EC number:1.14.18.3

Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.18.3
Description:Methane monooxygenase (particulate).
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

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.18.3
BRENDA Enzyme Link: BRENDA 1.14.18.3
KEGG Enzyme Link: KEGG1.14.18.3
BioCyc Enzyme Link: BioCyc 1.14.18.3
ExPASy Enzyme Link: ExPASy1.14.18.3
EC2PDB Enzyme Link: EC2PDB 1.14.18.3
ExplorEnz Enzyme Link: ExplorEnz 1.14.18.3
PRIAM enzyme-specific profiles Link: PRIAM 1.14.18.3
IntEnz Enzyme Link: IntEnz 1.14.18.3
MEDLINE Enzyme Link: MEDLINE 1.14.18.3

EC number:1.14.18.3

MSA:

1.14.18.3;
Phylogenetic Tree:

1.14.18.3;
Uniprot:
M-CSA:
RHEA:30355 a quinol + methane + O2 = a quinone + H2O + methanol
RULE(radius=1) [CH4;+0:1].[O;H0;+0:2]=[O;H0;+0:3].[OH;+0:4]-[c;H0;+0:5]1:[cH;+0:6]:[cH;+0:7]:[c;H0;+0:8](-[OH;+0:9]):[cH;+0:10]:[cH;+0:11]:1>>[CH3;+0:1]-[OH;+0:2].[O;H0;+0:4]=[C;H0;+0:5]1-[CH;+0:6]=[CH;+0:7]-[C;H0;+0:8](=[O;H0;+0:9])-[CH;+0:10]=[CH;+0:11]-1.[OH2;+0:3]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors.Shiemke AK, Cook SA, Miley T, Singleton P1995 Aug 207646068
Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath).Kitmitto A, Myronova N, Basu P, Dalton H2005 Aug 2316101279