EC number:1.14.13.25

Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.13.25
Description:Methane monooxygenase (soluble).
Alternative Name: Methane hydroxylase.
Cath: 1.10.287.710; 1.10.620.20; 1.20.1050.50; 1.20.1280.10; 1.20.1280.30; 1.20.1450.10; 3.40.50.80; 2.40.30.10; 2.60.120.570; 2.60.40.1580;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.13.25
BRENDA Enzyme Link: BRENDA 1.14.13.25
KEGG Enzyme Link: KEGG1.14.13.25
BioCyc Enzyme Link: BioCyc 1.14.13.25
ExPASy Enzyme Link: ExPASy1.14.13.25
EC2PDB Enzyme Link: EC2PDB 1.14.13.25
ExplorEnz Enzyme Link: ExplorEnz 1.14.13.25
PRIAM enzyme-specific profiles Link: PRIAM 1.14.13.25
IntEnz Enzyme Link: IntEnz 1.14.13.25
MEDLINE Enzyme Link: MEDLINE 1.14.13.25

EC number:1.14.13.25

MSA:

1.14.13.25;
Phylogenetic Tree:

1.14.13.25;
Uniprot:
M-CSA:
RHEA:13641 H(+) + methane + NADPH + O2 = H2O + methanol + NADP(+)
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[CH4;+0:9].[H+;H0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[CH3;+0:9]-[OH;+0:12].[OH2;+0:11]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Methane oxidation by Nitrosomonas europaea.Hyman MR, Wood PM1983 Apr 156870854
Properties of the methane mono-oxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath).Stirling DI, Dalton H1979 May 2572296
The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds.Colby J, Stirling DI, Dalton H1977 Aug 1411486
Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b.Tonge GM, Harrison DE, Higgins IJ1977 Feb 115544
Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site.Whittington DA, Lippard SJ2001 Feb 711456616
RHEA:13637 H(+) + methane + NADH + O2 = H2O + methanol + NAD(+)
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[CH4;+0:9].[H+;H0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[CH3;+0:9]-[OH;+0:12].[OH2;+0:11]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Methane oxidation by Nitrosomonas europaea.Hyman MR, Wood PM1983 Apr 156870854
Properties of the methane mono-oxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath).Stirling DI, Dalton H1979 May 2572296
The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds.Colby J, Stirling DI, Dalton H1977 Aug 1411486
Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b.Tonge GM, Harrison DE, Higgins IJ1977 Feb 115544
Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site.Whittington DA, Lippard SJ2001 Feb 711456616