Literature summary for 1.2.7.4 extracted from

Tan, X.; Kagiampakis, I.; Surovtsev, I.V.; Demeler, B.; Lindahl, P.A.
Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase (2007), Biochemistry, 46, 11606-11613.

Search for more literature for 1.2.7.4

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli strain JM109	Moorella thermoacetica

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	no oligomerization or activity in the presence of Co2+, Zn2+, and Cu2+, oligomerization but no exhibition of catalytic activity in the presence of Pd2+ and Pt2+	Moorella thermoacetica
Ni2+	contains Ni2+-activated alpha subunits, Ni2+ is required for activity and oligomerization	Moorella thermoacetica

Molecular Weight [Da]

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

Organism

Organism	UniProt	Comment	Textmining
Moorella thermoacetica	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CO + H2O + acceptor	-	Moorella thermoacetica	CO2 + reduced acceptor	-	?
CO + H2O + acceptor	-	Moorella thermoacetica	CO2 + reduced acceptor	-	r

Subunits

Subunits	Comment	Organism
tetramer	-	Moorella thermoacetica

Synonyms

Synonyms	Comment	Organism
acetyl-CoA synthase/carbon monoxide dehydrogenase	bifunctional enzyme	Moorella thermoacetica
ACS/CODH	bifunctional enzyme	Moorella thermoacetica
CODH	forms a complex with acetyl-CoA synthase	Moorella thermoacetica

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Release 2023.1 (January 2023)