KEGG   ENZYME: 1.14.13.25
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
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
ec00680  Methane metabolism
ec01100  Metabolic pathways
ec01120  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)
METU: GNH96_11955 GNH96_11965 GNH96_11975 GNH96_11980
MMT: Metme_1649 Metme_1650 Metme_1652 Metme_1654
METL: U737_00780 U737_00790 U737_00800 U737_00805
MBUR: EQU24_05885 EQU24_05890 EQU24_05900 EQU24_05910
MMAI: sS8_0764 sS8_0767 sS8_0769 sS8_0770
MMOB: F6R98_10890 F6R98_10900 F6R98_10910 F6R98_10915
MISZ: MishRS11D_39880(ascD) MishRS11D_39900 MishRS11D_39920 MishRS11D_39930
MSL: Msil_1262 Msil_1263 Msil_1265 Msil_1267
MTUN: MTUNDRAET4_1698(mmoC) MTUNDRAET4_1700(mmoZ) MTUNDRAET4_1702(mmoY) MTUNDRAET4_1703(mmoX)
 » show all
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 165:395-402 (1977)
DOI:10.1042/bj1650395
Reference
2  [PMID:6870854]
  Authors
Hyman MR, Wood PM.
  Title
Methane oxidation by Nitrosomonas europaea.
  Journal
Biochem J 212:31-7 (1983)
DOI:10.1042/bj2120031
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 96:205-12 (1979)
DOI:10.1111/j.1432-1033.1979.tb13030.x
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 161:333-44 (1977)
DOI:10.1042/bj1610333
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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