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Literature summary for 2.3.1.169 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
Search for more literature for 2.3.1.169

Activating Compound

Activating Compound Comment Organism Structure
additional information reductive activation of the enzyme by ferrdoxin, mechanism, detailed overview Moorella thermoacetica

Cloned(Commentary)

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

Inhibitors

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + corrinoid protein Moorella thermoacetica
-
 CoA + CO + methylcorrinoid protein
-
 ?

Organism

Organism UniProt Comment Textmining
Moorella thermoacetica
-
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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
a

Renatured (Commentary)

Renatured (Comment) Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + corrinoid protein
-
 Moorella thermoacetica CoA + CO + methylcorrinoid protein
-
 ?
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
-
 ?

Subunits

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 acetyl-CoA exchange assay at room temperature Moorella thermoacetica
45
-
 methylation reaction assay at Moorella thermoacetica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
 acetyl-CoA exchange assay at Moorella thermoacetica
7.6
-
 methylation reaction assay at Moorella thermoacetica

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Moorella thermoacetica
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

General Information Comment Organism
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