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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
pathway
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
pathway
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
kinetics of methyl group transfer between the cobalt of the corrinoid/iron-sulfur protein and the nickel of Ni-X-Fe4S4 cluster, called the A-cluster of enzyme, the reaction is reversible
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
The transfer of Co bound methyl group from methylated corrinoid/iron-sulfur protein to acetyl-CoA synthase is an SN2 attack of a nucleophilic center of enzyme, presumably Ni4, on the methyl-Co(III) stat of the corrinoid/iron-sulfur protein, generating Co(I) and methylating acetyl-CoA synthase.
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
The transfer of Co bound methyl group from methylated corrinoid/iron-sulfur protein to acetyl-CoA synthase is an SN2 attack of a nucleophilic center of enzyme, presumably Ni4, on the methyl-Co(III) stat of the corrinoid/iron-sulfur protein, generating Co(I) and methylating acetyl-CoA synthase.
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
enzyme contains binding sites for the methyl, carbonyl, and CoA moieties of acetyl-CoA and catalyses the assembly of acetyl-CoA from these enzyme-bound groups, under optimal conditions the rate-limiting step involves methylation of enzyme by the methylated corrinoid/iron-sulfur protein
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
the corronoid protein functions as methyl group carrier during acetyl-CoA synthesis and decomposition
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
the multienzyme complex contains at least two protein components: a CO-oxidizing Ni/Fe-S component and a Co/Fe-S component
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
the FeS cluster is present to relay electrons from enzyme to CO
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
Enzyme accepts the methyl group from the methylated corrinoid/iron-sulfur protein, binds a carbonyl group from CO, CO2, or the carboxyl of pyruvate, and binds coenzyme A. Then the enzyme catalyses the synthesis of acetyl-CoA from these enzyme bound groups. Additionally the enzyme catalyses two exchange reactions between the methylated corrinoid/iron-sulfur protein and methylated enzyme and between methylated enzyme and the methyl moiety of acetyl-CoA.
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
the transfer of methyl group to enzyme occurs by SN2-type nucleophilic displacement, not a radical, reaction
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
the Ni-Fe4S4-5C cluster of enzyme catalyses the reversible reduction of CO2 to CO and is located in the beta-subunit. CO generated at this site migrates through the tunnel to the A-cluster, located in the alpha-subunit, where it reacts with CoA and a methyl group to generate acetyl-CoA. During catalysis, the two sites are mechanistically coupled.
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
the enzyme-bound complex is an [NiFe3-4S4]-acetyl complex
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
investigation of putative intermediate states from the catalytic cycle by hybrid density functional theory. A mononuclear mechanism in which CO and CH3 bind the proximal nickel is favored over the binuclear mechanism in which CO and CH3 bind the proximal and distal nickel ions resp. The formation of a disulfide bond in the active site could provide the two electrons necessary for the reaction if methylation occurs simultaneously. The crystallographic closed form of the active site needs to open to accomodate ligands in the equatorial state
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
stopped-flow analysis of two steps within the catalytic cycle. Vast majority of enzymes within a population should be in the methylated form suggesting that the following CO insertion step is rate limiting. Reaction rate is most sensitively affected by a change in the rate coefficient associated with the CO insertion step
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
two electrons are required for reductive activation of enzyme, starting from the oxidized state containing Ni2+. A Ni0 state may form upon reductive activation and reform after each catalytic cycle
-
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
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
CoA is the last substrate to bind and CO and the methyl group bind randomly as the first substrate in acetyl-CoA synthesis
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
chemical steps and conformational changes in the mechanism of acetyl-CoA synthase, overview
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
chemical steps and conformational changes in the mechanism of acetyl-CoA synthase, overview
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
the methyl and carbonyl groups bind to ACS in a random manner before the strictly ordered binding of the third substrate, CoA, mechanism of acetyl-CoA synthesis by ACS, overview
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
chemical steps and conformational changes in the mechanism of acetyl-CoA synthase, overview
-
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
chemical steps and conformational changes in the mechanism of acetyl-CoA synthase, overview
-
-
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
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
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
-
-
-
-
?
additional information
?
-
-
the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation
-
-
?
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co3+
-
part of the methylcorrinoid protein
Cu
-
the Ni in cluster A can be replaced by Cu yielding an inactive form of the acetyl-CoA synthase
Cu+
-
capture of Ni2+, Cu+ and Zn2+ by thiolate sulfurs of an N2S2Ni complex
Cu2+
the enzyme has a metallocofactor containing iron, sulfur, copper, and nickel, the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site
Zn
-
the Ni in cluster A can be replaced by Zn yielding an inactive form of the acetyl-CoA synthase
Zn2+
-
capture of Ni2+, Cu+ and Zn2+ by thiolate sulfurs of an N2S2Ni complex
CO
-
cobalt is the active site for the methyltransfer reaction
CO
-
a cobalt-containing Co/Fe-S component of multienzyme complex serves as a methyl carrier in the pathway of methane synthesis from acetate
CO
-
a cobalt-containing Co/Fe-S component of multienzyme complex serves as a methyl carrier in the pathway of methane synthesis from acetate
CO
-
cobalt is the active site for the methyltransfer reaction
copper
or iron, required. Copper is one of the most abundant metal species within the cells
copper
-
the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site. Distorted Cu(I)-S3 site in the fully active enzyme in solution. Average Cu-S bond length of 2.25 A and a metal neighbor at 2.65 A, consistent with the Cu-Ni distance observed in the crystal structure. Cu-SCoA intermediate in the mechanism of acetyl-CoA synthesis. Essential and functional role for copper in the enzyme
Fe
-
corrinoid/iron-sulfur protein required
Fe
-
corrinoid/iron-sulfur protein required
Fe
corrinoid/iron-sulfur protein required
Fe
-
the multienzyme complex contains at least two protein components: a CO-oxidizing Ni/Fe-S component and a cobalt-containing Co/Fe-S component
Fe
a Ni/Fe-S cluster of multienzyme CO dehydrogenase/acetyl-CoA synthase complex is the active site of acetyl-CoA cleavage and synthesis
Fe
-
the Ni-Fe4S4-5C cluster of enzyme catalyses the reversible reduction of CO2 to CO and is located in the beta-subunit.
Fe
-
corrinoid/iron-sulfur protein required
Fe
-
the enzyme-bound complex can be described as an [NiFe3-4S4]-acetyl complex
Fe2+
-
Fe/S-containing active site metal center, the A cluster
Fe2+
the enzyme has a metallocofactor containing iron, sulfur, copper, and nickel, the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site
Iron
or copper, required
Iron
-
protein contains in average 3.7 Fe atoms and 1.6 Ni atoms per monomer molecule, which is consistent with the presence of a [NipNid]-[Fe4S4]-center
Iron
-
the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site
Iron
-
Mössbauer and EPR study of enzyme alpha-subunit. About 70% contain [Fe4S4]1+ cubanes, and 30% contain [Fe4S4]2+ cubanes suggesting an extremely low [Fe4S4] 1+/2+ reduction potential
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
Ni
-
the functional cluster A of ACSCh contains a Ni-Ni-[4Fe-4S] site, in which the position proximal and distal to the cubane are occupied by Ni ions
Ni
-
the multienzyme complex contains at least two protein components: a CO-oxidizing Ni/Fe-S component and a cobalt-containing Co/Fe-S component
Ni
a Ni/Fe-S cluster of multienzyme CO dehydrogenase/acetyl-CoA synthase complex is the active site of acetyl-CoA cleavage and synthesis
Ni
-
the Ni-Fe4S4-5C cluster of enzyme catalyses the reversible reduction of CO2 to CO and is located in the beta-subunit.
Ni
-
the enzyme-bound complex can be described as an [NiFe3-4S4]-acetyl complex
Ni
-
enzyme contains nickel in the A-cluster of the enzyme
Ni2+
-
required as reductant of the methylcorrinoid protein
Ni2+
-
nickel-containing active site metal center, the A cluster, a binuclear Ni-Ni center bridged by a cysteine thiolate to an [Fe4S4] cluster. Ni2+-CO equatorial coordination environment in closed buried hydrophobic and open solvent-exposed states
Ni2+
-
capture of Ni2+, Cu+ and Zn2+ by thiolate sulfurs of an N2S2Ni complex
Ni2+
the enzyme has a metallocofactor containing iron, sulfur, copper, and nickel, instead of a [Fe4S4] cubane bridged to a mononuclear Ni site, the Ni is part of a Fe-[NiFe3S4] cluster
Ni2+
-
formation of the NiFeC species
Nickel
enzyme contains two-center zerovalent nickel complexes. The proximal nickel atom Ni easily assumes planar, tetrahedral, and intermediate type coordination
Nickel
-
protein contains in average 3.7 Fe atoms and 1.6 Ni atoms per monomer molecule, which is consistent with the presence of a [NipNid]-[Fe4S4]-center
Nickel
-
structural analogues of the bimetallic reaction center in acetyl CoA synthase: A Ni-Ni Model with bound CO
Nickel
-
the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site. Distorted Cu(I)-S3 site in the fully active enzyme in solution. Average Cu-S bond length of 2.25 A and a metal neighbor at 2.65 A, consistent with the Cu-Ni distance observed in the crystal structure
Nickel
-
two electrons are required for reductive activation of enzyme, starting from the oxidized state containing Ni2+. A Ni0 state may form upon reductive activation and reform after each catalytic cycle
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
Nickel
-
synthesis of a dinuclear nickel complex with methyl and thiolate ligands, Ni(N,N'-diethyl-3,7-diazanonane-1,9-dithiolate)Ni(Me)(2,6-dimesitylphenyl) as a dinuclear Nid-Nip-site model of acetyl-CoA synthase. The reaction of Ni(N,N'-diethyl-3,7-diazanonane-1,9-dithiolate)Ni(Me)(2,6-dimesitylphenyl) withexcess CO affords the acetylthioester CH3C(O)-2,6-dimesitylphenyl with concomitant formation of Ni(N,N'-diethyl-3,7-diazanonane-1,9-dithiolate)Ni(CO)2 and Ni(CO)4 plus Ni(N,N'-diethyl-3,7-diazanonane-1,9-dithiolate). When complex Ni(N,N'-diethyl-3,7-diazanonane-1,9-dithiolate)Ni(Me)(2,6-dimesitylphenyl) is treated with 1 equiv of CO in the presence of excess 1,5-cyclooctadiene, the formation of Ni(N,N'-diethyl-3,7-diazanonane-1,9-dithiolate)Ni(CO)2 and Ni(CO)4 is considerably suppressed, and instead the dinuclear Ni(II)-Ni(0) complex is generated in situ. The results suggest that ACS catalysis could include the Nid(II)-Nip(0) state as the active species, that the Nid(II)-Nip(0) species could first react with methylcobalamin to afford Nid(II)-Nip(II)Me, and that CO insertion into the Nip-Me bond and the successive reductive elimination of acetyl-CoA occurs immediately when CoA is coordinated to the Nip site to form the active Nid(II)-Nip(0) species
additional information
-
Ti3+ NTAis utilized in the CO exchange assay
additional information
-
Cu is not required for enzyme activity
additional information
-
a nucleophilic metal center on enzyme is the active site which accepts the methyl group from the methylated corrinoid/iron-sulfur protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,10-phenanthroline
-
1 mM, complete inhibition. 1,10-Phenanthroline additionally has inhibitory effects on growth of Peptoclostridium difficile
2,2-dipyridyl
-
1 mM, complete inhibition. 2,2-Dipyridyl additionally has inhibitory effects on growth of Peptoclostridium difficile
5,5'dithiobis-(2-nitrobenzoic acid)
-
inhibits the acetyl-CoA/CO exchange reaction
CN-
-
inhibitor on the CoA/acetyl-CoA exchange, 98% inhibition at 1.2 mM
CO2
-
inhibitor on the CoA/acetyl-CoA exchange
CoA
-
at concentration above 10 mM, 50% inhibition of acetyl-CoA synthesis from methyl iodide at 15 mM
dephospho-CoA
-
inhibitor on the CoA/acetyl-CoA exchange, 75% inhibition at 0.44 mM
desulfo-CoA
-
inhibitor on the CoA/acetyl-CoA exchange, 30% mM at 2.1 mM
Dithionite
-
inhibits reverse methyl group transfer, when it is preincubated with methylated enzyme but not when it is preincubated with Co+-iron-sulfur protein
Fe2+
-
in cofactor ferredoxin(II), which harbors two [4Fe-4S] clusters
Mersalyl acid
-
inhibits the acetyl-CoA/CO exchange reaction
methyl iodide
-
inhibits the acetyl-CoA/CO exchange reaction
N2O
-
inhibitor on the CoA/acetyl-CoA exchange
Sodium dithionite
-
inhibits the acetyl-CoA/CO exchange reaction
Ti3+-citrate
-
inhibits reverse methyl group transfer, when it is preincubated with methylated enzyme but not when it is preincubated with Co+-iron-sulfur protein
additional information
-
no inhibition of the exchange reaction by methyl- and phenylglyoxal, and butanedione
-
CO
-
non-competitive inhibitor on the CoA/acetyl-CoA exchange, the Ni-Fe-C-center appears to be the inhibitor site for CO
CO
-
inhibits the methyl group transfer reaction and synthesis of acetyl-CoA
CO
-
the complete alpha2beta2 enzyme exhibits strong cooperative inhibition, isolated alpha is weakly inhibited, apparently by a single CO with Ki = 1.5 mM. Absence of strong cooperative inhibition of CO in mutant enzymes A265M and AA110C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.3.1.169 CO-methylating acetyl-CoA synthase
more
top
