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Acetyl-CoA acetyltransferase 2
PDB 1wl4 EBI.png
PDB rendering based on 1wl4.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbol ACAT2
External IDs OMIM100678 MGI109182 HomoloGene55855 ChEMBL: 2240 GeneCards: ACAT2 Gene
EC number
Species Human Mouse
Entrez 39 110460
Ensembl ENSG00000120437 ENSMUSG00000023832
UniProt Q9BWD1 Q8CAY6
RefSeq (mRNA) NM_005891 NM_009338.3
RefSeq (protein) NP_005882 NP_033364.2
Location (UCSC) Chr 6:
160.18 – 160.2 Mb
Chr 17:
13.14 – 13.15 Mb
PubMed search [1] [2]

Acetyl-CoA acetyltransferase, cytosolic, also known as cytosolic acetoacetyl-CoA thiolase, is an enzyme that in humans is encoded by the ACAT2 (acetyl-Coenzyme A acetyltransferase 2) gene[1][2] that is responsible for the synthesis of cholesteryl esters which are part of lipoproteins containing apoB.

Acetyl-Coenzyme A acetyltransferase 2 is an acetyl-CoA C-acetyltransferase enzyme.


This gene shows complementary overlapping with the 3-prime region of the TCP1 gene in both mouse and human. These genes are encoded on opposite strands of DNA, as well as in opposite transcriptional orientation.[1]


The product of this gene is an enzyme involved in lipid metabolism, and it encodes cytosolic acetoacetyl-CoA thiolase.[1]

In a study done on rats, it was found that rats fed a fat-enriched diet whose ACAT2 gene were deleted were protected from dietary fat-induced atherosclerosis. LDL concentration, CE composition, and particle size were affected in ways that reduced atherogenesis in comparison to other rats whose ACAT2 gene were not modified.[3]


  1. ^ a b c "Entrez Gene: acetyl-Coenzyme A acetyltransferase 2". 
  2. ^ Morel Y, Bristow J, Gitelman SE, Miller WL (September 1989). "Transcript encoded on the opposite strand of the human steroid 21-hydroxylase/complement component C4 gene locus". Proc. Natl. Acad. Sci. U.S.A. 86 (17): 6582–6. doi:10.1073/pnas.86.17.6582. PMC 297888. PMID 2475872. 
  3. ^ Bell III T, Kelley K, Wilson M, et al. (2007). "Dietary Fat–Induced Alterations in Atherosclerosis Are Abolished by ACAT2-Deficiency in ApoB100 Only, LDLr–/– Mice.". Arteriosclerosis, Thrombosis, and Vascular Biology. 27: 89. doi:10.1161/ATVBAHA.107.142802. 

Further reading[edit]

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