Acetyl-CoA synthase

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{{STRUCTURE_1ru3| PDB=1ru3 | SIZE=400| SCENE= |right|CAPTION=Acetyl-CoA synthase with Fe4S4 center complex with glycerol and Ni+2 ion [[1ru3]].}}
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<StructureSection load='' size='350' side='right' scene='49/492892/Cv/8' caption='Acetyl-CoA synthase IV subunit α with Fe4S4 center complex with glycerol (stick model) and Ni+2 ions (green) [[1ru3]]'>
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__TOC__
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== Function ==
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'''Acetyl-CoA synthase''' (ACS) is a Fe-Ni-S containing enzyme found in archae and bacteria. ACS is divided to 4 classes:<br />
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Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
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* '''ACS-I''' catalyzes the synthesis of acetyl-CoA from CoA, CO2, methyl group and 2 electrons.<br />
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* '''ACS-I'''I catalyzes the reverse reaction. <br />
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to a Jmol applet. Check out the other buttons as well!
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* '''ACS-III''' uses pyruvate as the source of CO2 and 2 electrons to produce acetyl-CoA.<br />
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* '''ACS-IV''' catabolizes CO to CO2. <br />
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'''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).
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ACS can form a bifunctional entity with [[carbon monoxide dehydrogenase]] ('''CODH/ACS'''). CODH/ACS is part of the [[Wood-Ljungdahl pathway]] of [[Carbon Fixation|carbon fixation]] using CO and methyl group to produce acetyl-CoA.
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==3D structures of acetyl-CoA synthase==
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== Structural highlights ==
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'''CODH/ACS bifunctional entity'''
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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.
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*<scene name='49/492892/Cv/11'>Fe4S4 center and 2 Ni+2 ions form interactions with 6 cysteine residues</scene> in Acetyl-CoA synthase IV subunit α from ''Carboxydothermus hydrogenoformans'' ([[1ru3]]).<ref>PMID:14699043</ref> Water molecules shown as red spheres.
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[[1mjg]], [[1oao]], [[2z8y]], [[3i01]] – MtACS α+β + Fe4-Ni-S4 – ''Moorella thermoacetica''<br />
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==3D structures of acetyl-CoA synthase==
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[[3i04]] - MtACS α+β + CN + Fe4-Ni-S4<br />
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[[Acetyl-CoA synthase 3D structures]]
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[[3git]] - MtACS α + Fe4S4<br />
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[[3s2x]] - MtACS α C terminal + Ni<br />
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[[2h9a]] – ChACS γ + Fe4S4 - ''Carboxydothermus hydrogenoformans''<br />
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[[2ycl]] - ChACS γ + cobalamine + Fe4S4<br />
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'''ACS'''
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[[1ytl]] – ACS ε – ''Archaeoglobus fulgidus''<br />
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[[3cf4]] - ACS α+ε + CO + Fe3-Ni-S4 + Fe4S4 – ''Methanosarcina barkeri''
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'''ACS-IV'''
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[[1ru3]] - ChACS α + Fe4-Ni-S4
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</StructureSection>
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<b>References</b><br>
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<references/>
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[[Category: Topic Page]]

Current revision

Acetyl-CoA synthase IV subunit α with Fe4S4 center complex with glycerol (stick model) and Ni+2 ions (green) 1ru3

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References

  1. ↑ Svetlitchnyi V, Dobbek H, Meyer-Klaucke W, Meins T, Thiele B, Romer P, Huber R, Meyer O. A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans. Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):446-51. Epub 2003 Dec 29. PMID:14699043 doi:10.1073/pnas.0304262101

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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