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
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)
MMT: Metme_1649 Metme_1650 Metme_1652 Metme_1654
MSL: Msil_1262 Msil_1263 Msil_1265 Msil_1267
MBRY: B1812_14115 B1812_14125 B1812_14135 B1812_14140
MMI: MMAR_0130 MMAR_0131
MCB: Mycch_5395 Mycch_5875 Mycch_5897 Mycch_5898 Mycch_5900 Mycch_5901
MRH: MycrhN_3049 MycrhN_3050 MycrhN_3053 MycrhN_3054
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 165:395-402 (1977)
Reference
2  [PMID:6870854]
  Authors
Hyman MR, Wood PM.
  Title
Methane oxidation by Nitrosomonas europaea.
  Journal
Biochem J 212:31-7 (1983)
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)
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

DBGET integrated database retrieval system