EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.5.3 | CO + a quinone + H2O | - |
- |
CO2 + a quinol | - |
? | |
1.2.5.3 | CO + a quinone + H2O | Afipia carboxidovorans ATCC 49405 | - |
CO2 + a quinol | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.5.3 | Afipia carboxidovorans ATCC 49405 | P19919 AND P19920 AND P19921 | genes coxL, coxM, and coxS; genes coxS, coxM, and coxL | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.5.3 | CO + 1,2-naphthoquinone-4-sulfonic acid + H2O | - |
- |
CO2 + 1,2-naphthoquinol-4-sulfonic acid | - |
? | |
1.2.5.3 | CO + 1,2-naphthoquinone-4-sulfonic acid + H2O | - |
Afipia carboxidovorans ATCC 49405 | CO2 + 1,2-naphthoquinol-4-sulfonic acid | - |
? | |
1.2.5.3 | CO + 1,4-naphthoquinone + H2O | - |
- |
CO2 + 1,4-naphthoquinol | - |
? | |
1.2.5.3 | CO + 1,4-naphthoquinone + H2O | - |
Afipia carboxidovorans ATCC 49405 | CO2 + 1,4-naphthoquinol | - |
? | |
1.2.5.3 | CO + a quinone + H2O | - |
- |
CO2 + a quinol | - |
? | |
1.2.5.3 | CO + a quinone + H2O | - |
Afipia carboxidovorans ATCC 49405 | CO2 + a quinol | - |
? | |
1.2.5.3 | CO + benzoquinone + H2O | - |
- |
CO2 + benzoquinol | - |
? | |
1.2.5.3 | CO + benzoquinone + H2O | - |
Afipia carboxidovorans ATCC 49405 | CO2 + benzoquinol | - |
? | |
1.2.5.3 | CO + ubiquinone-1 + H2O | - |
- |
CO2 + ubiquinol-1 | - |
? | |
1.2.5.3 | additional information | routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site | - |
? | - |
? | |
1.2.5.3 | additional information | routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site | Afipia carboxidovorans ATCC 49405 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.2.5.3 | heterohexamer | the functional enzyme is a (alphabetagamma)2 hexamer that consists of a small 17.8 kDa subunit (CoxS) containing two [2Fe-2S] clusters, a medium 30.2 kDa subunit (CoxM) containing an FAD cofactor, and a large 88.7 kDa subunit (CoxL) that possesses the molybdenum center | - |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.5.3 | Carbon monoxide dehydrogenase | - |
- |
1.2.5.3 | CODH | - |
- |
1.2.5.3 | molybdenum- and copper-containing carbon monoxide dehydrogenase | - |
- |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.2.5.3 | evolution | the enzyme belongs to the XOR family | - |
1.2.5.3 | physiological function | carbon monoxide dehydrogenase from Oligotropha carboxydovorans catalyzes the oxidation of carbon monoxide to carbon dioxide, providing the organism both a carbon source and energy for growth. In the oxidative half of the catalytic cycle, electrons gained from CO are ultimately passed to the electron transport chain of the Gram-negative organism. Quinones are catalytically competent as proximal acceptor of reducing equivalents from the enzyme | - |