KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | rapid reaction kinetics, steady-state kinetics | Afipia carboxidovorans | |
0.0107 | - |
CO | pH 7.2, 25°C | Afipia carboxidovorans |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu | essential for enzyme activity, 1.69 Cu per mol of enzyme dimer | Afipia carboxidovorans | |
Fe2+ | 8.05 Fe per mol of enzyme dimer, in the Fe-S cluster | Afipia carboxidovorans | |
Mo3+ | essential for enzyme activity, 1.82 Mo per mol of enzyme dimer | Afipia carboxidovorans | |
additional information | metal contents are determined by inductively coupled plasma atomic emission spectrometry | Afipia carboxidovorans | |
Se | - |
Afipia carboxidovorans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
CO + a quinone + H2O | Afipia carboxidovorans | - |
CO2 + a quinol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Afipia carboxidovorans | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
CO + a quinone + H2O = CO2 + a quinol | CO initially binds rapidly to the enzyme, possibly at the Cu(I) of the active site, prior to undergoing oxidation. A Mo(V) species exhibits strong coupling to the copper of the active center, the rate-limiting step of overall turnover is likely in the reductive half-reaction | Afipia carboxidovorans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
CO + a quinone + H2O | - |
Afipia carboxidovorans | CO2 + a quinol | - |
? | |
CO + a quinone + H2O | the enzyme catalyzes the oxidation of CO to CO2, yielding two electrons and two H+ | Afipia carboxidovorans | CO2 + a quinol | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CO dehydrogenase | - |
Afipia carboxidovorans |
CODH | - |
Afipia carboxidovorans |
molybdenum-copper CO dehydrogenase | - |
Afipia carboxidovorans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Afipia carboxidovorans |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
51.1 | - |
CO | pH 7.2, 25°C, reductive half-reaction of enzyme CODH with CO | Afipia carboxidovorans | |
93.3 | - |
CO | pH 7.2, 25°C | Afipia carboxidovorans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
- |
Afipia carboxidovorans |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.5 | 10 | only modest loss of activity at these extreme pHs indicates that ionization of functional groups in the active site is not as critical to catalysis for CODH | Afipia carboxidovorans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Afipia carboxidovorans | |
additional information | presence of FAD, Fe/S clusters, and a [CuSMoO2] coordination in the active site determined by Raman spectra | Afipia carboxidovorans | |
[CuSMoO2] cofactor | - |
Afipia carboxidovorans |
General Information | Comment | Organism |
---|---|---|
physiological function | Oligotropha carboxidovorans is a carboxydotrophic bacterium capable of aerobic, chemolithoautotrophic growth using COas a sole source of carbon and energy. The key enzyme involved in this facultative metabolism is an air-stable molybdenum-containing CO dehydrogenase that catalyzes the oxidation of CO to CO2 | Afipia carboxidovorans |