EC Number   |
General Information |
Reference  |
|---|
   2.3.1.158 | physiological function |
upon expression of heterologous oleate 12-hydroxylase in Arabidopsis thaliana mutants deficient in phospholipid:diacylglycerol acyltransferases 1 or 2 accumulate hydroxy fatty acids and show no difference with wild-type plants. Mutants are also able to accumulate hydroxy fatty acids in seed neutral lipids. Individually, phospholipid:diacylglycerol acyltransferases 1 or 2 do not play a major role in the incorporation of hydroxy fatty acids into triacylglycerols |
697014 |
| 2.3.1.158 | evolution |
PDAT belongs to the LCAT-like family |
720694 |
| 2.3.1.158 | malfunction |
artificial microRNA silencing of PDAT alters the membrane lipid composition, reducing the maximum specific growth rate |
720694 |
| 2.3.1.158 | physiological function |
phospholipid:diacylglycerol acyltransferase in the green microalga Chlamydomonas reinhardtii catalyzes triacylglycerol synthesis via two pathways: transacylation of diacylglycerol with acyl groups from phospholipids and galactolipids and diacylglycerol:diacylglycerol transacylation. PDAT-mediated membrane lipid turnover and triacylglycerol synthesis is essential for vigorous growth under favorable culture conditions and for membrane lipid degradation with concomitant production of triacylglycerol for survival under stress. PDAT also possesses acyl hydrolase activities using triacylglycerols, phospholipids, galactolipids, and cholesteryl esters as substrates |
720694 |
| 2.3.1.158 | physiological function |
expression of isoform DGTT1 complements the defect in the yeast DELTAdga1DELTAlro1 mutant that lacks the activity of triacylglycerol synthesis and leads to presence of oleic acid and lipid droplet formation |
736102 |
| 2.3.1.158 | physiological function |
expression of isoform DGTT2 complements the defect in the yeast DELTAdga1DELTAlro1 mutant that lacks the activity of triacylglycerol synthesis. Complementation by DGTT2 increased triacylglycerol content by 9fold |
736102 |
| 2.3.1.158 | physiological function |
expression of isoform DGTT3 complements the defect in the yeast DELTAdga1DELTAlro1 mutant that lacks the activity of triacylglycerol synthesis |
736102 |
| 2.3.1.158 | physiological function |
expression of isoform PDAT1 restores triacylglycerol synthesis in Saccharomyces cerevisiae H1246 when culturing yeast in the presence of alpha-linolenic acid |
736422 |
| 2.3.1.158 | physiological function |
overexpression of isoform PDAT1 increases leaf triacylglycerol accumulation, leading to oil droplet overexpansion through fusion. Ectopic expression of oleosin promotes the clustering of small oil droplets. Coexpression of PDAT1 with oleosin boosts leaf triacylglycerol content by up to 6.4% of the dry weight without affecting membrane lipid composition and plant growth. PDAT1 overexpression stimulates fatty acid synthesis and increases fatty acid flux toward the prokaryotic glycerolipid pathway. In the trigalactosyldiacylglycerol1-1 mutant, defective in eukaryotic thylakoid lipid synthesis, the combined overexpression of PDAT1 with oleosin increases leaf triacylglycerol content to 8.6% of the dry weight and total leaf lipid by fourfold. In the plastidic glycerol-3-phosphate acyltransferase1 mutant, defective in the prokaryotic glycerolipid pathway, PDAT1 overexpression enhances triacylglycerol content at the expense of thylakoid membrane lipids, leading to defects in chloroplast division and thylakoid biogenesis |
736985 |
| 2.3.1.158 | metabolism |
the enzyme is responsible for the last step of triacylglycerol synthesis in the acyl-CoA-independent pathway, catalyzing membrane lipid transformation |
-, 755830 |
