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ATP citrate lyase
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| Identifiers | |
| Symbol | ACLY |
| Entrez | 47 |
| HUGO | 115 |
| OMIM | 108728 |
| RefSeq | NM_001096 |
| UniProt | P53396 |
| Other data | |
| EC number | 2.3.3.8 |
| Locus | Chr. 17 q21.2 |
ATP citrate lyase is an enzyme that represents an important step in fatty acid biosynthesis.[1]
Contents |
Function
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.[2] It is activated in by insulin.[3]
Reaction
In the presence of ATP and Coenzyme A, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and orthophosphate:
- citrate + ATP + CoA-->oxaloacetate + Acetyl-CoA + ADP + Pi.
This enzyme was formerly listed as EC 4.1.3.8.[4]
Location
The enzyme is cytosolic in plants[5] and animals.
Structure
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.[5]
References
- ^ Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS (March 1992). "Cloning and expression of a human ATP-citrate lyase cDNA". Eur. J. Biochem. 204 (2): 491–9. doi:. PMID 1371749. http://www.blackwell-synergy.com/openurl?genre=article&sid=nlm:pubmed&issn=0014-2956&date=1992&volume=204&issue=2&spage=491.
- ^ "Entrez Gene: ATP citrate lyase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=47.
- ^ Guay C, Madiraju SR, Aumais A, Joly E, Prentki M (December 2007). "A role for ATP-citrate lyase, malic enzyme, and pyruvate/citrate cycling in glucose-induced insulin secretion". J. Biol. Chem. 282 (49): 35657–65. doi:. PMID 17928289.
- ^ MeSH ATP+Citrate+Lyase
- ^ a b Fatland BL, Ke J, Anderson MD, Mentzen WI, Cui LW, Allred CC, Johnston JL, Nikolau BJ, Wurtele ES (October 2002). "Molecular characterization of a heteromeric ATP-citrate lyase that generates cytosolic acetyl-coenzyme A in Arabidopsis". Plant Physiol. 130 (2): 740–56. doi:. PMID 12376641.
External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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