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Literature summary for 1.2.7.4 extracted from

  • Carlson, E.; Papoutsakis, E.
    Heterologous expression of the Clostridium carboxidivorans CO dehydrogenase alone or together with the acetyl coenzyme A synthase enables both reduction of CO2 and oxidation of CO by Clostridium acetobutylicum (2017), Appl. Environ. Microbiol., 83, e00829 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.7.4

Activating Compound

Activating Compound Comment Organism Structure
H2 externally added H2 enhances the CODH-catalyzed CO formation from CO2 reduction Clostridium carboxidivorans

Inhibitors

Inhibitors Comment Organism Structure
CO substrate inhibition. Increasing CO concentrations in the gas phase inhibit CODH activity Clostridium carboxidivorans

Metals/Ions

Metals/Ions Comment Organism Structure
Ni2+ required. Nickel is inserted into CODH without the need to express the native Ni insertase protein Clostridium carboxidivorans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
300000
-
 gel filtration Clostridium carboxidivorans

Organism

Organism UniProt Comment Textmining
Clostridium carboxidivorans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO + H2O + 2 oxidized ferredoxin
-
 Clostridium carboxidivorans CO2 + 2 reduced ferredoxin + 2 H+
-
 r
CO2 + 2 reduced ferredoxin + 2 H+
-
 Clostridium carboxidivorans CO + H2O + 2 oxidized ferredoxin
-
 r

Subunits

Subunits Comment Organism
tetramer 2 * 67600, CODH-subunit, 2 * 77500, ACS-subunit, SDS-PAGE Clostridium carboxidivorans

Synonyms

Synonyms Comment Organism
CODH
-
 Clostridium carboxidivorans

General Information

General Information Comment Organism
physiological function functional expression of the CODH/acetyl-CoA synthase ACS complex in Clostridium acetobutylicum, engineered to express CODH alone or together with the ACS. Both strains exhibit CO2 reduction and CO oxidation activities. CODH uses a native C. acetobutylicum ferredoxin as an electron carrier for CO2 reduction. Heterologous CODH activity depends on actively growing cells and requires the addition of nickel, which is inserted into CODH without the need to express the native Ni insertase protein. Increasing CO concentrations in the gas phase inhibit CODH activity and alter the metabolite profile of the CODH-expressing cells Clostridium carboxidivorans