EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.7.4 | expressed in Escherichia coli | Moorella thermoacetica |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.2.7.4 | A110C | alpha subunit mutant enzyme showing electron paramagnetic resonance spectrum after Ni-activation | Moorella thermoacetica |
1.2.7.4 | A222L | alpha subunit mutant enzyme showing electron paramagnetic resonance spectrum after Ni-activation | Moorella thermoacetica |
2.3.1.169 | A110C | mutant designed to block the CO-migrating tunnel in the alpha-subunit. Electron paramagnetic resonance spectra indicates that the A-cluster is properly assembled. ACS activity is similar to that of the wild-type recombinant Ni-activated alpha-subunit | Moorella thermoacetica |
2.3.1.169 | A222L | mutant designed to block the CO-migrating tunnel in the alpha-subunit. Electron paramagnetic resonance spectra indicates that the A-cluster is properly assembled. ACS activity is similar to that of the wild-type recombinant Ni-activated alpha-subunit | Moorella thermoacetica |
6.2.1.1 | A110C | site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme | Moorella thermoacetica |
6.2.1.1 | A222L | site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme | Moorella thermoacetica |
6.2.1.1 | A265M | site-directed mutagenesis, alpha-subunit mutant, the recombinantly expressed mutant enzymes cannot be purified | Moorella thermoacetica |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.1 | CO | CO inhibits acetyl-CoA synthesis quite strongly and in a cooperative manner | Moorella thermoacetica | |
6.2.1.1 | O2 | the enzyme is O2-sensitive | Moorella thermoacetica |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.2.1.1 | 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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.2.7.4 | Ni2+ | activates | Moorella thermoacetica | |
2.3.1.169 | Iron | binding of Ni to the A-cluster slows the reduction kinetics of the [Fe4S4]2+ cubane. An upper limit of two electrons per a subunit are transferred from titanium(III) citrate to the Ni subcomponent of the A-cluster during reductive activation. These electrons are accepted quickly relative to the reduction of the [Fe4S4]2+ cubane. This reduction is probably a prerequisite for methyl group transfer | Moorella thermoacetica | |
2.3.1.169 | Nickel | binding of Ni to the A-cluster slows the reduction kinetics of the [Fe4S4]2+ cubane. An upper limit of two electrons per a subunit are transferred from titanium(III) citrate to the Ni subcomponent of the A-cluster during reductive activation. These electrons are accepted quickly relative to the reduction of the [Fe4S4]2+ cubane. This reduction is probably a prerequisite for methyl group transfer | Moorella thermoacetica | |
6.2.1.1 | Fe2+ | the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, bifunctional Ni-Fe-S containing ACS/CODH | Moorella thermoacetica | |
6.2.1.1 | Mg2+ | - |
Moorella thermoacetica | |
6.2.1.1 | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.1 | ATP + acetate + CoA | Moorella thermoacetica | - |
AMP + diphosphate + acetyl-CoA | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.7.4 | Moorella thermoacetica | - |
- |
- |
2.3.1.169 | Moorella thermoacetica | - |
- |
- |
6.2.1.1 | Moorella thermoacetica | - |
- |
- |
EC Number | Oxidation Stability | Organism |
---|---|---|
6.2.1.1 | the enzyme is O2-sensitive | Moorella thermoacetica |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.7.4 | - |
Moorella thermoacetica |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.3.1.169 | acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] | CO migrates to the A-cluster through two pathways, one involving and one not involving the tunnel | Moorella thermoacetica |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
6.2.1.1 | 7.4 | - |
Ni-activated A110C mutant alpha subunit at 1 atm CO | Moorella thermoacetica |
6.2.1.1 | 8.1 | - |
Ni-activated A222L mutant alpha subunit at 1 atm CO | Moorella thermoacetica |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.7.4 | CO + H2O + acceptor | - |
Moorella thermoacetica | CO2 + reduced acceptor | - |
? | |
6.2.1.1 | ATP + acetate + CoA | - |
Moorella thermoacetica | AMP + diphosphate + acetyl-CoA | - |
? | |
6.2.1.1 | 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 | - |
? | |
6.2.1.1 | 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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.2.1.1 | More | the beta2 subunits are solely responsible for catalyzing the CODH reaction | Moorella thermoacetica |
6.2.1.1 | tetramer | acetyl-coenzyme A synthase/carbon monoxide dehydrogenase is an alpha2beta2 tetramer, alpha-subunit structure, overview | Moorella thermoacetica |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.7.4 | acetyl coenzyme A synthase/carbon monoxide dehydrogenase | - |
Moorella thermoacetica |
1.2.7.4 | ACS/CODH | - |
Moorella thermoacetica |
1.2.7.4 | CODH | beta subunit of the bifunctional acetyl coenzyme A synthase/carbon monoxide dehydrogenase complex | Moorella thermoacetica |
6.2.1.1 | acetyl coenzyme A synthase/carbon monoxide dehydrogenase | - |
Moorella thermoacetica |
6.2.1.1 | ACS/CODH | - |
Moorella thermoacetica |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.7.4 | Ni-Fe-4S center | active site called the C-cluster | Moorella thermoacetica | |
6.2.1.1 | ATP | - |
Moorella thermoacetica |