorfont-size:100%.mw-parser-output .cs1-maintdisplay:none;color:#33aa33;margin-left:0.3em.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-formatfont-size:95%.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-leftpadding-left:0.2em.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-rightpadding-right:0.2em
^ Bergmann DJ, Hooper AB (October 1994). "Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monoxygenase of Nitrosomonas europaea". Biochemical and Biophysical Research Communications. 204 (2): 759–62. doi:10.1006/bbrc.1994.2524. PMID 7980540.
^ Holmes AJ, Costello A, Lidstrom ME, Murrell JC (October 1995). "Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related". FEMS Microbiology Letters. 132 (3): 203–8. doi:10.1111/j.1574-6968.1995.tb07834.x. PMID 7590173.
^ Zahn JA, Arciero DM, Hooper AB, DiSpirito AA (November 1996). "Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea". FEBS Letters. 397 (1): 35–8. doi:10.1016/s0014-5793(96)01116-7. PMID 8941709.
^ Moir JW, Crossman LC, Spiro S, Richardson DJ (May 1996). "The purification of ammonia monooxygenase from Paracoccus denitrificans". FEBS Letters. 387 (1): 71–4. doi:10.1016/0014-5793(96)00463-2. PMID 8654570.
^ Whittaker M, Bergmann D, Arciero D, Hooper AB (August 2000). "Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea". Biochimica et Biophysica Acta. 1459 (2–3): 346–55. doi:10.1016/s0005-2728(00)00171-7. PMID 11004450.
^ Arp DJ, Sayavedra-Soto LA, Hommes NG (October 2002). "Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea". Archives of Microbiology. 178 (4): 250–5. doi:10.1007/s00203-002-0452-0. PMID 12209257.
^ Gilch S, Meyer O, Schmidt I (September 2009). "A soluble form of ammonia monooxygenase in Nitrosomonas europaea". Biological Chemistry. 390 (9): 863–73. doi:10.1515/BC.2009.085. PMID 19453274.
^ Rasche ME, Hicks RE, Hyman MR, Arp DJ (September 1990). "Oxidation of monohalogenated ethanes and n-chlorinated alkanes by whole cells of Nitrosomonas europaea". Journal of Bacteriology. 172 (9): 5368–73. PMC 213201. PMID 2394686.
External links
Ammonia+monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
