2.3.1.42: glycerone-phosphate O-acyltransferase
This is an abbreviated version!
For detailed information about glycerone-phosphate O-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.42
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2.3.1.42
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peroxisomal
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plasmalogens
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zellweger
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chondrodysplasia
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rhizomelic
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punctata
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glycerolipids
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phytanic
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alkyl-dhap
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hemochromatosis
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adrenoleukodystrophy
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stippling
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cerebro-hepato-renal
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lignoceric
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refsum
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medicine
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analysis
- 2.3.1.42
- peroxisomal
- plasmalogens
- zellweger
-
chondrodysplasia
-
rhizomelic
- punctata
- glycerolipids
-
phytanic
- alkyl-dhap
- hemochromatosis
- adrenoleukodystrophy
-
stippling
-
cerebro-hepato-renal
-
lignoceric
- refsum
- medicine
- analysis
Reaction
Synonyms
acyltransferase, dihydroxyacetone phosphate, DAP-AT, DAT, DHAP acyltransferase, DHAP-AT, DHAPAT, dihydroxyacetone phosphate acyl-transferase, dihydroxyacetone phosphate acyltransferase, dihydroxyacetone-phosphate acyltransferase, dihydroxyacetonephosphate acyltransferase, glyceronephosphate O-acyltransferase, GNPAT, LmDAT, male sterility protein, TtFARAT
ECTree
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General Information
General Information on EC 2.3.1.42 - glycerone-phosphate O-acyltransferase
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malfunction
metabolism
physiological function
additional information
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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
malfunction
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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
malfunction
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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
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catalyses initial step for glycerolipid metabolism, such as ether lipid derived virulence factor lipophosphoglycan and glycosylphosphatidylinositol-anchored proteins
metabolism
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in Trypanosoma brucei procyclic forms the enzyme is the physiologically relevant initial acyltransferase producing ether lipid precursors
metabolism
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catalyses initial step for glycerolipid metabolism, such as ether lipid derived virulence factor lipophosphoglycan and glycosylphosphatidylinositol-anchored proteins
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important for normal growth, survival during stationary phase, and virulence
physiological function
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the enzyme is important for survival during stationary phase and synthesis of ether lipids. In contrast, the enzyme is dispensable for normal growth
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
physiological function
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important for normal growth, survival during stationary phase, and virulence
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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
additional information
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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
additional information
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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
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