Acetyl-CoA synthase

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{{STRUCTURE_1ru3| PDB=1ru3 | SIZE=400| SCENE= |right|CAPTION=Acetyl-CoA synthase IV with Fe4S4 center complex with glycerol and Ni+2 ions (green) [[1ru3]].}}
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{{STRUCTURE_1ru3| PDB=1ru3 | SIZE=350| SCENE= |right|CAPTION=Acetyl-CoA synthase IV with Fe4S4 center complex with glycerol and Ni+2 ions (green) [[1ru3]].}}
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Revision as of 11:24, 30 November 2015

Template:STRUCTURE 1ru3


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 Woods-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.

3D structures of acetyl-CoA synthase

Updated on 30-November-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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