EC number:1.2.5.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.2 Acting on the aldehyde or oxo group of donors |
| 1.2.5 With a quinone or similar compound as acceptor |
| ID: | 1.2.5.3 |
|---|---|
| Description: | Aerobic carbon monoxide dehydrogenase. |
| Alternative Name: |
Molybdoenzyme carbon monoxide dehydrogenase. |
| Cath: | 1.10.1060.10; 1.10.150.120; 1.20.1270.30; 3.30.365.10; 3.30.390.50; 3.30.43.10; 3.30.465.10; 3.90.1170.50; 3.40.50.20; 3.40.50.2030; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.2.5.3 |
| BRENDA Enzyme Link: | BRENDA 1.2.5.3 |
| KEGG Enzyme Link: | KEGG1.2.5.3 |
| BioCyc Enzyme Link: | BioCyc 1.2.5.3 |
| ExPASy Enzyme Link: | ExPASy1.2.5.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.2.5.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.2.5.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.2.5.3 |
| IntEnz Enzyme Link: | IntEnz 1.2.5.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.2.5.3 |
| RHEA:48880 | a quinone + CO + H2O = a quinol + CO2 |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[C;H0;+0:7](-[*:8])=[C;H0;+0:9](-[*:10])-[C;H0;+0:11]-1=[O;H0;+0:12].[C-;H0:13]#[O+;H0:14].[OH2;+0:15]>>[*:1]-[c;H0;+0:2]1:[c;H0;+0:11](-[OH;+0:12]):[c;H0;+0:9](-[*:10]):[c;H0;+0:7](-[*:8]):[c;H0;+0:5](-[OH;+0:6]):[c;H0;+0:3]:1-[*:4].[O;H0;+0:14]=[C;H0;+0:13]=[O;H0;+0:15] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Insights into the posttranslational assembly of the Mo-, S- and Cu-containing cluster in the active site of CO dehydrogenase of Oligotropha carboxidovorans. | Pelzmann AM, Mickoleit F, Meyer O | 2014 Dec | 25377894 |
| The aerobic CO dehydrogenase from Oligotropha carboxidovorans. | Hille R, Dingwall S, Wilcoxen J | 2015 Mar | 25156151 |
| Reaction of the molybdenum- and copper-containing carbon monoxide dehydrogenase from Oligotropha carboxydovorans with quinones. | Wilcoxen J, Zhang B, Hille R | 2011 Mar 22 | 21275368 |
| Structural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans. | Resch M, Dobbek H, Meyer O | 2005 Aug | 16091936 |
| A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy. | Gnida M, Ferner R, Gremer L, Meyer O, Meyer-Klaucke W | 2003 Jan 14 | 12515558 |
| Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution. | Dobbek H, Gremer L, Kiefersauer R, Huber R, Meyer O | 2002 Dec 10 | 12475995 |
| Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli. | Gremer L, Kellner S, Dobbek H, Huber R, Meyer O | 2000 Jan 21 | 10636886 |