ATP citrate lyase

protein
Name=ATP citrate lyase
caption=


width=
HGNCid=115
Symbol=ACLY
AltSymbols=
EntrezGene=47
OMIM=108728
RefSeq=NM_001096
UniProt=P53396
PDB=
ECnumber=2.3.3.8
Chromosome=17
Arm=q
Band=21.2
LocusSupplementaryData=

ATP citrate lyase is an enzyme that represents an important step in fatty acid biosynthesis.cite journal | author = Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS | title = Cloning and expression of a human ATP-citrate lyase cDNA | journal = Eur. J. Biochem. | volume = 204 | issue = 2 | pages = 491–9 | year = 1992 | month = March | pmid = 1371749 | doi = | url = http://www.blackwell-synergy.com/openurl?genre=article&sid=nlm:pubmed&issn=0014-2956&date=1992&volume=204&issue=2&spage=491 | issn = ]

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.cite web | title = Entrez Gene: ATP citrate lyase | url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=47 | accessdate = ] It is activated in by insulin.cite journal | author = Guay C, Madiraju SR, Aumais A, Joly E, Prentki M | title = A role for ATP-citrate lyase, malic enzyme, and pyruvate/citrate cycling in glucose-induced insulin secretion | journal = J. Biol. Chem. | volume = 282 | issue = 49 | pages = 35657–65 | year = 2007 | month = December | pmid = 17928289 | doi = 10.1074/jbc.M707294200 | url = | issn = ]

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. [MeshName|ATP+Citrate+Lyase]

Location

The enzyme is cytosolic in plantscite journal | author = Fatland BL, Ke J, Anderson MD, Mentzen WI, Cui LW, Allred CC, Johnston JL, Nikolau BJ, Wurtele ES | title = Molecular characterization of a heteromeric ATP-citrate lyase that generates cytosolic acetyl-coenzyme A in Arabidopsis | journal = Plant Physiol. | volume = 130 | issue = 2 | pages = 740–56 | year = 2002 | month = October | pmid = 12376641 | pmc = 166603 | doi = 10.1104/pp.008110 | url = | issn = ] and animals.

tructure

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.

References

External links

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