KEGG   ENZYME: 1.14.99.39Help
Entry
EC 1.14.99.39               Enzyme                                 

Name
ammonia monooxygenase;
AMO
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
BRITE hierarchy
Sysname
ammonia,donor:oxygen oxidoreductase (hydroxylamine-producing)
Reaction(IUBMB)
NH3 + a reduced acceptor + O2 = NH2OH + an acceptor + H2O [RN:R09519]
Reaction(KEGG)
R09519 > R00148;
(other) R09156
Show
Substrate
NH3 [CPD:C00014];
reduced acceptor [CPD:C00030];
O2 [CPD:C00007]
Product
NH2OH [CPD:C00192];
acceptor [CPD:C00028];
H2O [CPD:C00001]
Comment
The enzyme catalyses the first reaction in the pathway of ammonia oxidation to nitrite. It contains copper [1], iron [5] and possibly zinc [9]. The enzyme requires two electrons, which are derived indirectly from the quinone pool via a membrane-bound donor.
History
EC 1.14.99.39 created 2010
Pathway
ec00910  Nitrogen metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K10944  methane/ammonia monooxygenase subunit A
Genes
MCA: MCA1797(pmoA) MCA2854(pmoA2)
MMT: Metme_0304
MDN: JT25_004545 JT25_012445
MDH: AYM39_18580 AYM39_19770
MKO: MKLM6_3758 MKLM6_3997
MAH: MEALZ_0515(pmoA)
MPSY: CEK71_17435
NOC: Noc_2502
NHL: Nhal_0676
NWA: Nwat_0632
NTT: TAO_1521(amoA)
NEU: NE0944(amoA1) NE2063(amoA2)
MSC: BN69_0203(pmoA2) BN69_2827(pmoA) BN69_3534(pmoA)
MIN: Minf_1507(pmoA) Minf_1510(pmoA) Minf_1590(pmoA)
NIO: NITINOP_1853(amoA)
MOX: DAMO_2450(pmoA)
NMR: Nmar_1500
NID: NPIRD3C_2147(amoA)
NIN: NADRNF5_0394(amoA)
NCT: NMSP_0259
NGA: Ngar_c25350(amoA)
NVN: NVIE_027270(amoA)
NEV: NTE_00961
NCV: NCAV_0492(amoA)
NBV: T478_0302
NDV: NDEV_1777(amoA)
 » show all
Taxonomy
Reference
1  [PMID:8458839]
  Authors
Ensign SA, Hyman MR, Arp DJ
  Title
In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper.
  Journal
J Bacteriol 175:1971-80 (1993)
DOI:10.1128/JB.175.7.1971-1980.1993
Reference
2  [PMID:8085841]
  Authors
Hyman MR, Page CL, Arp DJ
  Title
Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea.
  Journal
Appl Environ Microbiol 60:3033-5 (1994)
Reference
3  [PMID:7980540]
  Authors
Bergmann DJ, Hooper AB
  Title
Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monoxygenase of Nitrosomonas europaea.
  Journal
Biochem Biophys Res Commun 204:759-62 (1994)
DOI:10.1006/bbrc.1994.2524
  Sequence
Reference
4  [PMID:7590173]
  Authors
Holmes AJ, Costello A, Lidstrom ME, Murrell JC
  Title
Evidence that particulate methane monooxygenase and ammonia monooxygenase may be  evolutionarily related.
  Journal
FEMS Microbiol Lett 132:203-8 (1995)
DOI:10.1111/j.1574-6968.1995.tb07834.x
Reference
5  [PMID:8941709]
  Authors
Zahn JA, Arciero DM, Hooper AB, DiSpirito AA
  Title
Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea.
  Journal
FEBS Lett 397:35-8 (1996)
DOI:10.1016/S0014-5793(96)01116-7
Reference
6  [PMID:8654570]
  Authors
Moir JW, Crossman LC, Spiro S, Richardson DJ
  Title
The purification of ammonia monooxygenase from Paracoccus denitrificans.
  Journal
FEBS Lett 387:71-4 (1996)
DOI:10.1016/0014-5793(96)00463-2
Reference
7  [PMID:11004450]
  Authors
Whittaker M, Bergmann D, Arciero D, Hooper AB.
  Title
Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea.
  Journal
Biochim Biophys Acta 1459:346-55 (2000)
DOI:10.1016/S0005-2728(00)00171-7
Reference
8  [PMID:12209257]
  Authors
Arp DJ, Sayavedra-Soto LA, Hommes NG.
  Title
Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea.
  Journal
Arch Microbiol 178:250-5 (2002)
DOI:10.1007/s00203-002-0452-0
Reference
9  [PMID:19453274]
  Authors
Gilch S, Meyer O, Schmidt I
  Title
A soluble form of ammonia monooxygenase in Nitrosomonas europaea.
  Journal
Biol Chem 390:863-73 (2009)
DOI:10.1515/BC.2009.085
Other DBs
ExplorEnz - The Enzyme Database: 1.14.99.39
IUBMB Enzyme Nomenclature: 1.14.99.39
ExPASy - ENZYME nomenclature database: 1.14.99.39
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.99.39
BRENDA, the Enzyme Database: 1.14.99.39

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