Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetyl-CoA + corrinoid protein
CoA + CO + methylcorrinoid protein
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA
CH3-CO-S-CoA + corrinoid/iron-sulfur protein
CH3-CO-S-CoA + H+ + tetrahydromethanopterin
CH3-tetrahydromethanopterin + CO + HS-CoA
CH3-CO-S-CoA + tetrahydrosarcinapterin + H2O
CH3-tetrahydrosarcinapterin + CO2 + H+ + electron
CH3-tetrahydrofolate + CO + HS-CoA
CH3-CO-S-CoA + tetrahydrofolate
CH3-tetrahydrosarcinapterin + CO + HS-CoA
CH3-CO-S-CoA + tetrahydrosarcinapterin
-
-
-
?
CH3I + CO + HS-CoA
CH3-CO-S-CoA + HI
CO + H2O
CO2 + H+ + electron
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
CO2 + H+ + electron
CO + H2O
additional information
?
-
acetyl-CoA + corrinoid protein
CoA + CO + methylcorrinoid protein
-
-
-
-
r
acetyl-CoA + corrinoid protein
CoA + CO + methylcorrinoid protein
-
-
-
-
r
acetyl-CoA + corrinoid protein
CoA + CO + methylcorrinoid protein
-
-
-
-
r
acetyl-CoA + corrinoid protein
CoA + CO + methylcorrinoid protein
-
-
-
-
r
acetyl-CoA + corrinoid protein
CoA + CO + methylcorrinoid protein
-
-
-
-
?
acetyl-CoA + corrinoid protein
CoA + CO + methylcorrinoid protein
-
Fd-II can act as a redox mediator by accepting electrons from the acetyl-ACS intermediate and by serving as the initial reducing agent linked to formation of the Ni1+-CO catalytic intermediate
-
-
?
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA
CH3-CO-S-CoA + corrinoid/iron-sulfur protein
-
-
-
-
?
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA
CH3-CO-S-CoA + corrinoid/iron-sulfur protein
-
-
-
-
?
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA
CH3-CO-S-CoA + corrinoid/iron-sulfur protein
-
-
-
?
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA
CH3-CO-S-CoA + corrinoid/iron-sulfur protein
-
under anaerobic conditions
-
?
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA
CH3-CO-S-CoA + corrinoid/iron-sulfur protein
-
under anaerobic conditions
-
?
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA
CH3-CO-S-CoA + corrinoid/iron-sulfur protein
-
under anaerobic conditions
-
-
?
CH3-CO-S-CoA + H+ + tetrahydromethanopterin
CH3-tetrahydromethanopterin + CO + HS-CoA
-
-
?
CH3-CO-S-CoA + H+ + tetrahydromethanopterin
CH3-tetrahydromethanopterin + CO + HS-CoA
-
-
?
CH3-CO-S-CoA + tetrahydrosarcinapterin + H2O
CH3-tetrahydrosarcinapterin + CO2 + H+ + electron
-
the carbon monoxide dehydrogenase-corrinoid enzyme complex catalyzes the cleavage of acetyl-CoA, tetrahydrosarcinapterin functions as the methyl group acceptor, the major products of reaction are methyltetrahydrosarcinapterin and CO2, free CoA is identified as an additional product
-
-
?
CH3-CO-S-CoA + tetrahydrosarcinapterin + H2O
CH3-tetrahydrosarcinapterin + CO2 + H+ + electron
-
the carbon monoxide dehydrogenase-corrinoid enzyme complex catalyzes the cleavage of acetyl-CoA, tetrahydrosarcinapterin functions as the methyl group acceptor, the major products of reaction are methyltetrahydrosarcinapterin and CO2, free CoA is identified as an additional product
-
?
CH3-tetrahydrofolate + CO + HS-CoA
CH3-CO-S-CoA + tetrahydrofolate
-
-
-
?
CH3-tetrahydrofolate + CO + HS-CoA
CH3-CO-S-CoA + tetrahydrofolate
-
-
-
-
?
CH3-tetrahydrofolate + CO + HS-CoA
CH3-CO-S-CoA + tetrahydrofolate
-
-
-
?
CH3-tetrahydrofolate + CO + HS-CoA
CH3-CO-S-CoA + tetrahydrofolate
-
this multistep reaction involves four proteins: CO dehydrogenase, methyltransferase, the corrinoid/iron-sulfur protein and ferredoxin
-
?
CH3-tetrahydrofolate + CO + HS-CoA
CH3-CO-S-CoA + tetrahydrofolate
-
The methyltransferase catalyses the reaction of CH3-H4folate with the corrinoid/iron-sulfur protein to form a methylcobalt species. The Ni/Fe-S enzyme CO dehydrogease then catalyses the final steps in the formation of acetyl-CoA.
-
?
CH3I + CO + HS-CoA
CH3-CO-S-CoA + HI
-
the multienzyme complex catalyses the acetyl-CoA synthesis from CH3I, CO and CoA as well as to cleave acetyl-CoA into its methyl, carbonyl, and CoA components as the first step in the catabolism of acetyl-CoA to methane and CO2
-
-
?
CH3I + CO + HS-CoA
CH3-CO-S-CoA + HI
-
-
-
?
CH3I + CO + HS-CoA
CH3-CO-S-CoA + HI
-
-
-
?
CO + H2O
CO2 + H+ + electron
-
-
-
r
CO + H2O
CO2 + H+ + electron
the multienzyme complex catalyses the reversible oxidation of CO to CO2
-
r
CO + H2O
CO2 + H+ + electron
the multienzyme complex catalyses the reversible oxidation of CO to CO2
-
r
CO + H2O
CO2 + H+ + electron
-
the multienzyme complex catalyses the reversible oxidation of CO to CO2
-
r
CO + H2O
CO2 + H+ + electron
-
the NiFe4S4-5C cluster catalyses the reversible oxidation of CO to CO2
-
r
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
-
-
-
?
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
-
acetyl-CoA synthase catalyses acetyl-CoA synthesis, an intermediate step is the transfer of the cobalt-bound methyl group from methylated corrinoid/iron-sulfur protein to the acetyl-CoA synthase
-
?
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
-
-
-
?
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
-
-
-
?
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
-
-
-
?
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
-
-
-
?
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
-
-
-
?
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
-
-
-
?
CO + methyl-X + HS-CoA
CH3-CO-S-CoA + HX
-
acetyl-CoA synthase catalyses acetyl-CoA synthesis, an intermediate step is the transfer of the cobalt-bound methyl group from methylated corrinoid/iron-sulfur protein to the acetyl-CoA synthase
-
?
CO2 + H+ + electron
CO + H2O
-
CO dehydrogenase catalyses the two-electron reduction of CO2 to CO
-
?
CO2 + H+ + electron
CO + H2O
-
CO dehydrogenase catalyses the two-electron reduction of CO2 to CO
-
?
additional information
?
-
-
the enzyme catalyzes the exchange of 14C from the carboxyl group of acetyl-CoA with 12C from CO
-
-
?
additional information
?
-
-
an Fe/S-containing active site metal center, the A cluster, catalyzes acetyl CC bond formation/breakdown. Carbonyl group exchange of acetyl-CoA with CO is a hallmark of CODH/ACS, coupling analysis of the recombinant A cluster protein of acetyl-CoA synthase of Carboxydothermus hydrogenoformans, ACSCh, and truncated ACSCh lacking its 317-amino acid N-terminal domain, overview
-
-
?
additional information
?
-
-
in assays of bacterial ACS, methylated corrinoid iron-sulfur protein is generally used as the source of methyl groups for acetyl-CoA synthesis
-
-
?
additional information
?
-
-
an Fe/S-containing active site metal center, the A cluster, catalyzes acetyl CC bond formation/breakdown. Carbonyl group exchange of acetyl-CoA with CO is a hallmark of CODH/ACS, coupling analysis of the recombinant A cluster protein of acetyl-CoA synthase of Carboxydothermus hydrogenoformans, ACSCh, and truncated ACSCh lacking its 317-amino acid N-terminal domain, overview
-
-
?
additional information
?
-
-
methylcobinamide, methylcobalamin, and CH3-(Me3-benzimidazolyl)cobamide are substrates of the acetyl-CoA synthase, methylcobalamin is 2000fold less reactive than methylcobinamide, CO dehydrogenase catalyses the CO-dependent reduction of methylcobinamide 10000fold faster than that of methylcobalamin
-
-
?
additional information
?
-
-
the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation
-
-
?
additional information
?
-
the multienzyme complex catalyses the exchange between free CO and carbonyl group of acetyl-CoA, and the exchange between CoA and the CoA moiety of acetyl-CoA
-
-
?
additional information
?
-
-
the multienzyme complex catalyses the exchange between free CO and carbonyl group of acetyl-CoA, and the exchange between CoA and the CoA moiety of acetyl-CoA
-
-
?
additional information
?
-
-
an nickel-containing active site metal center, the A cluster, catalyzes acetyl C-C bond formation/breakdown. Carbonyl group exchange of acetyl-CoA with CO is weakly active in ACDS, and exchange with CO2 is up to 350 times faster, indicating tight coupling of CO release at the A cluster to CO oxidation to CO2 at the C cluster in CO dehydrogenase, coupling analysis of the recombinant A cluster protein of ACDS. Direct role of the ACS N-terminal domain in promoting acetyl C-C bond fragmentation. Protein conformational changes, related to open/closed states have direct effects on the coordination geometry and stability of the A cluster Ni2+-acetyl intermediate, controlling Ni2-acetyl fragmentation and Ni2(CO)(CH3) condensation. Involvement of subunit-subunit interactions in ACDS, versus interdomain contacts in ACS, ensures that CO is not released from the ACDS beta-subunit in the absence of appropriate interactions with the alpha2epsilon2 CO dehydrogenase component, ACDS complex partial reactions in the overall synthesis and cleavage of acetyl-CoA, overview
-
-
?
additional information
?
-
-
an nickel-containing active site metal center, the A cluster, catalyzes acetyl C-C bond formation/breakdown. Carbonyl group exchange of acetyl-CoA with CO is weakly active in ACDS, and exchange with CO2 is up to 350 times faster, indicating tight coupling of CO release at the A cluster to CO oxidation to CO2 at the C cluster in CO dehydrogenase, coupling analysis of the recombinant A cluster protein of ACDS. Direct role of the ACS N-terminal domain in promoting acetyl C-C bond fragmentation. Protein conformational changes, related to open/closed states have direct effects on the coordination geometry and stability of the A cluster Ni2+-acetyl intermediate, controlling Ni2-acetyl fragmentation and Ni2(CO)(CH3) condensation. Involvement of subunit-subunit interactions in ACDS, versus interdomain contacts in ACS, ensures that CO is not released from the ACDS beta-subunit in the absence of appropriate interactions with the alpha2epsilon2 CO dehydrogenase component, ACDS complex partial reactions in the overall synthesis and cleavage of acetyl-CoA, overview
-
-
?
additional information
?
-
the multienzyme complex catalyses the exchange between free CO and carbonyl group of acetyl-CoA, and the exchange between CoA and the CoA moiety of acetyl-CoA
-
-
?
additional information
?
-
-
enzyme catalyses the CoA/acetyl-CoA exchange
-
-
?
additional information
?
-
-
methylcobinamide, methylcobalamin, and CH3-(Me3-benzimidazolyl)cobamide are substrates of the acetyl-CoA synthase, methylcobalamin is 2000fold less reactive than methylcobinamide, CO dehydrogenase catalyses the CO-dependent reduction of methylcobinamide 10000fold faster than that of methylcobalamin
-
-
?
additional information
?
-
-
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
-
-
?
additional information
?
-
-
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
-
-
?
additional information
?
-
-
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
-
-
?
additional information
?
-
-
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
-
-
?
additional information
?
-
-
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
-
-
?
additional information
?
-
-
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
-
-
?
additional information
?
-
-
key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway
-
-
?
additional information
?
-
-
enzyme and a corrinoid/iron-sulfur protein, methyltransferase and an electron transfer protein such as ferredoxin II play a pivotal role in the conversion of methylhydrofolate, CO, and CoA to acetyl-CoA
-
-
?
additional information
?
-
-
the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation
-
-
?
additional information
?
-
CoA is the last substrate to bind and CO and the methyl group bind randomly as the first substrate in acetyl-CoA synthesis. In pulse-chase experiments, up to 100% of the methyl groups and CoA and up to 60-70% of the CO employed in the pulse phase can be trapped in the product acetyl-CoA
-
-
?
additional information
?
-
-
the purified carbon monoxide dehydrogenase, EC 1.2.7.4, from Clostridium thermoaceticum is the only protein required to catalyze a reversible exchange reaction between carbon monoxide and the carbonyl group of acetyl-CoA. Carbon dioxide also exchanges with the C-1 of acetyl-coA, but at a much lower rate than does CO
-
-
?
additional information
?
-
mechanism by which acetyl-CoA is assembled at the A-cluster and mechanism of CO2 reduction at the C-cluster, overview
-
-
?