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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.7.4 expressed in Escherichia coli Moorella thermoacetica

Protein Variants

EC Number Protein Variants Comment Organism
1.2.7.4 A110C alpha subunit mutant enzyme showing electron paramagnetic resonance spectrum after Ni-activation Moorella thermoacetica
1.2.7.4 A222L alpha subunit mutant enzyme showing electron paramagnetic resonance spectrum after Ni-activation Moorella thermoacetica
2.3.1.169 A110C mutant designed to block the CO-migrating tunnel in the alpha-subunit. Electron paramagnetic resonance spectra indicates that the A-cluster is properly assembled. ACS activity is similar to that of the wild-type recombinant Ni-activated alpha-subunit Moorella thermoacetica
2.3.1.169 A222L mutant designed to block the CO-migrating tunnel in the alpha-subunit. Electron paramagnetic resonance spectra indicates that the A-cluster is properly assembled. ACS activity is similar to that of the wild-type recombinant Ni-activated alpha-subunit Moorella thermoacetica
6.2.1.1 A110C site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme Moorella thermoacetica
6.2.1.1 A222L site-directed mutagenesis, alpha-subunit mutant, which does not show cooperative CO inhibition in contrast to the wild-type enzyme Moorella thermoacetica
6.2.1.1 A265M site-directed mutagenesis, alpha-subunit mutant, the recombinantly expressed mutant enzymes cannot be purified Moorella thermoacetica

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.1 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

EC Number Metals/Ions Comment Organism Structure
1.2.7.4 Ni2+ activates Moorella thermoacetica
2.3.1.169 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 Moorella thermoacetica
2.3.1.169 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 Moorella thermoacetica
6.2.1.1 Fe2+ the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, bifunctional Ni-Fe-S containing ACS/CODH Moorella thermoacetica
6.2.1.1 Mg2+
-
Moorella thermoacetica
6.2.1.1 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)

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

Organism

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

Oxidation Stability

EC Number Oxidation Stability Organism
6.2.1.1 the enzyme is O2-sensitive Moorella thermoacetica

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.7.4
-
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] CO migrates to the A-cluster through two pathways, one involving and one not involving the tunnel Moorella thermoacetica

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.2.1.1 7.4
-
Ni-activated A110C mutant alpha subunit at 1 atm CO Moorella thermoacetica
6.2.1.1 8.1
-
Ni-activated A222L mutant alpha subunit at 1 atm CO Moorella thermoacetica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.4 CO + H2O + acceptor
-
Moorella thermoacetica CO2 + reduced acceptor
-
?
6.2.1.1 ATP + acetate + CoA
-
Moorella thermoacetica AMP + diphosphate + acetyl-CoA
-
?
6.2.1.1 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
-
?
6.2.1.1 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

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

Synonyms

EC Number Synonyms Comment Organism
1.2.7.4 acetyl coenzyme A synthase/carbon monoxide dehydrogenase
-
Moorella thermoacetica
1.2.7.4 ACS/CODH
-
Moorella thermoacetica
1.2.7.4 CODH beta subunit of the bifunctional acetyl coenzyme A synthase/carbon monoxide dehydrogenase complex Moorella thermoacetica
6.2.1.1 acetyl coenzyme A synthase/carbon monoxide dehydrogenase
-
Moorella thermoacetica
6.2.1.1 ACS/CODH
-
Moorella thermoacetica

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.7.4 Ni-Fe-4S center active site called the C-cluster Moorella thermoacetica
6.2.1.1 ATP
-
Moorella thermoacetica