EC Number   |
General Information |
Reference |
|---|
   2.3.1.42 | malfunction |
an active enzyme is critical for normal growth and survival during the stationary phase. Deletion analyses show that the large N-terminal extension of this initial acyltransferase may be important for its stability or activity. Abrogation of the C-terminal glycosomal targeting signal sequence of LmDAT lead to extraglycosomal localization, do not impair its enzymatic activity but affect synthesis of the ether glycerolipid-based virulence factor lipophosphoglycan |
720841 |
| 2.3.1.42 | malfunction |
null mutant produces longer lipophosphoglycan molecules, that migrate slower into the membrane and are not released into the medium, levels of glycosylphosphatidylinositol-anchored proteins are increased in the membrane (maybe due to slower trnasperot through the secretory pathway), however, the integrity of detergent resistant membranes is not affected, and the typical metacyclic genes such as SHERP are still expressed, arabinosylated forms of lipophosphoglycan are still produced, and the normal morphology is still exhibited |
-, 705601 |
| 2.3.1.42 | metabolism |
catalyses initial step for glycerolipid metabolism, such as ether lipid derived virulence factor lipophosphoglycan and glycosylphosphatidylinositol-anchored proteins |
-, 705601 |
| 2.3.1.42 | metabolism |
in Trypanosoma brucei procyclic forms the enzyme is the physiologically relevant initial acyltransferase producing ether lipid precursors |
758156 |
| 2.3.1.42 | more |
the dihydroxyacetone phosphate acyltransferase in Tetrahymena termophila is fused to the fatty acid reductase, a bifunctional protein resulting from a gene fusion event that provides both substrates required to initiate ether lipid biosynthesis. The enzyme possesses an N-terminal FAR-like domain and a C-terminal acyltransferase-like domain, the latter shows dihydroxyacetone phosphate acyltransferase activity |
-, 736453 |
| 2.3.1.42 | physiological function |
important for normal growth, survival during stationary phase, and virulence |
-, 705601 |
| 2.3.1.42 | physiological function |
the enzyme is important for survival during stationary phase and synthesis of ether lipids. In contrast, the enzyme is dispensable for normal growth |
758156 |
| 2.3.1.42 | physiological function |
the enzyme recruits the enzyme USP30, which deubiquitylates and stabilizes dynamin-related protein 1, thereby facilitating regulation of mitochondrial morphology, lipid metabolism, and hepatocarcinogenesis |
756338 |
