EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.2.5.3 | Cu2+ | - |
Afipia carboxidovorans | |
1.2.5.3 | Molybdenum | - |
Afipia carboxidovorans |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.5.3 | Afipia carboxidovorans | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.5.3 | CO + a quinone + H2O | - |
Afipia carboxidovorans | CO2 + a quinol | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.5.3 | CODH | - |
Afipia carboxidovorans |
1.2.5.3 | molybdenum-copper carbon monoxide dehydrogenase | - |
Afipia carboxidovorans |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.5.3 | molybdenum cofactor | presence of a square pyramidal (Mo) oxidized active site, i.e. [(MCD)MoVIOX(Fe-S)CuI(S-Cys)]n, MCD = molybdopterin cytosine dinucleotide, X = OH3 or O4, cofactor reaction mechanism, computational modelling, overview | Afipia carboxidovorans |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.2.5.3 | additional information | the enzyme has a unique heterobimetallic Mo/Cu active site, mass spectrometric and EPR spectra analysis, overview. Key to the catalytic mechanism of the CODH site is the electronic communication between the Mo and Cu atoms | Afipia carboxidovorans |
1.2.5.3 | physiological function | the enzyme catalyzes the oxidation of CO to CO2, thereby providing carbon and energy to the organism and maintaining subtoxic levels of CO in the troposphere | Afipia carboxidovorans |