ATP-citrate synthase: Difference between revisions
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
[[3mwd]] – hACS + citrate – human<br /> | [[3mwd]], [[5tde]] – hACS + citrate – human<br /> | ||
[[5tdf]], [[5tet]] – hACS + citrate derivative<br /> | |||
[[5teq]] – hACS N-terminal (mutant) + citrate <br /> | |||
[[5te1]] – hACS N-terminal (mutant) + citrate derivative<br /> | |||
[[5tes]] – hACS + citrate + ADP<br /> | |||
[[5tdm]] – hACS + citrate derivative + ADP<br /> | |||
[[3mwe]] – hACS + tartrate<br /> | [[3mwe]] – hACS + tartrate<br /> | ||
[[3pff]] - hACS + tartrate + ADP | [[3pff]], [[5tdz]] - hACS + tartrate + ADP<br /> | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Revision as of 15:07, 22 March 2018
FunctionATP-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. See also Citrate Synthase Structural highlightsCrystal structures have shown that tartrate and citrate bind to ACS in the same binding site. of ATP-citrate synthase. , 3pff. [1]
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3D Structures of ATP-citrate synthase3D Structures of ATP-citrate synthase
Updated on 22-March-2018
3mwd, 5tde – hACS + citrate – human
5tdf, 5tet – hACS + citrate derivative
5teq – hACS N-terminal (mutant) + citrate
5te1 – hACS N-terminal (mutant) + citrate derivative
5tes – hACS + citrate + ADP
5tdm – hACS + citrate derivative + ADP
3mwe – hACS + tartrate
3pff, 5tdz - hACS + tartrate + ADP
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