KEGG   ENZYME: 1.14.13.25Help
Entry
EC 1.14.13.25               Enzyme                                 

Name methane monooxygenase;
methane hydroxylase
Class Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
With NADH or NADPH as one donor, and incorporation of one atom of
oxygen into the other donor
BRITE hierarchy
Sysname methane,NAD(P)H:oxygen oxidoreductase (hydroxylating)
Reaction(IUBMB) methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O [RN:R01142
R01143]
Reaction(KEGG) R01142 R01143;
(other) R02823
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Substrate methane [CPD:C01438];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product methanol [CPD:C00132];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Cofactor Iron [CPD:C00023]
Comment Broad specificity; many alkanes can be hydroxylated, and alkenes are
converted into the corresponding epoxides; CO is oxidized to CO2,
ammonia is oxidized to hydroxylamine, and some aromatic compounds
and cyclic alkanes can also be hydroxylated, but more slowly.
Pathway PATH: ec00680  Methane metabolism
PATH: ec01100  Metabolic pathways
Orthology KO: K08684  methane monooxygenase
Genes PYO: PY07725 PY07726
MCA: MCA0295(pmoC3) MCA1194(mmoX) MCA1195(mmoY) MCA1196(mmoB)
     MCA1198(mmoZ) MCA1199(mmoD) MCA1200(mmoC) MCA1796(pmoB)
     MCA1797(pmoA) MCA1798(pmoC1) MCA2853(pmoB2) MCA2854(pmoA2)
REU: Reut_B5683
RME: Rmet_1328
BVI: Bcep1808_7596
BUR: Bcep18194_B1122 Bcep18194_B2968
AJS: Ajs_0209
VEI: Veis_2793 Veis_4409 Veis_4411
MPT: Mpe_A0950(prmA)
AZO: azo1219 azo1221
BRA: BRADO4348 BRADO4350
BBT: BBta_3630 BBta_3632
RSH: Rsph17029_1508
ACR: Acry_1381
MSM: MSMEG_1971 MSMEG_1972
RHA: RHA1_ro00441
NCA: Noca_4807 Noca_4809
FRA: Francci3_2520
Taxonomy
Structures PDB: 1FYZ  1FZ0  1FZ1  1FZ2  1FZ3  1FZ4  1FZ5  1FZ6  1FZ7  1FZ8  
     1FZ9  1FZH  1FZI  1JQ4  1MHY  1MHZ  1MMO  1MTY  1TVC  1XMF  
     1XMG  1XMH  1XU3  1XU5  1XVB  1XVC  1XVD  1XVE  1XVF  1XVG  
Reference
  Authors
  Title


  Journal
  Organism
1  [PMID:411486]
Colby J, Stirling DI, Dalton H.
The soluble methane mono-oxygenase of Methylococcus capsulatus
(Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and
alicyclic, aromatic and heterocyclic compounds.
Biochem. J. 165 (1977) 395-402.
Methylococcus capsulatus [GN:mca]
Reference
  Authors
  Title
  Journal
  Organism
2  [PMID:6870854]
Hyman MR, Wood PM.
Methane oxidation by Nitrosomonas europaea.
Biochem. J. 212 (1983) 31-7.
Nitrosomonas europeae [GN:neu]
Reference
  Authors
  Title


  Journal
  Organism
3  [PMID:572296]
Stirling DI, Dalton H.
Properties of the methane mono-oxygenase from extracts of
Methylosinus trichosporium OB3b and evidence for its similarity to
the enzyme from Methylococcus capsulatus (Bath).
Eur. J. Biochem. 96 (1979) 205-12.
Methylococcus capsulatus [GN:mca], Methylosinus trichosporium
Reference
  Authors
  Title

  Journal
  Organism
4  [PMID:15544]
Tonge GM, Harrison DE, Higgins IJ.
Purification and properties of the methane mono-oxygenase enzyme
system from Methylosinus trichosporium OB3b.
Biochem. J. 161 (1977) 333-44.
Methylosinus trichosporium
Other DBs ExplorEnz - The Enzyme Database: 1.14.13.25
IUBMB Enzyme Nomenclature: 1.14.13.25
ExPASy - ENZYME nomenclature database: 1.14.13.25
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.25
BRENDA, the Enzyme Database: 1.14.13.25
CAS: 51961-97-8

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