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Literature summary extracted from

  • Bender, G.; Ragsdale, S.
    Evidence that ferredoxin interfaces with an internal redox shuttle in acetyl-CoA synthase during reductive activation and catalysis (2011), Biochemistry, 50, 276-286.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.169 additional information reductive activation of the enzyme by ferrdoxin, mechanism, detailed overview Moorella thermoacetica
6.2.1.1 reduced ferredoxin required Moorella thermoacetica

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.169 expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) from a pet29a(+) vector Moorella thermoacetica
6.2.1.1 expression of C-terminally His-tagged ACS in Escherichia coli strain BL21(DE3) Moorella thermoacetica

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.169 Cu2+
-
Moorella thermoacetica
2.3.1.169 Fe2+ in cofactor ferredoxin(II), which harbors two [4Fe-4S] clusters Moorella thermoacetica
2.3.1.169 Zn2+
-
Moorella thermoacetica

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.169 Ni2+ formation of the NiFeC species Moorella thermoacetica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.169 acetyl-CoA + corrinoid protein Moorella thermoacetica
-
CoA + CO + methylcorrinoid protein
-
?
6.2.1.1 ATP + acetate + CoA Moorella thermoacetica reaction of acetylated ACS with CoA and Fd-II, a step of the catalytic cycle in which the acetylated ACS reacts with CoA to form acetyl-CoA AMP + diphosphate + acetyl-CoA
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.169 Moorella thermoacetica
-
-
-
6.2.1.1 Moorella thermoacetica
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.169 recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography under a N2 atmosphere Moorella thermoacetica
6.2.1.1 recombinant C-terminally His-tagged ACS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography under anaerobic conditions Moorella thermoacetica

Reaction

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] 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 Moorella thermoacetica

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.3.1.169 purified recombinant ACS is Ni-reconstituted in the elution buffer with 6 equivalents of NiCl2 for 2 or 3 days at 27°C or at 45°C Moorella thermoacetica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.169 acetyl-CoA + corrinoid protein
-
Moorella thermoacetica CoA + CO + methylcorrinoid protein
-
?
2.3.1.169 acetyl-CoA + corrinoid 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 Moorella thermoacetica CoA + CO + methylcorrinoid protein
-
?
6.2.1.1 ATP + acetate + CoA
-
Moorella thermoacetica AMP + diphosphate + acetyl-CoA
-
?
6.2.1.1 ATP + acetate + CoA reaction of acetylated ACS with CoA and Fd-II, a step of the catalytic cycle in which the acetylated ACS reacts with CoA to form acetyl-CoA Moorella thermoacetica AMP + diphosphate + acetyl-CoA
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.169 heterotetramer CODH and ACS make up the two subunits of a 310 kDa alpha2beta2 heterotetrameric enzymatic complex Moorella thermoacetica

Synonyms

EC Number Synonyms Comment Organism
6.2.1.1 Acetyl-CoA synthase
-
Moorella thermoacetica
6.2.1.1 ACS
-
Moorella thermoacetica
6.2.1.1 More acetyl-CoA synthase is a subunit of the bifunctional CO dehydrogenase/acetyl-CoA synthase, CODH/ACS, complex Moorella thermoacetica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.169 22
-
acetyl-CoA exchange assay at room temperature Moorella thermoacetica
2.3.1.169 45
-
methylation reaction assay at Moorella thermoacetica
6.2.1.1 27
-
CO/acetyl-CoA exchange assay at Moorella thermoacetica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.169 6.2
-
acetyl-CoA exchange assay at Moorella thermoacetica
2.3.1.169 7.6
-
methylation reaction assay at Moorella thermoacetica
6.2.1.1 6.2
-
CO/acetyl-CoA exchange assay at Moorella thermoacetica

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.169 acetyl-CoA
-
Moorella thermoacetica
2.3.1.169 Ferredoxin Fd-II, which harbors two [4Fe-4S] clusters and is an electron acceptor for CODH, serves as a redox activator of ACS. Catalytic one-electron redox-active species in the CO/acetyl-CoA exchange reaction. Incubation of ACS with Fd-II and CO leads to the formation of the NiFeC species. FdII is purified from Moorella thermoacetica, overview Moorella thermoacetica

General Information

EC Number General Information Comment Organism
2.3.1.169 physiological function acetyl-CoA synthase, ACS, a subunit of the bifunctional CO dehydrogenase/acetyl-CoA synthase, CODH/ACS, complex of Moorella thermoacetica requires reductive activation in order to catalyze acetyl-CoA synthesis and related partial reactions, including the CO/acetyl-CoA exchange reaction Moorella thermoacetica
6.2.1.1 metabolism acetyl-CoA synthase, a subunit of the bifunctional CO dehydrogenase/acetyl-CoA synthase, CODH/ACS, complex of Moorella thermoacetica requires reductive activation in order to catalyze acetyl-CoA synthesis and related partial reactions, including the CO/acetyl-CoA exchange reaction. Ferredoxin(II), which harbors two [4Fe-4S] clusters and is an electron acceptor for CODH, serves as a redox activator of ACS. Ferredoxin interfaces with an internal redox shuttle in acetyl-CoA synthase during reductive activation and catalysis. The midpoint reduction potential for the catalytic one-electron redoxactive species in the CO/acetyl-CoAexchange reaction is -511 mV. Incubation of ACS with Fd-II and CO leads to the formation of the NiFeC species. Mechanism, overview Moorella thermoacetica