2.3.1.169: CO-methylating acetyl-CoA synthase
This is an abbreviated version!
For detailed information about CO-methylating acetyl-CoA synthase, go to the full flat file.
Word Map on EC 2.3.1.169
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2.3.1.169
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methanosarcina
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thermophila
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acetylthiocholine
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methyl-coenzyme
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methanogenesis
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butyrylthiocholine
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busch
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base-off
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propionylthiocholine
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nickel-containing
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moorella
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azinphos-methyl
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acetivorans
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2-naphthyl
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thermoacetica
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bioorganometallic
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five-subunit
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methylcobalamin
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acetate-grown
- 2.3.1.169
- methanosarcina
- thermophila
- acetylthiocholine
-
methyl-coenzyme
-
methanogenesis
- butyrylthiocholine
-
busch
-
base-off
- propionylthiocholine
-
nickel-containing
-
moorella
- azinphos-methyl
- acetivorans
-
2-naphthyl
- thermoacetica
-
bioorganometallic
-
five-subunit
- methylcobalamin
-
acetate-grown
Reaction
Synonyms
ACDS multienzyme complex, acetyl-CoA decarbonylase/synthase multienzyme complex, acetyl-CoA decarboxylase/synthase, Acetyl-CoA synthase, Acetyl-coenzyme A synthase, acetyl-coenzyme A synthase/carbon monoxide dehydrogenase, ACS/CODH, ACSCh, Carbon monoxide dehydrogenase, carbon monoxide dehydrogenase-corrinoid enzyme complex, carbon monoxide dehydrogenase/acetyl coenzyme A synthase, carbon monoxide dehydrogenase/acetyl-CoA synthase, carbon monoxide dehydrogenase/acetyl-coenzyme A synthase, CDH1, Cdh2, CO dehydrogenase, CO dehydrogenase enzyme complex, CO dehydrogenase/acetyl CoA synthase, CO dehydrogenase/acetyl coenzyme A synthase, CO dehydrogenase/acetyl-CoA synthase, CODH, CODH/ACS, CODH/ASC, KSU1_D0226, KSU1_D0227, monoxide dehydrogenase/acetyl-CoA synthase, multienzyme carbon monoxide dehydrogenase complex, multienzyme CO dehydrogenase/acetyl-CoA synthase complex
ECTree
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Metals Ions on EC 2.3.1.169 - CO-methylating acetyl-CoA synthase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CO
copper
Cu
-
the Ni in cluster A can be replaced by Cu yielding an inactive form of the acetyl-CoA synthase
Cu+
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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
Fe
Fe2+
Iron
Ni
Ni2+
Nickel
Zn
-
the Ni in cluster A can be replaced by Zn yielding an inactive form of the acetyl-CoA synthase
Zn2+
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capture of Ni2+, Cu+ and Zn2+ by thiolate sulfurs of an N2S2Ni complex
additional information
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
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a cobalt-containing Co/Fe-S component of multienzyme complex serves as a methyl carrier in the pathway of methane synthesis from acetate
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
-
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
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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+
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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
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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
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the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site
Iron
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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
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
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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
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Ti3+ NTAis utilized in the CO exchange assay
additional information
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a nucleophilic metal center on enzyme is the active site which accepts the methyl group from the methylated corrinoid/iron-sulfur protein
