Literature summary for 1.2.5.3 extracted from

Gourlay, C.; Nielsen, D.; White, J.; Knottenbelt, S.; Kirk, M.; Young, C.
Paramagnetic active site models for the molybdenum-copper carbon monoxide dehydrogenase (2006), J. Am. Chem. Soc., 128, 2164-2165.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	-	Afipia carboxidovorans
Molybdenum	-	Afipia carboxidovorans

Organism

Organism	UniProt	Comment	Textmining
Afipia carboxidovorans	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CO + a quinone + H2O	-	Afipia carboxidovorans	CO2 + a quinol	-	?

Synonyms

Synonyms	Comment	Organism
CODH	-	Afipia carboxidovorans
molybdenum-copper carbon monoxide dehydrogenase	-	Afipia carboxidovorans

Cofactor

Cofactor	Comment	Organism	Structure
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

General Information

General Information	Comment	Organism
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
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

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Release 2023.1 (January 2023)