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Literature summary extracted from

  • Xu, Y.; Caldo, K.M.P.; Pal-Nath, D.; Ozga, J.; Lemieux, M.J.; Weselake, R.J.; Chen, G.
    Properties and biotechnological applications of acyl-CoA diacylglycerol acyltransferase and phospholipid diacylglycerol acyltransferase from terrestrial plants and microalgae (2018), Lipids, 53, 663-688 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.20 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

EC Number Application Comment Organism
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.158 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
2.3.1.158 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 Crepis palaestina
2.3.1.158 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
2.3.1.158 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 Helianthus annuus
2.3.1.158 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.20 gene DGAT3, heterologous expression in Saccharomyces cerevisiae TAG-deficient mutant strain H1246 Phaeodactylum tricornutum
2.3.1.158 gene LRO1, DNA and amino acid sequence determination and analysis Saccharomyces cerevisiae
2.3.1.158 overexpression in Arabidopsis thaliana increases alpha-linolenic acis content in seed oil Linum usitatissimum
2.3.1.158 overexpression in Arabidopsis thaliana increases hydroxy fatty acid in seed oil Ricinus communis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.20 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.20 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

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.20 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
-
2.3.1.20 membrane
-
 Ricinus communis 16020
-
2.3.1.20 membrane
-
 Glycine max 16020
-
2.3.1.20 membrane
-
 Arabidopsis thaliana 16020
-
2.3.1.20 membrane
-
 Nicotiana tabacum 16020
-
2.3.1.20 membrane
-
 Tropaeolum majus 16020
-
2.3.1.20 membrane
-
 Brassica napus 16020
-
2.3.1.20 membrane
-
 Olea europaea 16020
-
2.3.1.20 membrane
-
 Euonymus alatus 16020
-
2.3.1.20 membrane
-
 Sesamum indicum 16020
-
2.3.1.20 membrane
-
 Cuphea avigera 16020
-
2.3.1.20 membrane
-
 Echium pitardii 16020
-
2.3.1.20 membrane
-
 Linum usitatissimum 16020
-
2.3.1.20 membrane
-
 Arachis hypogaea 16020
-
2.3.1.20 membrane
-
 Zea mays 16020
-
2.3.1.20 membrane
-
 Boechera stricta 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Chlamydomonas reinhardtii 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Nicotiana tabacum 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Arachis hypogaea 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Linum usitatissimum 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Tropaeolum majus 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Phaeodactylum tricornutum 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Ricinus communis 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Vernicia fordii 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Glycine max 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Brassica napus 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Arabidopsis thaliana 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Thraustochytrium aureum 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Triadica sebifera 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Olea europaea 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Euonymus alatus 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Sesamum indicum 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Cuphea avigera var. pulcherrima 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Umbelopsis ramanniana 16020
-
2.3.1.20 membrane embedded in the membrane lipid bilayer Caenorhabditis elegans 16020
-
2.3.1.20 membrane tung tree DGAT1 appears to have two termini localized in the cytosol, suggesting the presence of even-numbered transmembrane domains Vernicia fordii 16020
-
2.3.1.20 microsome
-
 Arabidopsis thaliana
-
-
2.3.1.158 microsome
-
 Helianthus annuus
-
-
2.3.1.158 additional information phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Crepis palaestina
-
-
2.3.1.158 additional information phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Arabidopsis thaliana
-
-
2.3.1.158 additional information phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Saccharomyces cerevisiae
-
-
2.3.1.158 additional information phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Brassica napus
-
-
2.3.1.158 additional information phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Helianthus annuus
-
-
2.3.1.158 additional information phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Ricinus communis
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Arabidopsis thaliana
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Phaeodactylum tricornutum
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Ricinus communis
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Vernicia fordii
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Arachis hypogaea
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Glycine max
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Nicotiana tabacum
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Tropaeolum majus
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Brassica napus
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Olea europaea
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Euonymus alatus
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Sesamum indicum
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Cuphea avigera
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Echium pitardii
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Linum usitatissimum
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Zea mays
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol Boechera stricta
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol Brassica napus
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol Crepis palaestina
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol Arabidopsis thaliana
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol Saccharomyces cerevisiae
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol Helianthus annuus
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol Ricinus communis
-
 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol Saccharomyces cerevisiae ATCC 204508
-
 CoA + 1,2,3-triacylglycerol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.20 Arabidopsis thaliana
-
-
-
2.3.1.20 Arabidopsis thaliana Q9ASU1
-
-
2.3.1.20 Arabidopsis thaliana Q9C5W0
-
-
2.3.1.20 Arabidopsis thaliana Q9SLD2
-
-
2.3.1.20 Arachis hypogaea
-
-
-
2.3.1.20 Arachis hypogaea A0A0M3SGK9
-
-
2.3.1.20 Arachis hypogaea Q2KP14
-
-
2.3.1.20 Boechera stricta
-
-
-
2.3.1.20 Brassica napus K9LL63 isozyme DGAT1.a
-
2.3.1.20 Brassica napus Q9XGR5
-
-
2.3.1.20 Brassica napus Q9XGV4
-
-
2.3.1.20 Caenorhabditis elegans Q9XUW0
-
-
2.3.1.20 Chlamydomonas reinhardtii
-
-
-
2.3.1.20 Cuphea avigera A0A193DVK9 var. pulcherrima
-
2.3.1.20 Cuphea avigera var. pulcherrima A0A193DVK9
-
-
2.3.1.20 Echium pitardii D9U3F8
-
-
2.3.1.20 Euonymus alatus Q5UEM2
-
-
2.3.1.20 Glycine max I1MSF2
-
-
2.3.1.20 Glycine max Q5GKZ7
-
-
2.3.1.20 Glycine max Q5GKZ7 isozyme DGAT1A
-
2.3.1.20 Linum usitatissimum
-
-
-
2.3.1.20 Linum usitatissimum V5LV83 isozyme DGAT2-1
-
2.3.1.20 Linum usitatissimum V5LV86
-
-
2.3.1.20 Mus musculus Q9Z2A7
-
-
2.3.1.20 Nicotiana tabacum
-
-
-
2.3.1.20 Nicotiana tabacum Q9SEG9
-
-
2.3.1.20 Olea europaea Q6ED63
-
-
2.3.1.20 Phaeodactylum tricornutum
-
-
-
2.3.1.20 Ricinus communis A1A442
-
-
2.3.1.20 Ricinus communis Q67C39
-
-
2.3.1.20 Sesamum indicum M1E7W9
-
-
2.3.1.20 Thraustochytrium aureum R9QY77
-
-
2.3.1.20 Triadica sebifera
-
-
-
2.3.1.20 Tropaeolum majus
-
-
-
2.3.1.20 Tropaeolum majus Q8RX96
-
-
2.3.1.20 Umbelopsis ramanniana Q96UY1
-
-
2.3.1.20 Umbelopsis ramanniana Q96UY2
-
-
2.3.1.20 Vernicia fordii Q0QJH9
-
-
2.3.1.20 Vernicia fordii Q0QJI1
-
-
2.3.1.20 Zea mays B0LF77
-
-
2.3.1.158 Arabidopsis thaliana Q9FNA9
-
-
2.3.1.158 Arabidopsis thaliana Q9FYC7
-
-
2.3.1.158 Brassica napus
-
-
-
2.3.1.158 Crepis palaestina
-
-
-
2.3.1.158 Helianthus annuus A0A251VCQ4
-
-
2.3.1.158 Linum usitatissimum
-
-
-
2.3.1.158 Ricinus communis
-
-
-
2.3.1.158 Ricinus communis F2VR35
-
-
2.3.1.158 Saccharomyces cerevisiae P40345
-
-
2.3.1.158 Saccharomyces cerevisiae ATCC 204508 P40345
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.1.20 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)

EC Number Purification (Comment) Organism
2.3.1.20 native enzyme Arachis hypogaea

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.20 flower
-
 Arabidopsis thaliana
-
2.3.1.20 leaf
-
 Arabidopsis thaliana
-
2.3.1.20 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
-
2.3.1.20 additional information isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues Arabidopsis thaliana
-
2.3.1.20 additional information the expression level of soybean DGAT1 is much higher relative to DGAT2 throughout seed development Glycine max
-
2.3.1.20 additional information the expression level of soybean DGAT1 is much higher relative to DGAT2 throughout seed development Zea mays
-
2.3.1.20 pollen
-
 Arabidopsis thaliana
-
2.3.1.20 pollen high DGAT1 expression Arabidopsis thaliana
-
2.3.1.20 root
-
 Arabidopsis thaliana
-
2.3.1.20 seed
-
 Ricinus communis
-
2.3.1.20 seed
-
 Vernicia fordii
-
2.3.1.20 seed
-
 Glycine max
-
2.3.1.20 seed
-
 Nicotiana tabacum
-
2.3.1.20 seed
-
 Tropaeolum majus
-
2.3.1.20 seed
-
 Brassica napus
-
2.3.1.20 seed
-
 Olea europaea
-
2.3.1.20 seed
-
 Euonymus alatus
-
2.3.1.20 seed
-
 Sesamum indicum
-
2.3.1.20 seed
-
 Cuphea avigera
-
2.3.1.20 seed
-
 Echium pitardii
-
2.3.1.20 seed
-
 Linum usitatissimum
-
2.3.1.20 seed
-
 Arachis hypogaea
-
2.3.1.20 seed
-
 Zea mays
-
2.3.1.20 seed
-
 Boechera stricta
-
2.3.1.20 seed developing seeds, high DGAT1 expression Arabidopsis thaliana
-
2.3.1.20 seed low expresssion of DGAT2 Arabidopsis thaliana
-
2.3.1.20 seedling
-
 Arabidopsis thaliana
-
2.3.1.20 seedling high DGAT1 expression Arabidopsis thaliana
-
2.3.1.20 shoot
-
 Arabidopsis thaliana
-
2.3.1.20 silique
-
 Arabidopsis thaliana
-
2.3.1.20 silique high DGAT1 expression Arabidopsis thaliana
-
2.3.1.158 leaf AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds Arabidopsis thaliana
-
2.3.1.158 additional information isozyme AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds, whereas isozyme AtPDAT2 is highly expressed in seeds Arabidopsis thaliana
-
2.3.1.158 seed
-
 Helianthus annuus
-
2.3.1.158 seed high expression Arabidopsis thaliana
-
2.3.1.158 seed AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds Arabidopsis thaliana
-
2.3.1.158 seed highly expressed in seeds Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Arabidopsis thaliana CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Phaeodactylum tricornutum CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Ricinus communis CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Vernicia fordii CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Arachis hypogaea CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Glycine max CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Nicotiana tabacum CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Tropaeolum majus CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Brassica napus CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Olea europaea CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Euonymus alatus CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Sesamum indicum CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Cuphea avigera CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Echium pitardii CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Linum usitatissimum CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Zea mays CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Boechera stricta CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.20 additional information bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75 Arabidopsis thaliana ?
-
-
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Brassica napus CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Crepis palaestina CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Arabidopsis thaliana CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Saccharomyces cerevisiae CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Helianthus annuus CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Ricinus communis CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 acyl-CoA + 1,2-diacyl-sn-glycerol
-
 Saccharomyces cerevisiae ATCC 204508 CoA + 1,2,3-triacylglycerol
-
 ?
2.3.1.158 additional information Saccharoymces cerevisiae PDAT also displays low DAG:DAG transacylase activity Saccharomyces cerevisiae ?
-
-
2.3.1.158 additional information Saccharoymces cerevisiae PDAT also displays low DAG:DAG transacylase activity Saccharomyces cerevisiae ATCC 204508 ?
-
-

Subunits

EC Number Subunits Comment Organism
2.3.1.20 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

EC Number Synonyms Comment Organism
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Phaeodactylum tricornutum
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Ricinus communis
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Vernicia fordii
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Arachis hypogaea
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Glycine max
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Arabidopsis thaliana
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Nicotiana tabacum
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Tropaeolum majus
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Brassica napus
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Olea europaea
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Euonymus alatus
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Sesamum indicum
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Cuphea avigera
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Echium pitardii
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Linum usitatissimum
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Zea mays
2.3.1.20 acyl-CoA:diacylglycerol acyltransferase
-
 Boechera stricta
2.3.1.20 bifunctional wax synthase/DGAT
-
 Arabidopsis thaliana
2.3.1.20 DAGAT
-
 Nicotiana tabacum
2.3.1.20 DGAT
-
 Phaeodactylum tricornutum
2.3.1.20 DGAT
-
 Ricinus communis
2.3.1.20 DGAT
-
 Vernicia fordii
2.3.1.20 DGAT
-
 Arachis hypogaea
2.3.1.20 DGAT
-
 Glycine max
2.3.1.20 DGAT
-
 Arabidopsis thaliana
2.3.1.20 DGAT
-
 Nicotiana tabacum
2.3.1.20 DGAT
-
 Tropaeolum majus
2.3.1.20 DGAT
-
 Brassica napus
2.3.1.20 DGAT
-
 Olea europaea
2.3.1.20 DGAT
-
 Euonymus alatus
2.3.1.20 DGAT
-
 Sesamum indicum
2.3.1.20 DGAT
-
 Cuphea avigera
2.3.1.20 DGAT
-
 Echium pitardii
2.3.1.20 DGAT
-
 Linum usitatissimum
2.3.1.20 DGAT
-
 Zea mays
2.3.1.20 DGAT
-
 Boechera stricta
2.3.1.20 DGAT1
-
 Nicotiana tabacum
2.3.1.20 DGAT1
-
 Arachis hypogaea
2.3.1.20 DGAT1
-
 Linum usitatissimum
2.3.1.20 DGAT1
-
 Tropaeolum majus
2.3.1.20 DGAT1
-
 Ricinus communis
2.3.1.20 DGAT1
-
 Mus musculus
2.3.1.20 DGAT1
-
 Vernicia fordii
2.3.1.20 DGAT1
-
 Glycine max
2.3.1.20 DGAT1
-
 Brassica napus
2.3.1.20 DGAT1
-
 Arabidopsis thaliana
2.3.1.20 DGAT1
-
 Olea europaea
2.3.1.20 DGAT1
-
 Euonymus alatus
2.3.1.20 DGAT1
-
 Sesamum indicum
2.3.1.20 DGAT1
-
 Cuphea avigera var. pulcherrima
2.3.1.20 DGAT1
-
 Cuphea avigera
2.3.1.20 DGAT1
-
 Echium pitardii
2.3.1.20 DGAT1
-
 Boechera stricta
2.3.1.20 DGAT1-2
-
 Zea mays
2.3.1.20 DGAT1.a
-
 Brassica napus
2.3.1.20 DGAT1A
-
 Glycine max
2.3.1.20 DGAT1B
-
 Glycine max
2.3.1.20 DGAT2
-
 Chlamydomonas reinhardtii
2.3.1.20 DGAT2
-
 Phaeodactylum tricornutum
2.3.1.20 DGAT2
-
 Vernicia fordii
2.3.1.20 DGAT2
-
 Brassica napus
2.3.1.20 DGAT2
-
 Thraustochytrium aureum
2.3.1.20 DGAT2
-
 Triadica sebifera
2.3.1.20 DGAT2
-
 Caenorhabditis elegans
2.3.1.20 DGAT2
-
 Ricinus communis
2.3.1.20 DGAT2
-
 Arabidopsis thaliana
2.3.1.20 DGAT2-1
-
 Linum usitatissimum
2.3.1.20 DGAT2A
-
 Umbelopsis ramanniana
2.3.1.20 DGAT2b
-
 Umbelopsis ramanniana
2.3.1.20 DGAT3
-
 Phaeodactylum tricornutum
2.3.1.20 DGAT3
-
 Arachis hypogaea
2.3.1.20 DGAT3
-
 Arabidopsis thaliana
2.3.1.20 diacylglycerol O-acyltransferase 2
-
 Vernicia fordii
2.3.1.20 diacylglycerol O-acyltransferase 2
-
 Ricinus communis
2.3.1.20 More see also EC 2.3.1.75 Arabidopsis thaliana
2.3.1.158 At3g44830
-
 Arabidopsis thaliana
2.3.1.158 At5g13640
-
 Arabidopsis thaliana
2.3.1.158 AtPDAT1
-
 Arabidopsis thaliana
2.3.1.158 AtPDAT2
-
 Arabidopsis thaliana
2.3.1.158 LRO1
-
 Saccharomyces cerevisiae
2.3.1.158 PDAT
-
 Brassica napus
2.3.1.158 PDAT
-
 Ricinus communis
2.3.1.158 PDAT
-
 Linum usitatissimum
2.3.1.158 PDAT
-
 Crepis palaestina
2.3.1.158 PDAT
-
 Arabidopsis thaliana
2.3.1.158 PDAT
-
 Saccharomyces cerevisiae
2.3.1.158 PDAT
-
 Helianthus annuus
2.3.1.158 PDAT1
-
 Arabidopsis thaliana
2.3.1.158 PDAT2
-
 Arabidopsis thaliana
2.3.1.158 phospholipid:diacylglycerol acyltransferase
-
 Brassica napus
2.3.1.158 phospholipid:diacylglycerol acyltransferase
-
 Crepis palaestina
2.3.1.158 phospholipid:diacylglycerol acyltransferase
-
 Arabidopsis thaliana
2.3.1.158 phospholipid:diacylglycerol acyltransferase
-
 Saccharomyces cerevisiae
2.3.1.158 phospholipid:diacylglycerol acyltransferase
-
 Helianthus annuus
2.3.1.158 phospholipid:diacylglycerol acyltransferase
-
 Ricinus communis
2.3.1.158 YNR008w
-
 Saccharomyces cerevisiae

Expression

EC Number Organism Comment Expression
2.3.1.20 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
2.3.1.20 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
2.3.1.20 Zea mays activation of DGAT1 by a phenylalanine insertion in the maize (Zea mays) DGAT1 up
2.3.1.20 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
2.3.1.158 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
2.3.1.158 Crepis palaestina 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
2.3.1.158 Arabidopsis thaliana 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
2.3.1.158 Helianthus annuus 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
2.3.1.158 Ricinus communis 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
2.3.1.158 Saccharomyces cerevisiae the R2R3-type MYB96 transcription factor was 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

EC Number General Information Comment Organism
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 malfunction DGAT1 overexpression during seed development in Brassica napus decreases the penalty on seed oil content caused by drought Brassica napus
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 metabolism the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol Umbelopsis ramanniana
2.3.1.20 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
2.3.1.20 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
2.3.1.20 metabolism the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol Chlamydomonas reinhardtii
2.3.1.20 metabolism the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol Phaeodactylum tricornutum
2.3.1.20 metabolism the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol Brassica napus
2.3.1.20 metabolism the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol Thraustochytrium aureum
2.3.1.20 metabolism the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol Triadica sebifera
2.3.1.20 metabolism the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol Umbelopsis ramanniana
2.3.1.20 metabolism the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol Ricinus communis
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 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
2.3.1.20 physiological function regulation of the enzyme, overview Phaeodactylum tricornutum
2.3.1.20 physiological function regulation of the enzyme, overview Ricinus communis
2.3.1.20 physiological function regulation of the enzyme, overview Vernicia fordii
2.3.1.20 physiological function regulation of the enzyme, overview Arachis hypogaea
2.3.1.20 physiological function regulation of the enzyme, overview Glycine max
2.3.1.20 physiological function regulation of the enzyme, overview Nicotiana tabacum
2.3.1.20 physiological function regulation of the enzyme, overview Tropaeolum majus
2.3.1.20 physiological function regulation of the enzyme, overview Olea europaea
2.3.1.20 physiological function regulation of the enzyme, overview Euonymus alatus
2.3.1.20 physiological function regulation of the enzyme, overview Sesamum indicum
2.3.1.20 physiological function regulation of the enzyme, overview Cuphea avigera
2.3.1.20 physiological function regulation of the enzyme, overview Echium pitardii
2.3.1.20 physiological function regulation of the enzyme, overview Linum usitatissimum
2.3.1.20 physiological function regulation of the enzyme, overview Arabidopsis thaliana
2.3.1.20 physiological function regulation of the enzyme, overview Zea mays
2.3.1.20 physiological function regulation of the enzyme, overview Boechera stricta
2.3.1.20 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
2.3.1.158 evolution phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Helianthus annuus
2.3.1.158 evolution phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Ricinus communis
2.3.1.158 evolution phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Brassica napus
2.3.1.158 evolution phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Crepis palaestina
2.3.1.158 evolution two PDAT orthologues, AtPDAT1 and AtPDAT2, with 57% amino acid sequence similarity, are identified in Arabidopsis thaliana. Phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1 Arabidopsis thaliana
2.3.1.158 malfunction the removal of the putative N-terminal transmembrane domain (TMD) in Saccharomyces cerevisiae PDAT does not affect activity Saccharomyces cerevisiae
2.3.1.158 metabolism 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. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG Arabidopsis thaliana
2.3.1.158 metabolism 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. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG Brassica napus
2.3.1.158 metabolism 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. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG Crepis palaestina
2.3.1.158 metabolism 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. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG Arabidopsis thaliana
2.3.1.158 metabolism 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. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG Helianthus annuus
2.3.1.158 metabolism 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. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG Ricinus communis
2.3.1.158 metabolism 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. PDAT and DGAT2 are the major contributors to TAG biosynthesis and their relative contributions were dependent on the yeast growth stage Saccharomyces cerevisiae
2.3.1.158 metabolism the enzyme catalyzes the acyl-CoA-independent synthesis of triacylglycerol using membrane glycerolipids as acyl donors Saccharomyces cerevisiae
2.3.1.158 metabolism the enzyme is a major determinant of triacylglycerol biosynthesis at the exponential growth stage. Overexpression of AtPDAT1 results in no effects on the fatty-acid and lipid composition, despite the fact that increased PDAT activity is observed in microsomes prepared from AtPDAT1 Arabidopsis overexpressor lines. PDAT1 is a dominant determinant in Arabidopsis seed triacylglycerol biosynthesis in the absence of DGAT1 activity Arabidopsis thaliana
2.3.1.158 additional information comparison to human enzyme LCAT (EC 2.3.1.43) Saccharomyces cerevisiae
2.3.1.158 physiological function triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine Brassica napus
2.3.1.158 physiological function triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine Crepis palaestina
2.3.1.158 physiological function triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine Arabidopsis thaliana
2.3.1.158 physiological function triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine Saccharomyces cerevisiae
2.3.1.158 physiological function triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine Helianthus annuus
2.3.1.158 physiological function triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine Ricinus communis