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ATP-citrate synthase
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| - | + | <StructureSection load='3pff' size='350' side='right' scene='47/477091/Cv/1' caption='ATP-citrate synthase complex with ADP (stick model), tartrate and Mg+2 ions (green), [[3pff]]'> | |
| - | + | == Function == | |
| - | + | '''ATP-citrate synthase''' (ACS) or '''ATP citrate lyase''' or '''citryl-CoA synthetase''' is part of the citrate cycle. It catalyzes the transformation of ADP, acetyl-CoA and oxaloacetate to ATP, citrate and CoA. ACS is the link between energy metabolism from carbohydrates to the production of fatty acids. | |
| - | + | See also [[Citrate Synthase]]<br /> | |
| + | [[Citric acid cycle intermediates serve as substrates for biosynthetic processes]]<br /> | ||
| + | [[Reverse Krebs cycle]]. | ||
| - | + | == Structural highlights == | |
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| + | Crystal structures have shown that tartrate and citrate bind to ACS in the same binding site. <scene name='47/477091/Cv/4'>Binding site of tartrate</scene> of ATP-citrate synthase. Water molecules are shown as red spheres. <scene name='47/477091/Cv/6'>Binding site of ADP and Mg+2 ions</scene>, [[3pff]]. <ref>PMID:22102020</ref> | ||
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| + | == 3D Structures of ATP-citrate synthase == | ||
| + | [[ATP-citrate synthase 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | + | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Sun T, Hayakawa K, Fraser ME. ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1168-72., Epub 2011 Sep 24. PMID:22102020 doi:10.1107/S1744309111028363
