Topic
Acyl-CoA
About: Acyl-CoA is a research topic. Over the lifetime, 527 publications have been published within this topic receiving 25134 citations. The topic is also known as: Acyl Coenzyme A.
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01 Jan 1998
TL;DR: An expressed sequence tag clone that shared regions of similarity with acyl CoA:cholesterol acyltransferase, an enzyme that also uses fatty acyl coA as a substrate was identified, which will greatly facilitate studies of cellular glycerolipid metabolism and its regulation.
Abstract: Triacylglycerols are quantitatively the most important storage form of energy for eukaryotic cells. Acyl CoA:diacylglycerol acyltransferase (DGAT, EC 2.3.1.20) cat- alyzes the terminal and only committed step in triacylglycerol synthesis, by using diacylglycerol and fatty acyl CoA as substrates. DGAT plays a fundamental role in the metabolism of cellular diacylglycerol and is important in higher eu- karyotes for physiologic processes involving triacylglycerol metabolism such as intestinal fat absorption, lipoprotein assembly, adipose tissue formation, and lactation. DGAT is an integral membrane protein that has never been purified to homogeneity, nor has its gene been cloned. We identified an expressed sequence tag clone that shared regions of similarity with acyl CoA:cholesterol acyltransferase, an enzyme that also uses fatty acyl CoA as a substrate. Expression of a mouse cDNA for this expressed sequence tag in insect cells resulted in high levels of DGAT activity in cell membranes. No other acyltransferase activity was detected when a variety of sub- strates, including cholesterol, were used as acyl acceptors. The gene was expressed in all tissues examined; during differen- tiation of NIH 3T3-L1 cells into adipocytes, its expression increased markedly in parallel with increases in DGAT activ- ity. The identification of this cDNA encoding a DGAT will greatly facilitate studies of cellular glycerolipid metabolism and its regulation.
2 citations
TL;DR: Generally, arachidonic, linoleic and eicosapentaenoic acids were better substrates for the acyl-CoA:1-acyl-lysophospholipid acyltransferases than oleic, docosahexaenoic and palmitic acids.
2 citations
TL;DR: The discovery highlights the functional diversity of DGAT2-like proteins and provides valuable information on steryl ester and Squalene synthesis in thraustochytrids, paving the way to enhance squalene production through metabolic engineering.
Abstract: Thraustochytrids are heterotrophic marine eukaryotes known to accumulate large amounts of triacylglycerols, and they also synthesize terpenoids like carotenoids and squalene, which all have an increasing market demand. However, a more extensive knowledge of the lipid metabolism is needed to develop thraustochytrids for profitable biomanufacturing. In this study, two putative type-2 Acyl-CoA:diacylglycerol acyltransferases (DGAT2) genes of Aurantiochytrium sp. T66, T66ASATa, and T66ASATb, and their homologs in Aurantiochytrium limacinum SR21, AlASATa and AlASATb, were characterized. In A. limacinum SR21, genomic knockout of AlASATb reduced the amount of the steryl esters of palmitic acid, SE (16:0), and docosahexaenoic acid, SE (22:6). The double mutant of AlASATa and AlASATb produced even less of these steryl esters. The expression and overexpression of T66ASATb and AlASATb, respectively, enhanced SE (16:0) and SE (22:6) production more significantly than those of T66ASATa and AlASATa. In contrast, these mutations did not significantly change the level of triacylglycerols or other lipid classes. The results suggest that the four genes encoded proteins possessing acyl-CoA:sterol acyltransferase (ASAT) activity synthesizing both SE (16:0) and SE (22:6), but with the contribution from AlASATb and T66ASATb being more important than that of AlASATa and T66ASATa. Furthermore, the expression and overexpression of T66ASATb and AlASATb enhanced squalene accumulation in SR21 by up to 88%. The discovery highlights the functional diversity of DGAT2-like proteins and provides valuable information on steryl ester and squalene synthesis in thraustochytrids, paving the way to enhance squalene production through metabolic engineering.
2 citations
TL;DR: In this article , the details of fatty acyl-CoA recognition by zDHHC acyltransferases using insights from the recent structure are discussed. But, the authors do not discuss the potential mechanisms that underlie the potential mechanism for fat-coA compartmentalization and intracellular transport.
2 citations
Patent•
21 Nov 1988
TL;DR: In this article, the first reagent containing at least ATP, CoA and acyl CoA synthesizing enzyme is reacted with a free fatty acid in a specimen to afford CoA.
Abstract: PURPOSE:To enable to stably determine free fatty acid in a specimen, especially free fatty acid in blood on clinical inspection in good precision, by using a specific fatty acid or water soluble salt thereof as a part of reagents. CONSTITUTION:The first reagent containing at least ATP, CoA and acyl CoA synthesizing enzyme is reacted with a free fatty acid in a specimen to afford CoA. Then the second reagent containing a fatty acid expressed by formula I (R is 1-20C aliphatic group; n is integer of 0, or 1-2; A is -CH=CH- or -CHY-CHZ-; Y and Z are H, hydroxyl group or lower alkyl group) or water soluble salt thereof and acyl CoA oxidation enzyme and as necessary further reagent for measuring hydrogen peroxide by colorimetric method is reacted with the above-mentioned acyl CoA and change caused by oxidation of acyl CoA, e.g. produced hydrogen peroxide is measured.
2 citations