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Literature summary extracted from

  • Dittrich-Domergue, F.; Joubes, J.; Moreau, P.; Lessire, R.; Stymne, S.; Domergue, F.
    The bifunctional protein TtFARAT from Tetrahymena thermophila catalyzes the formation of both precursors required to initiate ether lipid biosynthesis (2014), J. Biol. Chem., 289, 21984-21994.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.42 gene TTHERM_00221020, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant transient expression of GFP-tagged truncated bifunctional enzyme in Nicotiana tabacum cv. Petit Havana epidermis, using the Agrobacterium tumefaciens GV3101 strain and used for transient expression system, and transgenic expression in Saccharomyces cerevisiae, the recombinant enzyme's N-terminal FAR-like domain produces both 16:0 and 18:0 fatty alcohols, whereas the C-terminal acyltransferase-like domain is able to rescue the lethal phenotype of the Saccharomyces cerevisiae double mutant cmy228 (gat1DELTAgat2DELTA). Coexpression in Saccharomyces cerevisiae with the alkyl-dihydroxyacetone phosphate synthase from Tetrahymena thermophila results the detection of various glycerolipids with an ether bond. In yeast, GAT1 and GAT2 are the only two acyltransferases acylating the sn-1 position of G3P and DHAP, thus being essential to initiate glycerolipid biosynthesis Tetrahymena thermophila

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.42 peroxisome
-
 Tetrahymena thermophila 5777
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.42 Mg2+ required Tetrahymena thermophila

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.42 acyl-CoA + glycerone phosphate Tetrahymena thermophila
-
 CoA + 1-acylglycerone phosphate
-
 ?
2.3.1.42 acyl-CoA + glycerone phosphate Tetrahymena thermophila SB210
-
 CoA + 1-acylglycerone phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.42 Tetrahymena thermophila I7LW01 gene TTHERM_00221020
-
2.3.1.42 Tetrahymena thermophila SB210 I7LW01 gene TTHERM_00221020
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.42 acyl-CoA + glycerone phosphate
-
 Tetrahymena thermophila CoA + 1-acylglycerone phosphate
-
 ?
2.3.1.42 acyl-CoA + glycerone phosphate
-
 Tetrahymena thermophila SB210 CoA + 1-acylglycerone phosphate
-
 ?
2.3.1.42 additional information the bifunctional enzyme preferentially displays dihydroxyacetone phosphate acyltransferase activity, substrate specificity, overview Tetrahymena thermophila ?
-
 ?
2.3.1.42 additional information the bifunctional enzyme preferentially displays dihydroxyacetone phosphate acyltransferase activity, substrate specificity, overview Tetrahymena thermophila SB210 ?
-
 ?
2.3.1.42 oleoyl-CoA + glycerone phosphate
-
 Tetrahymena thermophila CoA + 1-oleoyl-glycerone phosphate
-
 ?
2.3.1.42 oleoyl-CoA + glycerone phosphate
-
 Tetrahymena thermophila SB210 CoA + 1-oleoyl-glycerone phosphate
-
 ?
2.3.1.42 palmitoleyl-CoA + glycerone phosphate
-
 Tetrahymena thermophila CoA + 1-palmitoleyl-glycerone phosphate
-
 ?
2.3.1.42 palmitoleyl-CoA + glycerone phosphate
-
 Tetrahymena thermophila SB210 CoA + 1-palmitoleyl-glycerone phosphate
-
 ?
2.3.1.42 palmitoyl-CoA + glycerone phosphate palmitoyl-CoA is the preferred substrate Tetrahymena thermophila CoA + 1-palmitoyl-glycerone phosphate
-
 ?
2.3.1.42 palmitoyl-CoA + glycerone phosphate palmitoyl-CoA is the preferred substrate Tetrahymena thermophila SB210 CoA + 1-palmitoyl-glycerone phosphate
-
 ?
2.3.1.42 stearoyl-CoA + glycerone phosphate
-
 Tetrahymena thermophila CoA + 1-stearoyl-glycerone phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.42 DHAP acyltransferase
-
 Tetrahymena thermophila
2.3.1.42 DHAPAT
-
 Tetrahymena thermophila
2.3.1.42 dihydroxyacetone phosphate acyltransferase
-
 Tetrahymena thermophila
2.3.1.42 male sterility protein UniProt Tetrahymena thermophila
2.3.1.42 TtFARAT
-
 Tetrahymena thermophila

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.42 30
-
 assay at Tetrahymena thermophila

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.42 7.5
-
 assay at Tetrahymena thermophila

General Information

EC Number General Information Comment Organism
2.3.1.42 additional information 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 Tetrahymena thermophila