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Literature summary for 1.2.5.3 extracted from
- The aerobic CO dehydrogenase from Oligotropha carboxidovorans (2015), J. Biol. Inorg. Chem., 20, 243-251.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the enzyme is encoded by the coxMSL structural genes in the megaplasmid-localized coxBCMSLDEFGHIK gene cluster | Afipia carboxidovorans |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| enzyme in complex with inhibitor n-butylisonitrile, PDB ID 1N62, structure analysis | Afipia carboxidovorans |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | thiol inhibition of CO dehydrogenase | Afipia carboxidovorans | |
| n-butylisonitrile | - |
Afipia carboxidovorans |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | the enzyme's physiological position is on the inner side of the cytoplasmic membrane, membrane associated, if not membrane-integral | Afipia carboxidovorans | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | - |
Afipia carboxidovorans | |
| Molybdenum | - |
Afipia carboxidovorans | |
| [2Fe-2S] cluster | two [2Fe-2S] iron-sulfur clusters in the small subunit | Afipia carboxidovorans | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CO + ubiquinone + H2O | Afipia carboxidovorans | ubiquinone is the likely physiological oxidant for CO dehydrogenase | CO2 + ubiquinol | - |
? | |
| additional information | Afipia carboxidovorans | air-stable CO dehydrogenase having a binuclear molybdenum- and copper-containing active site catalyzes the first step in this process, the oxidation of CO to CO2, with the reducing equivalents. Enzyme reduction and reactivity with H2, kinetics, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Afipia carboxidovorans | P19919 and P19920 and P19921 | genes coxL, coxM, and coxS; the enzyme is encoded by coxMSL structural genes in the megaplasmid-localized coxBCMSLDEFGHIK gene cluster | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| CO + a quinone + H2O = CO2 + a quinol | proposed reaction mechanisms for CO dehydrogenase, the rate-limiting step for overall turnover resides in the reductive half-reaction, reoxidation of reduced enzyme by quinones occurs at the FAD site | Afipia carboxidovorans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CO + 1,2-naphthoquinone-4-sulfonic acid + H2O | - |
Afipia carboxidovorans | CO2 + 1,2-naphthoquinol-4-sulfonic acid | - |
? | |
| CO + 1,4-naphthoquinone + H2O | - |
Afipia carboxidovorans | CO2 + 1,4-naphthoquinol | - |
? | |
| CO + a quinone + H2O | - |
Afipia carboxidovorans | CO2 + a quinol | - |
? | |
| CO + benzoquinone + H2O | - |
Afipia carboxidovorans | CO2 + benzoquinol | - |
? | |
| CO + ubiquinone + H2O | ubiquinone is the likely physiological oxidant for CO dehydrogenase | Afipia carboxidovorans | CO2 + ubiquinol | - |
? | |
| additional information | air-stable CO dehydrogenase having a binuclear molybdenum- and copper-containing active site catalyzes the first step in this process, the oxidation of CO to CO2, with the reducing equivalents. Enzyme reduction and reactivity with H2, kinetics, overview | Afipia carboxidovorans | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterohexamer | (abc)2 structure, each protomer of the enzyme has a small subunit (CoxS, 18 kDa) with two [2Fe-2S] iron-sulfur clusters, a medium subunit (CoxM, 30 kDa) that possesses FAD, and a large subunit (CoxL, 89 kDa) that has the active site binuclear center | Afipia carboxidovorans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| aerobic Mo/Cu-containing CO dehydrogenase | - |
Afipia carboxidovorans |
| molybdenum- and copper-dependent CO dehydrogenase | - |
Afipia carboxidovorans |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| benzoquinone | - |
Afipia carboxidovorans | |
| FAD | located in the medium subunit | Afipia carboxidovorans | |
| molybdopterin cofactor | the structure of the active site binuclear center of CO dehydrogenase in its oxidized form, overview. The oxidized Mo(VI) ion has the distorted square-pyramidal coordination geometry seen in other members of the xanthine oxidase family of molybdenum-containing enzymes, with an apical Mo=O and an equatorial plane consisting of a second Mo=O group rather than the catalytically labile Mo-OH seen in other family members and two sulfurs from a pyranopterin cofactor that is common to all molybdenum and tungsten enzymes. The pyranopterin cofactor is present as the dinucleotide of cytosine | Afipia carboxidovorans | |
| quinone | quinone cofactors interact with CODH at its FAD site | Afipia carboxidovorans | |
| ubiquinone-1 | - |
Afipia carboxidovorans | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | despite the unique nature of the binuclear active site of CO dehydrogenase the enzyme is clearly a member of the xanthine oxidase family of molybdenum-containing enzymes | Afipia carboxidovorans |
| malfunction | thiol inhibition of CO dehydrogenase may be a physiologically important mechanism of enzyme regulation | Afipia carboxidovorans |
| metabolism | four other genes (coxB, coxC, coxH and coxK) are predicted to encode proteins possessing one (CoxB) to as many as nine (CoxK) transmembrane helices, one or more of which are likely to be involved in anchoring CO dehydrogenase to its physiological position on the inner side of the cytoplasmic membrane | Afipia carboxidovorans |
| additional information | the enzyme possesses a deeply buried binuclear center of CO dehydrogenase activity | Afipia carboxidovorans |
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