KEGG   ENZYME: 1.14.13.25Help
Entry
EC 1.14.13.25               Enzyme                                 

Name
methane monooxygenase (soluble);
methane hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
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)
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]
Comment
The enzyme is soluble, in contrast to the particulate enzyme, EC 1.14.18.3. 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.
History
EC 1.14.13.25 created 1984, modified 2011
Pathway
Methane metabolism
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K16157  
methane monooxygenase component A alpha chain
K16158  
methane monooxygenase component A beta chain
K16159  
methane monooxygenase component A gamma chain
K16161  
methane monooxygenase component C
Genes
MCA: 
MCA1194(mmoX) MCA1195(mmoY) MCA1198(mmoZ) MCA1200(mmoC)
MMT: 
MSL: 
MMI: 
MRH: 
MCB: 
NCA: 
Taxonomy
Reference
1  [PMID:411486]
  Authors
Colby J, Stirling DI, Dalton H.
  Title
The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds.
  Journal
Biochem. J. 165 (1977) 395-402.
Reference
2  [PMID:6870854]
  Authors
Hyman MR, Wood PM.
  Title
Methane oxidation by Nitrosomonas europaea.
  Journal
Biochem. J. 212 (1983) 31-7.
Reference
3  [PMID:572296]
  Authors
Stirling DI, Dalton H.
  Title
Properties of the methane mono-oxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath).
  Journal
Eur. J. Biochem. 96 (1979) 205-12.
Reference
4  [PMID:15544]
  Authors
Tonge GM, Harrison DE, Higgins IJ.
  Title
Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b.
  Journal
Biochem. J. 161 (1977) 333-44.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
51961-97-8

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