Literature summary for 2.3.1.42 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.

Cloned(Commentary)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Tetrahymena thermophila

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Tetrahymena thermophila	I7LW01	gene TTHERM_00221020	-
Tetrahymena thermophila SB210	I7LW01	gene TTHERM_00221020	-

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information	Comment	Organism
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