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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
peroxisome | - |
Tetrahymena thermophila | 5777 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Tetrahymena thermophila |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Tetrahymena thermophila | I7LW01 | gene TTHERM_00221020 | - |
Tetrahymena thermophila SB210 | I7LW01 | gene TTHERM_00221020 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Tetrahymena thermophila |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Tetrahymena thermophila |
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 |