| Entry |
|
| 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
 |
| 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
 |
| 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
 |
| 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 |