Acetyl-CoA synthase

Function Acetyl-CoA synthase (ACS) is a Fe-Ni-S containing enzyme found in archae and bacteria. ACS is divided to 4 classes: ACS-I catalyzes the synthesis of acetyl-CoA from CoA, CO2, methyl group and 2 electrons. ACS-II catalyzes the reverse reaction. ACS-III uses pyruvate as the source of CO2 and 2 electrons to produce acetyl-CoA. ACS-IV catabolizes CO to CO2. ACS can form a bifunctional entity with carbon monoxide dehydrogenase (CODH/ACS). CODH/ACS is part of the Wood-Ljungdahl pathway of carbon fixation using CO and methyl group to produce acetyl-CoA. Structural highlights ACS-I and ACS-II contain 5 subunits: α, β, γ, δ, ε. ACS-III is composed of 2 proteins: 2α+2β and γ+δ. ACS-IV is composed of α monomer. in Acetyl-CoA synthase IV subunit α from Carboxydothermus hydrogenoformans (1ru3). Water molecules shown as red spheres. 3D structures of acetyl-CoA synthase Acetyl-CoA synthase 3D structures

spinqualitylabelsall models Acetyl-CoA synthase IV subunit α with Fe4S4 center complex with glycerol (stick model) and Ni+2 ions (green) 1ru3 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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