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Literature summary for 1.2.5.3 extracted from
- Substitution of silver for copper in the binuclear Mo/Cu center of carbon monoxide dehydrogenase from Oligotropha carboxidovorans (2011), J. Am. Chem. Soc., 133, 12934-12936.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the enzyme is encoded by the megaplasmid-localized coxBCMSLDEFGHIK gene cluster, the cosMSL structural genes encoding the enzyme | Afipia carboxidovorans |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis | Afipia carboxidovorans |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | the small subunit CoxS harbors two [2Fe-2S] iron-sulfur clusters | Afipia carboxidovorans |  |
| Molybdenum | - |
Afipia carboxidovorans | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 30000 | - |
(alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE | Afipia carboxidovorans |
| 89000 | - |
(alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE | Afipia carboxidovorans |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CO + a quinone + H2O | Afipia carboxidovorans | - |
CO2 + a quinol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Afipia carboxidovorans | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | Oligotropha carboxidovorans is aerobe and able to grow with CO as sole source of both carbon and energy | Afipia carboxidovorans | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CO + a quinone + H2O | - |
Afipia carboxidovorans | CO2 + a quinol | - |
? | |
| additional information | quinones are unusual physiological oxidants for this family of enzymes | Afipia carboxidovorans | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterohexamer | (alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE | Afipia carboxidovorans |
| More | the the active site molybdenum center is located in the large subunit, while the medium subunit contains FAD, and the small subunit contains the [2Fe-2S]-clusters | Afipia carboxidovorans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| molybdenum-containing CO dehydrogenase | - |
Afipia carboxidovorans |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | bound by the medium subunit | Afipia carboxidovorans | |
| molybdenum-containing cofactor | the active site molybdenum center located in teh large subunit. The molybdenum becomes reduced in the final step of the reaction | Afipia carboxidovorans | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the noncanonical members of the xanthine oxidase family. The Mo-containing CO dehydrogenase from Oligotropha carboxidovorans and related organisms is distinct from the highly O2-sensitive Ni/Fe-containing CO dehydrogenase from obligate anaerobes such as Clostridum thermoaceticum or Methanosarcina barkerii. Quinones are unusual physiological oxidants for this family of enzymes, the overall fold of the FAD-containing domain of CO dehydrogenase resembles the dehydrogenase rather than the oxidase form of the bovine xanthine oxidoreductase, particularly with regard to the position of the mobile loop referred to above that is involved in the Dto-O conversion, but there are significant differences in the environment of the FAD in CO dehydrogenase and xanthine dehydrogenase. A Lys-Asp pair near the pyrimidine subnucleus of the flavin is preserved, for example, but the positions of the Ile and aromatic residues are reversed, with the Ile on the re side and Tyr (a Phe in the bovine enzyme) on the si side of the isoalloxazine ring | Afipia carboxidovorans |
| metabolism | the enzyme catalyzes the critical first step in this process, the oxidation of CO to CO2 with the reducing equivalents thus obtained ultimately being passed on ultimately to a CO-insensitive terminal oxidase | Afipia carboxidovorans |
| additional information | the enzyme is noncanonical in terms of the structure of the molybdenum center, the nature of the reaction catalyzed, the type of redox-active centers that are found, or some combination of these. The active site is located in the large subunit | Afipia carboxidovorans |
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Release 2023.1 (January 2023)
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