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Literature summary for 6.2.1.1 extracted from

  • Tan, X.; Lindahl, P.A.
    Tunnel mutagenesis and Ni-dependent reduction and methylation of the alpha subunit of acetyl coenzyme A synthase/carbon monoxide dehydrogenase (2008), J. Biol. Inorg. Chem., 13, 771-778.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A110C site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme Moorella thermoacetica
A222L site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme Moorella thermoacetica
A265M site-directed mutagenesis, alpha-subunit mutant, the recombinantly expressed mutant enzymes cannot be purified Moorella thermoacetica

Inhibitors

Inhibitors Comment Organism Structure
CO CO inhibits acetyl-CoA synthesis quite strongly and in a cooperative manner Moorella thermoacetica
O2 the enzyme is O2-sensitive Moorella thermoacetica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics and extent of reduction of the Fe4S4 cubane in the apo-alpha subunit and the Ni-activated a subunit upon exposure to titanium(III) citrate, detailed overview Moorella thermoacetica

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, bifunctional Ni-Fe-S containing ACS/CODH Moorella thermoacetica
Mg2+
-
Moorella thermoacetica
Ni2+ activates, the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, bifunctional Ni-Fe-S containing ACS/CODH. Upon incubation in NiCl2, the complete A-cluster assembles, and the isolated a subunit develops approximately 10% of the maximal catalytic activity relative to that of the alpha2beta2 tetramer Moorella thermoacetica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + acetate + CoA Moorella thermoacetica
-
AMP + diphosphate + acetyl-CoA
-
?

Organism

Organism UniProt Comment Textmining
Moorella thermoacetica
-
-
-

Oxidation Stability

Oxidation Stability Organism
the enzyme is O2-sensitive Moorella thermoacetica

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.4
-
Ni-activated A110C mutant alpha subunit at 1 atm CO Moorella thermoacetica
8.1
-
Ni-activated A222L mutant alpha subunit at 1 atm CO Moorella thermoacetica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetate + CoA
-
Moorella thermoacetica AMP + diphosphate + acetyl-CoA
-
?
ATP + acetate + CoA the ACS reaction is catalyzed at the alpha-subunit A-cluster, an [Fe4S4] cubane bridged to a dinickel [NipNid] subcomponent, overview Moorella thermoacetica AMP + diphosphate + acetyl-CoA
-
?
additional information bifunctional Ni-Fe-S containing ACS/CODH, although alpha and beta subunits catalyze separate reactions, they interact functionally when CO2 is used as a substrate in the synthesis of acetyl-CoA Moorella thermoacetica ?
-
?

Subunits

Subunits Comment Organism
More the beta2 subunits are solely responsible for catalyzing the CODH reaction Moorella thermoacetica
tetramer acetyl-coenzyme A synthase/carbon monoxide dehydrogenase is an alpha2beta2 tetramer, alpha-subunit structure, overview Moorella thermoacetica

Synonyms

Synonyms Comment Organism
acetyl coenzyme A synthase/carbon monoxide dehydrogenase
-
Moorella thermoacetica
ACS/CODH
-
Moorella thermoacetica

Cofactor

Cofactor Comment Organism Structure
ATP
-
Moorella thermoacetica