ATP-citrate synthase: Difference between revisions
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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 == | == Function == | ||
'''ATP-citrate synthase''' (ACS) 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. | '''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]] | See also [[Citrate Synthase]]<br /> | ||
[[Citric acid cycle intermediates serve as substrates for biosynthetic processes]]<br /> | |||
[[Reverse Krebs cycle]]. | |||
== Structural highlights == | |||
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> | |||
== 3D Structures of ATP-citrate synthase == | == 3D Structures of ATP-citrate synthase == | ||
[[ATP-citrate synthase 3D structures]] | |||
</StructureSection> | |||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 12:45, 21 January 2024
FunctionATP-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 Citric acid cycle intermediates serve as substrates for biosynthetic processes Structural highlightsCrystal structures have shown that tartrate and citrate bind to ACS in the same binding site. of ATP-citrate synthase. Water molecules are shown as red spheres. , 3pff. [1] 3D Structures of ATP-citrate synthaseATP-citrate synthase 3D structures
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ReferencesReferences
- ↑ 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