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Frontiers in Biology

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ISSN 1674-7992(Online)

CN 11-5892/Q

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Front Biol Chin    2009, Vol. 4 Issue (2) : 129-136    https://doi.org/10.1007/s11515-008-0096-9
REVIEW
Acyl-coenzyme A: cholesterol acyltransferase family
Yali LIU, Zhanyun GUO()
Institute of Protein Research, College of Life Science and Technology, Tongji University, Shanghai 200092, China
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Abstract

The enzymes of the acyl-coenzyme A: cholesterol acyltransferase (ACAT) family are responsible for the in vivo synthesis of neutral lipids. They are potential drug targets for the intervention of atherosclerosis, hyperlipidemia, obesity, type II diabetes and even Alzheimer’s disease. ACAT family enzymes are integral endoplasmic reticulum (ER) membrane proteins and can be divided into ACAT branch and acyl-coenzyme A: diacylglycerol acyltransferase 1 (DGAT1) branch according to their substrate specificity. The ACAT branch catalyzes synthesis of cholesteryl esters using long-chain fatty acyl-coenzyme A and cholesterol as substrates, while the DGAT1 branch catalyzes synthesis of triacylglycerols using fatty acyl-coenzyme A and diacylglycerol as substrates. In this review, we mainly focus on the recent progress in the structural research of ACAT family enzymes, including their disulfide linkage, membrane topology, subunit interaction and catalysis mechanism.
Keywords lipid      acyl-coenzyme A: cholesterol acyltransferase (ACAT)      acyl-coenzyme A: diacylglycerol acyltransferase 1 (DGAT1)      acyltransferase      catalysis     
Corresponding Author(s): GUO Zhanyun,Email:zhan-yun.guo@mail.tongji.edu.cn   
Issue Date: 05 June 2009
 Cite this article:   
Yali LIU,Zhanyun GUO. Acyl-coenzyme A: cholesterol acyltransferase family[J]. Front Biol Chin, 2009, 4(2): 129-136.
 URL:  
https://academic.hep.com.cn/fib/EN/10.1007/s11515-008-0096-9
https://academic.hep.com.cn/fib/EN/Y2009/V4/I2/129
Fig.1  Amino acid sequence alignment of human ACAT1, human ACAT2, and human DGAT1. The possible transmembrane domains (TMDs) are shaded. The conserved residues are shown in red, and the cysteine residues are shown in blue.
Fig.2  A general ER membrane topology model for ACAT family enzymes. The possible cholesterol/diacyglycerol-binding region (TMD7) is shown in red, and other TMDs are shown in blue. The possible acyl-coenzyme A-binding regions (the loop between TMD6 and TMD7 and the loop between TMD4 and TMD5) are shown in green. The position of the active site His in TMD7 is indicated by a white star.
Fig.3  Structure of ACAT family enzymes. A: two distinct functional sides of TMD7 of ACAT1. Residues critical for enzyme activity are shown in red; residues involved in subunit interaction are shown in blue. B: A proposed tunnel model for ACAT family enzymes. The TMDs form a tunnel structure in the center. Only TMD7 and TMD8 are shown. Other TMDs, the N-terminal domain and the loops are omitted.
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