Literature summary for 2.3.1.169 extracted from

Kung, Y.; Doukov, T.I.; Seravalli, J.; Ragsdale, S.W.; Drennan, C.L.
Crystallographic snapshots of cyanide- and water-bound C-clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase (2009), Biochemistry, 48, 7432-7440.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of the 310 kDa bifunctional CODH/acetyl-CoA synthase complex bound both with a substrate H2O/OH- molecule and with a cyanide inhibitor. Both in native crystals and identical crystals soaked in a solution containing potassium cyanide, the substrateH2O/OH- molecule exhibits binding to the unique Fe site of the C-cluster. Cyanide binding is also observed in a bent conformation to Ni of the C-cluster, adjacent the substrate H2O/OH-molecule. The bridging sulfide is not present in either structure. Findings do not support a fifth, bridging sulfide playing a catalytic role in the enzyme mechanism	Moorella thermoacetica

Crystallization (Comment)

Organism

structures of the 310 kDa bifunctional CODH/acetyl-CoA synthase complex bound both with a substrate H2O/OH- molecule and with a cyanide inhibitor. Both in native crystals and identical crystals soaked in a solution containing potassium cyanide, the substrateH2O/OH- molecule exhibits binding to the unique Fe site of the C-cluster. Cyanide binding is also observed in a bent conformation to Ni of the C-cluster, adjacent the substrate H2O/OH-molecule. The bridging sulfide is not present in either structure. Findings do not support a fifth, bridging sulfide playing a catalytic role in the enzyme mechanism

Moorella thermoacetica

Organism

Organism	UniProt	Comment	Textmining
Moorella thermoacetica	-	bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase	-

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Release 2023.1 (January 2023)