Any feedback?
Literature summary for 2.3.1.20 extracted from
- Properties and biotechnological applications of acyl-CoA diacylglycerol acyltransferase and phospholipid diacylglycerol acyltransferase from terrestrial plants and microalgae (2018), Lipids, 53, 663-688 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| PtdOH | a feedforward activator of plant DGAT1. PtdOH is suggested to aid in relieving possible autoinhibition by interacting with the N-terminal regulatory domain spanning the autoinhibitory motif and converts DGAT1 to a more active state that is also less sensitive to substrate inhibition | Brassica napus |  |
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Arabidopsis thaliana |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Phaeodactylum tricornutum |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Ricinus communis |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Vernicia fordii |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Arachis hypogaea |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Glycine max |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Nicotiana tabacum |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Tropaeolum majus |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Brassica napus |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Olea europaea |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Euonymus alatus |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Sesamum indicum |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Cuphea avigera |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Echium pitardii |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Linum usitatissimum |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Zea mays |
| biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Boechera stricta |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene DGAT3, heterologous expression in Saccharomyces cerevisiae TAG-deficient mutant strain H1246 | Phaeodactylum tricornutum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the intrinsically disordered region (IDR) of the N-terminal domain encompasses an autoinhibitory motif. Purified BnaDGAT1 can be phosphorylated and inactivated by SnRK1 | Brassica napus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | the N-terminal regions of Brassica napus DGAT1 enzymes binds acyl-CoA in a sigmoidal fashion, suggesting positive cooperative binding | Brassica napus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum membrane | an endoplasmic reticulum (ER) retrieval motif responsible for the steady state localization of DGAT2 protein in the ER is identified near the C-terminus of tung tree DGAT2 | Vernicia fordii | 5789 | - |
| membrane | - |
Ricinus communis | 16020 | - |
| membrane | - |
Glycine max | 16020 | - |
| membrane | - |
Arabidopsis thaliana | 16020 | - |
| membrane | - |
Nicotiana tabacum | 16020 | - |
| membrane | - |
Tropaeolum majus | 16020 | - |
| membrane | - |
Brassica napus | 16020 | - |
| membrane | - |
Olea europaea | 16020 | - |
| membrane | - |
Euonymus alatus | 16020 | - |
| membrane | - |
Sesamum indicum | 16020 | - |
| membrane | - |
Cuphea avigera | 16020 | - |
| membrane | - |
Echium pitardii | 16020 | - |
| membrane | - |
Linum usitatissimum | 16020 | - |
| membrane | - |
Arachis hypogaea | 16020 | - |
| membrane | - |
Zea mays | 16020 | - |
| membrane | - |
Boechera stricta | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Chlamydomonas reinhardtii | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Nicotiana tabacum | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Arachis hypogaea | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Linum usitatissimum | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Tropaeolum majus | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Phaeodactylum tricornutum | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Ricinus communis | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Vernicia fordii | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Glycine max | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Brassica napus | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Arabidopsis thaliana | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Thraustochytrium aureum | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Triadica sebifera | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Olea europaea | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Euonymus alatus | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Sesamum indicum | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Cuphea avigera var. pulcherrima | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Umbelopsis ramanniana | 16020 | - |
| membrane | embedded in the membrane lipid bilayer | Caenorhabditis elegans | 16020 | - |
| membrane | tung tree DGAT1 appears to have two termini localized in the cytosol, suggesting the presence of even-numbered transmembrane domains | Vernicia fordii | 16020 | - |
| microsome | - |
Arabidopsis thaliana | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acyl-CoA + 1,2-diacyl-sn-glycerol | Arabidopsis thaliana | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Phaeodactylum tricornutum | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Ricinus communis | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Vernicia fordii | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Arachis hypogaea | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Glycine max | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Nicotiana tabacum | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Tropaeolum majus | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Brassica napus | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Olea europaea | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Euonymus alatus | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Sesamum indicum | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Cuphea avigera | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Echium pitardii | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Linum usitatissimum | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Zea mays | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | Boechera stricta | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
| Arabidopsis thaliana | Q9ASU1 | - |
- |
| Arabidopsis thaliana | Q9C5W0 | - |
- |
| Arabidopsis thaliana | Q9SLD2 | - |
- |
| Arachis hypogaea | - |
- |
- |
| Arachis hypogaea | A0A0M3SGK9 | - |
- |
| Arachis hypogaea | Q2KP14 | - |
- |
| Boechera stricta | - |
- |
- |
| Brassica napus | K9LL63 | isozyme DGAT1.a | - |
| Brassica napus | Q9XGR5 | - |
- |
| Brassica napus | Q9XGV4 | - |
- |
| Caenorhabditis elegans | Q9XUW0 | - |
- |
| Chlamydomonas reinhardtii | - |
- |
- |
| Cuphea avigera | A0A193DVK9 | var. pulcherrima | - |
| Cuphea avigera var. pulcherrima | A0A193DVK9 | - |
- |
| Echium pitardii | D9U3F8 | - |
- |
| Euonymus alatus | Q5UEM2 | - |
- |
| Glycine max | I1MSF2 | - |
- |
| Glycine max | Q5GKZ7 | - |
- |
| Glycine max | Q5GKZ7 | isozyme DGAT1A | - |
| Linum usitatissimum | - |
- |
- |
| Linum usitatissimum | V5LV83 | isozyme DGAT2-1 | - |
| Linum usitatissimum | V5LV86 | - |
- |
| Mus musculus | Q9Z2A7 | - |
- |
| Nicotiana tabacum | - |
- |
- |
| Nicotiana tabacum | Q9SEG9 | - |
- |
| Olea europaea | Q6ED63 | - |
- |
| Phaeodactylum tricornutum | - |
- |
- |
| Ricinus communis | A1A442 | - |
- |
| Ricinus communis | Q67C39 | - |
- |
| Sesamum indicum | M1E7W9 | - |
- |
| Thraustochytrium aureum | R9QY77 | - |
- |
| Triadica sebifera | - |
- |
- |
| Tropaeolum majus | - |
- |
- |
| Tropaeolum majus | Q8RX96 | - |
- |
| Umbelopsis ramanniana | Q96UY1 | - |
- |
| Umbelopsis ramanniana | Q96UY2 | - |
- |
| Vernicia fordii | Q0QJH9 | - |
- |
| Vernicia fordii | Q0QJI1 | - |
- |
| Zea mays | B0LF77 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | purified BnaDGAT1 can be phosphorylated and inactivated by SnRK1. SnRK1 has also been found to act on the WRI transcription factor, which subsequently regulates DGAT expression | Brassica napus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme | Arachis hypogaea |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| flower | - |
Arabidopsis thaliana | - |
| leaf | - |
Arabidopsis thaliana | - |
| additional information | in Arabidopsis thaliana, DGAT1 is expressed in different plant organs such as leaves, roots, flowers, siliques, seeds, and seedlings, the last two of which exhibit the highest expression levels. The high expression of AtDGAT1 in developing seeds and pollen correlates with the ability of these organs to accumulate high amounts of TAG. In addition, DGAT1 is expressed at lower levels in shoots and roots of seedling, which are sites exhibiting active cell division and growth | Arabidopsis thaliana | - |
| additional information | isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues | Arabidopsis thaliana | - |
| additional information | the expression level of soybean DGAT1 is much higher relative to DGAT2 throughout seed development | Glycine max | - |
| additional information | the expression level of soybean DGAT1 is much higher relative to DGAT2 throughout seed development | Zea mays | - |
| pollen | - |
Arabidopsis thaliana | - |
| pollen | high DGAT1 expression | Arabidopsis thaliana | - |
| root | - |
Arabidopsis thaliana | - |
| seed | - |
Ricinus communis | - |
| seed | - |
Vernicia fordii | - |
| seed | - |
Glycine max | - |
| seed | - |
Nicotiana tabacum | - |
| seed | - |
Tropaeolum majus | - |
| seed | - |
Brassica napus | - |
| seed | - |
Olea europaea | - |
| seed | - |
Euonymus alatus | - |
| seed | - |
Sesamum indicum | - |
| seed | - |
Cuphea avigera | - |
| seed | - |
Echium pitardii | - |
| seed | - |
Linum usitatissimum | - |
| seed | - |
Arachis hypogaea | - |
| seed | - |
Zea mays | - |
| seed | - |
Boechera stricta | - |
| seed | developing seeds, high DGAT1 expression | Arabidopsis thaliana | - |
| seed | low expresssion of DGAT2 | Arabidopsis thaliana | - |
| seedling | - |
Arabidopsis thaliana | - |
| seedling | high DGAT1 expression | Arabidopsis thaliana | - |
| shoot | - |
Arabidopsis thaliana | - |
| silique | - |
Arabidopsis thaliana | - |
| silique | high DGAT1 expression | Arabidopsis thaliana | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Arabidopsis thaliana | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Phaeodactylum tricornutum | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Ricinus communis | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Vernicia fordii | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Arachis hypogaea | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Glycine max | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Nicotiana tabacum | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Tropaeolum majus | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Brassica napus | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Olea europaea | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Euonymus alatus | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Sesamum indicum | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Cuphea avigera | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Echium pitardii | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Linum usitatissimum | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Zea mays | CoA + 1,2,3-triacylglycerol | - |
? | |
| acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Boechera stricta | CoA + 1,2,3-triacylglycerol | - |
? | |
| additional information | bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75 | Arabidopsis thaliana | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the N-terminal region of DGAT1 forms dimers and tetramers based on crosslinking experiments. The N-terminal region plays a role in self-oligomerization. N-terminal structure-function analysis of Brassica napus DGAT1, overview. The remainder of DGAT1 accounting for more than 75% of the enzyme contains the transmembrane dommain (TMD) and the catalytic sites. The TMD is expected to form helical bundles in the membrane, which agrees with the circular dichroism profile of purified BnaDGAT1 indicating the predominance of alpha-helices | Brassica napus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acyl-CoA:diacylglycerol acyltransferase | - |
Phaeodactylum tricornutum |
| acyl-CoA:diacylglycerol acyltransferase | - |
Ricinus communis |
| acyl-CoA:diacylglycerol acyltransferase | - |
Vernicia fordii |
| acyl-CoA:diacylglycerol acyltransferase | - |
Arachis hypogaea |
| acyl-CoA:diacylglycerol acyltransferase | - |
Glycine max |
| acyl-CoA:diacylglycerol acyltransferase | - |
Arabidopsis thaliana |
| acyl-CoA:diacylglycerol acyltransferase | - |
Nicotiana tabacum |
| acyl-CoA:diacylglycerol acyltransferase | - |
Tropaeolum majus |
| acyl-CoA:diacylglycerol acyltransferase | - |
Brassica napus |
| acyl-CoA:diacylglycerol acyltransferase | - |
Olea europaea |
| acyl-CoA:diacylglycerol acyltransferase | - |
Euonymus alatus |
| acyl-CoA:diacylglycerol acyltransferase | - |
Sesamum indicum |
| acyl-CoA:diacylglycerol acyltransferase | - |
Cuphea avigera |
| acyl-CoA:diacylglycerol acyltransferase | - |
Echium pitardii |
| acyl-CoA:diacylglycerol acyltransferase | - |
Linum usitatissimum |
| acyl-CoA:diacylglycerol acyltransferase | - |
Zea mays |
| acyl-CoA:diacylglycerol acyltransferase | - |
Boechera stricta |
| bifunctional wax synthase/DGAT | - |
Arabidopsis thaliana |
| DAGAT | - |
Nicotiana tabacum |
| DGAT | - |
Phaeodactylum tricornutum |
| DGAT | - |
Ricinus communis |
| DGAT | - |
Vernicia fordii |
| DGAT | - |
Arachis hypogaea |
| DGAT | - |
Glycine max |
| DGAT | - |
Arabidopsis thaliana |
| DGAT | - |
Nicotiana tabacum |
| DGAT | - |
Tropaeolum majus |
| DGAT | - |
Brassica napus |
| DGAT | - |
Olea europaea |
| DGAT | - |
Euonymus alatus |
| DGAT | - |
Sesamum indicum |
| DGAT | - |
Cuphea avigera |
| DGAT | - |
Echium pitardii |
| DGAT | - |
Linum usitatissimum |
| DGAT | - |
Zea mays |
| DGAT | - |
Boechera stricta |
| DGAT1 | - |
Nicotiana tabacum |
| DGAT1 | - |
Arachis hypogaea |
| DGAT1 | - |
Linum usitatissimum |
| DGAT1 | - |
Tropaeolum majus |
| DGAT1 | - |
Ricinus communis |
| DGAT1 | - |
Mus musculus |
| DGAT1 | - |
Vernicia fordii |
| DGAT1 | - |
Glycine max |
| DGAT1 | - |
Brassica napus |
| DGAT1 | - |
Arabidopsis thaliana |
| DGAT1 | - |
Olea europaea |
| DGAT1 | - |
Euonymus alatus |
| DGAT1 | - |
Sesamum indicum |
| DGAT1 | - |
Cuphea avigera var. pulcherrima |
| DGAT1 | - |
Cuphea avigera |
| DGAT1 | - |
Echium pitardii |
| DGAT1 | - |
Boechera stricta |
| DGAT1-2 | - |
Zea mays |
| DGAT1.a | - |
Brassica napus |
| DGAT1A | - |
Glycine max |
| DGAT1B | - |
Glycine max |
| DGAT2 | - |
Chlamydomonas reinhardtii |
| DGAT2 | - |
Phaeodactylum tricornutum |
| DGAT2 | - |
Vernicia fordii |
| DGAT2 | - |
Brassica napus |
| DGAT2 | - |
Thraustochytrium aureum |
| DGAT2 | - |
Triadica sebifera |
| DGAT2 | - |
Caenorhabditis elegans |
| DGAT2 | - |
Ricinus communis |
| DGAT2 | - |
Arabidopsis thaliana |
| DGAT2-1 | - |
Linum usitatissimum |
| DGAT2A | - |
Umbelopsis ramanniana |
| DGAT2b | - |
Umbelopsis ramanniana |
| DGAT3 | - |
Phaeodactylum tricornutum |
| DGAT3 | - |
Arachis hypogaea |
| DGAT3 | - |
Arabidopsis thaliana |
| diacylglycerol O-acyltransferase 2 | - |
Vernicia fordii |
| diacylglycerol O-acyltransferase 2 | - |
Ricinus communis |
| More | see also EC 2.3.1.75 | Arabidopsis thaliana |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Brassica napus | DGAT1 overexpression during seed development in Brassica napus decreases the penalty on seed oil content caused by drought. The WRI transcription factor regulates DGAT expression | additional information |
| Boechera stricta | the expression of DGAT1 is found to be highly cold responsive and correlated with the cold tolerance in Brassica stricta lines | additional information |
| Zea mays | activation of DGAT1 by a phenylalanine insertion in the maize (Zea mays) DGAT1 | up |
| Brassica napus | the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75) | Phaeodactylum tricornutum |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75) | Arachis hypogaea |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75) | Arabidopsis thaliana |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75) | Boechera stricta |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Ricinus communis |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Vernicia fordii |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Glycine max |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Arabidopsis thaliana |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Nicotiana tabacum |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Tropaeolum majus |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Brassica napus |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Olea europaea |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Euonymus alatus |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Sesamum indicum |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Cuphea avigera |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Echium pitardii |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Linum usitatissimum |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Arachis hypogaea |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues | Zea mays |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases | Vernicia fordii |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases | Ricinus communis |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases | Arabidopsis thaliana |
| evolution | the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases | Linum usitatissimum |
| malfunction | DGAT1 overexpression during seed development in Brassica napus decreases the penalty on seed oil content caused by drought | Brassica napus |
| malfunction | enhanced DGAT1 expression leads to increased freezing tolerance in Arabidopsis thaliana, whereas DGAT1 deficient mutant lines are sensitive to freezing. The overexpression of DGAT1 with the mutated SnRK1 site translated to higher seed TAG levels in Arabidopsis thaliana when compared to an unmodified enzyme | Arabidopsis thaliana |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Ricinus communis |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Vernicia fordii |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Arachis hypogaea |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Glycine max |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Tropaeolum majus |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Brassica napus |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Olea europaea |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Euonymus alatus |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Sesamum indicum |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Cuphea avigera |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Arabidopsis thaliana |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Echium pitardii |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Linum usitatissimum |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Boechera stricta |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. Involvement of DGAT3 in TAG biosynthesis in microalgae and diatoms confirmed by heterologous expression in Saccharomyces cerevisiae TAG-deficient mutant strain H1246 | Phaeodactylum tricornutum |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. The activation of DGAT1 in the maize is responsible for the increased embryo oil content in a high-oil maize line | Zea mays |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of sn-1, 2-DAG to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG | Nicotiana tabacum |
| metabolism | diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of sn-1,2-DAG to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1, 2-DAG to yield TAG | Arabidopsis thaliana |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol | Umbelopsis ramanniana |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Mus musculus |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Arabidopsis thaliana |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol | Chlamydomonas reinhardtii |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol | Phaeodactylum tricornutum |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol | Brassica napus |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol | Thraustochytrium aureum |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol | Triadica sebifera |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol | Umbelopsis ramanniana |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol | Ricinus communis |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Nicotiana tabacum |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Arachis hypogaea |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Linum usitatissimum |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Tropaeolum majus |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Ricinus communis |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Vernicia fordii |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Glycine max |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Brassica napus |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Olea europaea |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Euonymus alatus |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Sesamum indicum |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Cuphea avigera var. pulcherrima |
| metabolism | the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties | Caenorhabditis elegans |
| additional information | the expression of DGAT1 is found to be highly cold responsive and correlated with the cold tolerance in Boechera stricta lines | Boechera stricta |
| additional information | the N-terminal region plays a role in self-oligomerization. The hydrophilic N-terminal region of DGAT1 constitutes the enzyme's regulatory domain, which is not necessary for catalysis. This domain is comprised of two distinct segments, specifically an intrinsically disordered region (IDR) and a folded segment. The IDR can form interactions that are important for dimerization and may allow it to partially mediate positive cooperativity. Truncation of this IDR results in a more active enzyme form, suggesting the IDR encompasses an autoinhibitory motif. N-terminal structure-function analysis of Brassica napus DGAT1, overview | Brassica napus |
| physiological function | DGAT1 appears to play a role in freezing and/or drought stress responses in Arabidopsis thaliana. DGAT1 is suggested to be involved in maintaining a balance of DAG and acyl-CoA for the biosynthesis of membrane lipids and recycling of fatty acids to TAG under conditions where catabolic reactions are halted. Regulation of the enzyme, overview | Arabidopsis thaliana |
| physiological function | DGAT1 appears to play a role in freezing and/or drought stress responses in Brassica napus. Regulation of the enzyme, overview | Brassica napus |
| physiological function | regulation of the enzyme, overview | Phaeodactylum tricornutum |
| physiological function | regulation of the enzyme, overview | Ricinus communis |
| physiological function | regulation of the enzyme, overview | Vernicia fordii |
| physiological function | regulation of the enzyme, overview | Arachis hypogaea |
| physiological function | regulation of the enzyme, overview | Glycine max |
| physiological function | regulation of the enzyme, overview | Nicotiana tabacum |
| physiological function | regulation of the enzyme, overview | Tropaeolum majus |
| physiological function | regulation of the enzyme, overview | Olea europaea |
| physiological function | regulation of the enzyme, overview | Euonymus alatus |
| physiological function | regulation of the enzyme, overview | Sesamum indicum |
| physiological function | regulation of the enzyme, overview | Cuphea avigera |
| physiological function | regulation of the enzyme, overview | Echium pitardii |
| physiological function | regulation of the enzyme, overview | Linum usitatissimum |
| physiological function | regulation of the enzyme, overview | Arabidopsis thaliana |
| physiological function | regulation of the enzyme, overview | Zea mays |
| physiological function | regulation of the enzyme, overview | Boechera stricta |
| physiological function | regulation of the enzyme, overview. Arabidopsis thaliana DGAT3 appears to be involved in recycling of linoleic acid (18:2DELTA9cis,12cis) and alpha-linolenic acid (18:3DELTA9cis, 12cis,15cis) into for triacylglycerol (TAG) when TAG breakdown is blocked | Arabidopsis thaliana |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
