Protein Variants | Comment | Organism |
---|---|---|
A110C | site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme | Moorella thermoacetica |
A222L | site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme | Moorella thermoacetica |
A265M | site-directed mutagenesis, alpha-subunit mutant, the recombinantly expressed mutant enzymes cannot be purified | Moorella thermoacetica |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CO | CO inhibits acetyl-CoA synthesis quite strongly and in a cooperative manner | Moorella thermoacetica | |
O2 | the enzyme is O2-sensitive | Moorella thermoacetica |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics and extent of reduction of the Fe4S4 cubane in the apo-alpha subunit and the Ni-activated a subunit upon exposure to titanium(III) citrate, detailed overview | Moorella thermoacetica |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, bifunctional Ni-Fe-S containing ACS/CODH | Moorella thermoacetica | |
Mg2+ | - |
Moorella thermoacetica | |
Ni2+ | activates, the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, bifunctional Ni-Fe-S containing ACS/CODH. Upon incubation in NiCl2, the complete A-cluster assembles, and the isolated a subunit develops approximately 10% of the maximal catalytic activity relative to that of the alpha2beta2 tetramer | Moorella thermoacetica |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + acetate + CoA | Moorella thermoacetica | - |
AMP + diphosphate + acetyl-CoA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Moorella thermoacetica | - |
- |
- |
Oxidation Stability | Organism |
---|---|
the enzyme is O2-sensitive | Moorella thermoacetica |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
7.4 | - |
Ni-activated A110C mutant alpha subunit at 1 atm CO | Moorella thermoacetica |
8.1 | - |
Ni-activated A222L mutant alpha subunit at 1 atm CO | Moorella thermoacetica |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + acetate + CoA | - |
Moorella thermoacetica | AMP + diphosphate + acetyl-CoA | - |
? | |
ATP + acetate + CoA | the ACS reaction is catalyzed at the alpha-subunit A-cluster, an [Fe4S4] cubane bridged to a dinickel [NipNid] subcomponent, overview | Moorella thermoacetica | AMP + diphosphate + acetyl-CoA | - |
? | |
additional information | bifunctional Ni-Fe-S containing ACS/CODH, although alpha and beta subunits catalyze separate reactions, they interact functionally when CO2 is used as a substrate in the synthesis of acetyl-CoA | Moorella thermoacetica | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the beta2 subunits are solely responsible for catalyzing the CODH reaction | Moorella thermoacetica |
tetramer | acetyl-coenzyme A synthase/carbon monoxide dehydrogenase is an alpha2beta2 tetramer, alpha-subunit structure, overview | Moorella thermoacetica |
Synonyms | Comment | Organism |
---|---|---|
acetyl coenzyme A synthase/carbon monoxide dehydrogenase | - |
Moorella thermoacetica |
ACS/CODH | - |
Moorella thermoacetica |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Moorella thermoacetica |