World Library  
Flag as Inappropriate
Email this Article

ATP citrate lyase

Article Id: WHEBN0008396468
Reproduction Date:

Title: ATP citrate lyase  
Author: World Heritage Encyclopedia
Language: English
Subject: Glycolysis, Acetyl-CoA, Fatty acid synthesis
Publisher: World Heritage Encyclopedia

ATP citrate lyase

ATP citrate lyase
Symbol ACLY
Entrez HUGO OMIM RefSeq UniProt EC number Locus q21.2

ATP citrate lyase is an enzyme that represents an important step in fatty acid biosynthesis.[2] This step in fatty acid biosynthesis occurs because ATP citrate lyase is the link between the metabolism of carbohydrates (which causes energy) and the production of fatty acids.[1]


ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer of apparently identical subunits. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis.[3] It is activated by insulin.[4] ATP-citrate lyase is also responsible for catalyzing the conversion of citrate and CoA into acetyl-CoA and oxaloacetate, along with the hydrolysis of ATP.[1]


In the presence of ATP and Coenzyme A, citrate lyase catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and orthophosphate:

citrate + ATP + CoA + H2O-->oxaloacetate + Acetyl-CoA + ADP + Pi.

This enzyme was formerly listed as EC[5]


The enzyme is cytosolic in plants[6] and animals.


The enzyme is composed of two subunits in green plants (including Chlorophyceae, Marchantimorpha, Bryopsida, Pinaceae, monocotyledons, and eudicots), species of fungi, Glaucophytes, Chlamydomonas, and prokaryotes.

Animal ACL enzymes are homomeric, presumably an evolutionary fusion of the ACLA and ACLB genes probably occurred early in the evolutionary history of this kingdom.[6]

A structure of human ATP citrate lyase was determined using X-ray diffraction to a resolution of 2.10 Å. The enzyme is composed of two polymer chains which are polypeptides. Chain A of the first polymer is 425 amino acids in length. Chain B of the second polymer is 334 amino acids in length.[1]


Further reading

External links

  • Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Ramachandran Plot of ATP Citrate Lyase

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Hawaii eBook Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.