Literature summary for 2.3.1.169 extracted from

Doukov, T.I.; Iverson, T.M.; Seravalli, J.; Ragsdale, S.W.; Drennan, C.L.
A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase (2002), Science, 298, 567-572.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop vapor diffusion at room temperature in a Coy anaerobic chamber, 0.005 ml of protein solution containing 40-60 mg/ml CODH/ACS in 50 mM Tris, pH 7.6, are mixed with 0.0075 ml of reservoir solution containing 8% polyethylene glycol MME 5000, 20% glycerol, 200 mM calcium acetate, 100 mM PIPES, pH 6.5, and 2 mM dithioerythritol, X-ray diffraction structure determination and analysis at 2.2 A resolution, multiwavelength anomalous dispersion techniques, molecular replacement	Moorella thermoacetica

Crystallization (Comment)

Organism

sitting drop vapor diffusion at room temperature in a Coy anaerobic chamber, 0.005 ml of protein solution containing 40-60 mg/ml CODH/ACS in 50 mM Tris, pH 7.6, are mixed with 0.0075 ml of reservoir solution containing 8% polyethylene glycol MME 5000, 20% glycerol, 200 mM calcium acetate, 100 mM PIPES, pH 6.5, and 2 mM dithioerythritol, X-ray diffraction structure determination and analysis at 2.2 A resolution, multiwavelength anomalous dispersion techniques, molecular replacement

Moorella thermoacetica

Metals/Ions

Metals/Ions	Comment	Organism
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	Moorella thermoacetica
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	Moorella thermoacetica
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	Moorella thermoacetica

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
310000	-	-	Moorella thermoacetica

Organism

Organism	UniProt	Comment	Textmining
Moorella thermoacetica	P27989	formerly Clostridium thermoaceticum	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	mechanism by which acetyl-CoA is assembled at the A-cluster and mechanism of CO2 reduction at the C-cluster, overview	Moorella thermoacetica	?	-	?

Subunits

Subunits	Comment	Organism
More	overall enzyme structure, channels, and protein-protein interactions, the beta domains are responsible for CO2/CO chemistry and contain the B-, C-, and D-clusters, detailed overview	Moorella thermoacetica
tetramer	alpha2beta2 heterotetramer, the beta2 domains form the center of the complex	Moorella thermoacetica

Synonyms

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

General Information

General Information	Comment	Organism
additional information	bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase, the different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit. The enzyme catalyzes two different reactions. The C-cluster in the CODH subunit generates CO from CO2, while the A-cluster of the ACS subunit combines the CO with CoA and a methyl group to form acetyl-CoA	Moorella thermoacetica
physiological function	CODH/ACS is used in the degradation of acetyl-CoA to form methane and CO2	Moorella thermoacetica