Acetyl-CoA synthase
From Proteopedia
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-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. ACS can form a bifunctional entity with carbon monoxide dehydrogenase (CODH).
3D structures of acetyl-CoA synthase
CODH/ACS bifunctional entity
1mjg, 1oao, 2z8y, 3i01 – MtACS α+β + Fe4-Ni-S4 – Moorella thermoacetica
3i04 - MtACS α+β + CN + Fe4-Ni-S4
3git - MtACS α + Fe4S4
3s2x - MtACS α C terminal + Ni
2h9a – ChACS γ + Fe4S4 - Carboxydothermus hydrogenoformans
2ycl - ChACS γ + cobalamine + Fe4S4
ACS
1ytl – ACS ε – Archaeoglobus fulgidus
3cf4 - ACS α+ε + CO + Fe3-Ni-S4 + Fe4S4 – Methanosarcina barkeri
ACS-IV
1ru3 - ChACS α + Fe4-Ni-S4
