Protein Family Models

The terminal step of triacylglycerol (TAG) formation is catalysed by the enzyme diacylglycerol acyltransferase (DAGAT), required for synthesis and storage of intracellular triglycerides [1,2,3]. In yeast, it is involved in lipid particle synthesis from the endoplasmic reticulum (ER), promoting localised TAG production at discrete ER subdomains, and in ergosterol biosynthesis [1,4]. This family also includes Acyl-CoA wax alcohol acyltransferase 1 and 2 (AWAT1/2) which catalyse the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters [5,6]. AWAT2 (also known as MFAT) also possesses acyl-CoA retinol acyltransferase (ARAT) activity that catalyses 11-cis-specific retinyl ester synthesis and shows higher catalytic efficiency toward 11-cis-retinol versus 9-cis-retinol, 13-cis-retinol, and all-trans-retinol substrates [7]. [1]. 11751875. The DGA1 gene determines a second triglyceride synthetic pathway in yeast. Oelkers P, Cromley D, Padamsee M, Billheimer JT, Sturley SL;. J Biol Chem 2002;277:8877-8881. [2]. 11751830. Synthesis of triacylglycerols by the acyl-coenzyme A:diacyl-glycerol acyltransferase Dga1p in lipid particles of the yeast Saccharomyces cerevisiae. Sorger D, Daum G;. J Bacteriol 2002;184:519-524. [3]. 27184406. Biochemical characterization of human acyl coenzyme A: 2-monoacylglycerol acyltransferase-3 (MGAT3). Brandt C, McFie PJ, Stone SJ;. Biochem Biophys Res Commun. 2016;475:264-270. [4]. 12963726. Schizosaccharomyces pombe cells deficient in triacylglycerols synthesis undergo apoptosis upon entry into the stationary phase. Zhang Q, Chieu HK, Low CP, Zhang S, Heng CK, Yang H. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function [1]. This family also includes tafazzin Swiss:Q16635, the Barth syndrome gene [2]. [1]. 9259571. Barth syndrome may be due to an acyltransferase deficiency. Neuwald AF;. Curr Biol 1997;7:465-466. [2]. 8630491. A novel X-linked gene, G4.5. is responsible for Barth syndrome. Bione S, D'Adamo P, Maestrini E, Gedeon AK, Bolhuis PA, Toniolo D;. Nat Genet 1996;12:385-389. (from Pfam)

Date:

2024-10-16

lysophospholipid acyltransferase (LPLAT) family protein may act as an acyltransferase of a de novo or remodeling pathway of glycerophospholipid biosynthesis, catalyzing the incorporation of an acyl group from either acyl-CoAs or acyl-acyl carrier proteins (acyl-ACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid

Date:

2024-06-25