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Literature summary extracted from

  • Wilcoxen, J.; Snider, S.; Hille, R.
    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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.5.3 the enzyme is encoded by the megaplasmid-localized coxBCMSLDEFGHIK gene cluster, the cosMSL structural genes encoding the enzyme Afipia carboxidovorans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.5.3 crystal structure analysis Afipia carboxidovorans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.7.4 0.00295
-
 methylene blue Ag+-substituted enzyme, at pH 7.0 and 25°C Afipia carboxidovorans
1.2.7.4 0.0107
-
 methylene blue native enzyme, at pH 7.0 and 25°C Afipia carboxidovorans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.5.3 Fe2+ the small subunit CoxS harbors two [2Fe-2S] iron-sulfur clusters Afipia carboxidovorans
1.2.5.3 Molybdenum
-
 Afipia carboxidovorans
1.2.7.4 Cu2+ the native enzyme contains copper in the active site Afipia carboxidovorans
1.2.7.4 [2Fe-2S]-center the small subunit contains two [2Fe-2S] centers Afipia carboxidovorans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.5.3 30000
-
 (alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE Afipia carboxidovorans
1.2.5.3 89000
-
 (alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE Afipia carboxidovorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.5.3 CO + a quinone + H2O Afipia carboxidovorans
-
 CO2 + a quinol
-
 ?
1.2.7.4 CO + H2O + acceptor Afipia carboxidovorans
-
 CO2 + reduced acceptor
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.5.3 Afipia carboxidovorans
-
-
-
1.2.7.4 Afipia carboxidovorans P19919 and P19920 and P19921 P19919 large subunit, P19920 medium subunit, P19921 small subunit
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.5.3 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.5.3 CO + a quinone + H2O
-
 Afipia carboxidovorans CO2 + a quinol
-
 ?
1.2.5.3 additional information quinones are unusual physiological oxidants for this family of enzymes Afipia carboxidovorans ?
-
 ?
1.2.7.4 CO + H2O + acceptor
-
 Afipia carboxidovorans CO2 + reduced acceptor
-
 ?
1.2.7.4 CO + H2O + methylene blue
-
 Afipia carboxidovorans CO2 + reduced methylene blue
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.5.3 heterohexamer (alphabetagamma)2, 2 * 89000, large subunit, + 1 * 30000, medium subunit, + 1 * 1800, small subunit, SDS-PAGE Afipia carboxidovorans
1.2.5.3 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
1.2.7.4 heterohexamer
-
 Afipia carboxidovorans

Synonyms

EC Number Synonyms Comment Organism
1.2.5.3 molybdenum-containing CO dehydrogenase
-
 Afipia carboxidovorans
1.2.7.4 CODH
-
 Afipia carboxidovorans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.7.4 8.2
-
 methylene blue Ag+-substituted enzyme, at pH 7.2 and 25°C Afipia carboxidovorans
1.2.7.4 93.3
-
 methylene blue native enzyme, at pH 7.2 and 25°C Afipia carboxidovorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.5.3 FAD bound by the medium subunit Afipia carboxidovorans
1.2.5.3 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
1.2.7.4 FAD the medium subunit contains FAD Afipia carboxidovorans

General Information

EC Number General Information Comment Organism
1.2.5.3 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
1.2.5.3 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
1.2.5.3 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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.7.4 2780
-
 methylene blue Ag+-substituted enzyme, at pH 7.2 and 25°C Afipia carboxidovorans
1.2.7.4 8700
-
 methylene blue native enzyme, at pH 7.2 and 25°C Afipia carboxidovorans