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Information on EC 2.3.1.20 - diacylglycerol O-acyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q93ZR6
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EC Tree
2.3.1.20 diacylglycerol O-acyltransferaseIUBMB Comments
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
Specify your search results
Word Map
- 2.3.1.20
- triacylglycerols
- triglyceride
- adipose
- milk
- acyl-coas
- lipoprotein
- obesity
- cholesterol
- droplet
- cattle
- adipocytes
- lipase
- steatosis
-
lipogenesis
-
lipogenic
-
high-fat
-
holstein
-
oleic
-
dairy
-
proliferator-activated
- phosphatidate
- glycerolipids
-
lipolysis
-
oleaginous
- glycerol-3-phosphate
- chylomicron
-
biodiesel
-
srebf1
-
oilseed
-
lipotoxicity
- stearoyl-coa
- acaca
- camelina
- industry
-
insig1
- biofuel production
-
oleosins
-
cholinephosphotransferase
- elovl6
- drug development
-
triacylglyceride
-
holstein-friesian
- sn-1,2-diacylglycerols
- analysis
- glycerolphosphate
- oleoyl-coa
- protein-1c
-
lipin
- lpaat
-
ricinoleic
- medicine
- baylyi
- chylomicronemia
- biotechnology
-
steryl
-
kennedy
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
dgat1, dgat2, dgat, diacylglycerol acyltransferase, diacylglycerol acyltransferase 1, diacylglycerol o-acyltransferase, dgat-1, monoacylglycerol acyltransferase, acyl-coa:diacylglycerol acyltransferase, diacylglycerol acyltransferase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
wax ester synthase/acyl-coenzyme A:diacylglycerol acyltransferase WSD1
bifunctional enzyme
1,2-diacylglycerol acyltransferase
-
-
-
-
acyl-CoA:1,2-dioleoyl-sn-glycerol acyltransferase
-
-
-
-
acyltransferase, diacylglycerol
-
-
-
-
DGAT
DGAT1
DGAT1A
-
-
-
-
DGAT2
DGAT2A
-
-
-
-
diacylglycerol acyltransferase
diglyceride acyltransferase
-
-
-
-
diglyceride O-acyltransferase
-
-
-
-
palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase
-
-
-
-
DGAT
-
-
-
-
DGAT1
-
-
-
-
DGAT2
-
-
-
-
diacylglycerol acyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:1,2-diacyl-sn-glycerol O-acyltransferase
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
CAS REGISTRY NUMBER
COMMENTARY
9029-98-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
palmitoyl-CoA + 1,2-dipalmitoylglycerol
CoA + tripalmitin
approximately 10fold lower level of diacylglycerol acyltransferase activity
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
?
caproyl-CoA + 1,2-dicaproyl-sn-glycerol
CoA + tricaproylglycerol
-
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
-
?
palmitoleoyl-CoA + 1,2-dipalmitoleoyl-sn-glycerol
CoA + tripalmitoleoylglycerol
-
preferred substrate for isoform DGAT2
-
-
?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + tripalmitoylglycerol
-
preferred substrate for isoform DGAT1
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
role in leaf metabolism, overview
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
additional information
?
-
rate of activity is highly dependent on acyl composition with highest activities for acyl groups containing several double bonds, epoxy, or hydroxy groups. Enzyme uses both sn-positions of phosphatidylcholine with 3fold preference for sn-2 position
-
-
?
additional information
?
-
-
bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
-
-
-
additional information
?
-
bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
-
-
-
additional information
?
-
bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
-
-
-
additional information
?
-
bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
role in leaf metabolism, overview
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
effectivity of detergents used in in vitro assays, overview
-
additional information
effectivity of detergents used in in vitro assays, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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
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
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
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
additional information
-
isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues
additional information
isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues
additional information
isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues
additional information
isozyme AtDGAT2 is expressed at a lower level in seeds compared to other tissues
additional information
temporal expression pattern of DGAT1, overview. DGAT1 expression is upregulated from 3 to 96 h upon cold exposure, with levels increasing 197 and 43fold in the shoots and the roots, respectively, at 96 h
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
thylakoid and envelope membranes, not in the stroma
embedded in the membrane lipid bilayer
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 genes is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
physiological function
role of the DGAT3 and WS/DGAT genes in lipid accumulation during seed development, overview
evolution
malfunction
metabolism
physiological function
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 genes is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
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)
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
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
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
malfunction
with or without cold acclimation, the dgat1 mutants exhibit higher sensitivity upon freezing exposure compared with the wild-type. Under cold conditions, the dgat1 mutants show reduced expression of C-REPEAT/DRE binding factor 2 and its regulons, which are essential for the acquisition of cold tolerance. Lipid profiling reveals that freezing significantly increases the levels of phosphatidic acid (PA) and diacylglycerol (DAG) while decreasing triacylglycerol (TAG) in the rosettes of dgat1 mutant plants. During freezing stress, the accumulation of PA in dgat1 mutant plants stimulates NADPH oxidase activity and enhances RbohD-dependent hydrogen peroxide production compared with the wild-type. Moreover, the cold-inducible transcripts of DGK2, DGK3, and DGK5, encoding diacylglycerol kinases, are significantly more upregulated in the dgat1 mutants than in the wild-type during cold stress. H2O2 and salicylic acid accumulate in the dgat1 mutants upon exposure to freezing temperatures. The dgat1 mutants show decreased expression of CBF2 and its target genes. Comparisons of lipid compositions and contents in wild-type and mutant leaves and seeds, phenotypes, detailed overview
metabolism
DGAT1 enzyme is evidenced to be a major determining factor for oil quantity and fatty acid composition of seed oils in several crops
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
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
metabolism
diacylglycerol acyltransferase and diacylglycerol kinase modulate triacylglycerol and phosphatidic acid production in the plant response to freezing stress
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
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
physiological function
regulation of the enzyme, overview
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
physiological function
role of the DGAT3 and WS/DGAT genes in lipid accumulation during seed development, overview
physiological function
the conversion of diacylglycerol (DAG) to triacylglycerol (TAG) by DGAT1 is critical for plant freezing tolerance, acting by balancing TAG and phosphatidic acid (PA) production in Arabidopsis thaliana
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). WSD1_ARATH
481
1
54417
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S205A
site-directed mutagenesis, mutant DGAT1m is less effective compared to wild-type in increasing seed mass, seed size and seed yield in the transgenic Camelina sativa plants when coexpressed with yeast GPD1
additional information
additional information
-
a recombinant acyl-CoA binding protein increased the activity of Arabidopsis thaliana DGAT1 expressed in insect cell culture by up to 70%, overexpression of AtDGAT1 cDNA from Arabidopsis does not complement the knocked-out acyl-CoA:cholesterol acyltransferases, ACAT, EC 2.3.1.26, in a yeast double-mutant
additional information
a recombinant acyl-CoA binding protein increased the activity of Arabidopsis thaliana DGAT1 expressed in insect cell culture by up to 70%, overexpression of AtDGAT1 cDNA from Arabidopsis does not complement the knocked-out acyl-CoA:cholesterol acyltransferases, ACAT, EC 2.3.1.26, in a yeast double-mutant
additional information
engineering transgenic Camelina sativa plants for enhanced oil and seed yields by combining heterologous expression of Arabidopsis thaliana diacylglycerol acyltransferase1 (DGAT1) and Saccharomyces cerevisiae cytosolic glycerol-3-phosphate dehydrogenase (GPD1) genes under the control of seed-specific promoters. Plants co-expressing DGAT1 and GPD1 exhibit up to 13% higher seed oil content and up to 52% increase in seed mass compared to wild-type plants. Further, DGAT1- and GDP1-coexpressing lines show significantly higher seed and oil yields on a dry weight basis than the wild-type controls or plants expressing DGAT1 and GPD1 alone. The oil harvest index (g oil per g total dry matter) for DGTA1- and GPD1-co-expressing lines is almost twofold higher as compared to wild-type and the lines expressing DGAT1 and GPD1 alone. Evaluation of the effect of stacking the two genes on achieving a synergistic effect on the flux through the TAG synthesis pathway, and thereby further increasing the oil yield. GDP1 and DGAT1 overexpression has no effect on seed germination and early seedling growth
additional information
-
engineering transgenic Camelina sativa plants for enhanced oil and seed yields by combining heterologous expression of Arabidopsis thaliana diacylglycerol acyltransferase1 (DGAT1) and Saccharomyces cerevisiae cytosolic glycerol-3-phosphate dehydrogenase (GPD1) genes under the control of seed-specific promoters. Plants co-expressing DGAT1 and GPD1 exhibit up to 13% higher seed oil content and up to 52% increase in seed mass compared to wild-type plants. Further, DGAT1- and GDP1-coexpressing lines show significantly higher seed and oil yields on a dry weight basis than the wild-type controls or plants expressing DGAT1 and GPD1 alone. The oil harvest index (g oil per g total dry matter) for DGTA1- and GPD1-co-expressing lines is almost twofold higher as compared to wild-type and the lines expressing DGAT1 and GPD1 alone. Evaluation of the effect of stacking the two genes on achieving a synergistic effect on the flux through the TAG synthesis pathway, and thereby further increasing the oil yield. GDP1 and DGAT1 overexpression has no effect on seed germination and early seedling growth
additional information
generation of plant mutant dgat1-1 (CS3861) by methanesulfonate, and of T-DNA insertional mutant dgat1-2 (SALK_039456), phenotypes, comparison of lipid compositions and contents in wild-type and mutant leaves and seeds, detailed overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene WSD1, Arabidopsis thaliana contains 11 WS/DGAT genes, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic tree
DGAT1, a single copy gene, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional overexpression in tobacco plants
gene DGAT1, seed-specific co-overexpression of AtDGAT1 and ScGPD1 codon-optimized genes in Camelina sativa cv. Suneson, increasing seed mass, seed size and seed yield in the transgenic plants, recombinant co-expression also with mutant DGATm, the glycinin promoter from Glycine max is selected to drive the expression of DGAT1, transfection using the Agrobacterium tumefaciens strain GV3101 method. Quantitative real-time PCR enzyme expression analysis and phenotypes, overview
gene DGAT1A, recombinant expression of isozyme AtDGAT1A in Saccharomyces cerevisiae strain INVSc1 microsomes, very low expression level, lipid analyses, overview
gene DGAT3, Arabidopsis thaliana contains a single DGAT3 gene, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic tree
isoform DGAT2 is expressed in Saccharomyces cerevisiae mutant strain H1246
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
DGAT1 expression is upregulated from 3 to 96 h upon cold exposure, with levels increasing 197 and 43fold in the shoots and the roots, respectively, at 96 h
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
combining the overexpression of TAG biosynthetic genes, DGAT1 and GPD1, appears to be a positive strategy to achieve a synergistic effect on the flux through the TAG synthesis pathway, and thereby further increase the oil yield of Camelina sativa, application of genetic engineering approaches to boost the metabolic flux of carbon into seed oils
biotechnology
biotechnology
combining the overexpression of TAG biosynthetic genes, DGAT1 and GPD1, appears to be a positive strategy to achieve a synergistic effect on the flux through the TAG synthesis pathway, and thereby further increase the oil yield of Camelina sativa, application of genetic engineering approaches to boost the metabolic flux of carbon into seed oils
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bouvier-Nave, P.; Benveniste, P.; Noiriel, A.; Schaller, H.
Expression in yeast of an acyl-CoA:diacylglycerol acyltransferase cDNA from Caenorhabditis elegans
Biochem. Soc. Trans.
28
692-695
2000
Arabidopsis thaliana, Caenorhabditis elegans, Nicotiana tabacum
Hobbs, D.H.; Hills, M.J.
Expression and characterization of diacylglycerol acyltransferase from Arabidopsis thaliana in insect cell cultures
Biochem. Soc. Trans.
28
687-689
2000
Arabidopsis thaliana
Routaboul, J.M.; Benning, C.; Bechtold, N.; Caboche, M.; Lepiniec, L.
The TAG1 locus of Arabidopsis encodes for a diacylglycerol acyltransferase
Plant Physiol. Biochem.
37
831-840
1999
Arabidopsis thaliana
Stahl, U.; Carlsson, A.S.; Lenman, M.; Dahlqvist, A.; Huang, B.; Banas, W.; Banas, A.; Stymne, S.
Cloning and functional characterization of a phospholipid:diacylglycerol acyltransferase from Arabidopsis
Plant Physiol.
135
1324-1335
2004
Arabidopsis thaliana (Q9FNA9)
Lung, S.C.; Weselake, R.J.
Diacylglycerol acyltransferase: a key mediator of plant triacylglycerol synthesis
Lipids
41
1073-1088
2006
Acinetobacter calcoaceticus, Arabidopsis thaliana, Arabidopsis thaliana (Q9SLD2), Arachis hypogaea, Brassica napus, Brassica napus (Q9XGR5), Brassica napus (Q9XGV4), Carthamus tinctorius, Ricinus communis, Ricinus communis (Q67C39), Glycine max, Umbelopsis ramanniana, Mus musculus, Mus musculus (Q9Z2A7), Olea europaea, Rattus norvegicus, Spinacia oleracea, Zea mays, Cuphea sp., Nicotiana tabacum (Q9SEG9)
Li, F.; Wu, X.; Lam, P.; Bird, D.; Zheng, H.; Samuels, L.; Jetter, R.; Kunst, L.
Identification of the wax ester synthase/acyl-coenzyme A: diacylglycerol acyltransferase WSD1 required for stem wax ester biosynthesis in Arabidopsis
Plant Physiol.
148
97-107
2008
Arabidopsis thaliana (Q93ZR6)
Dauk, M.; Lam, P.; Smith, M.
The role of diacylglycerol acyltransferase-1 and phospholipid: diacylglycerol acyltransferase-1 and -2 in the incorporation of hydroxy fatty acids into triacylglycerol in Arabidopsis thaliana expressing a castor bean oleate 12-hydroxylase gene
Botany
87
552-560
2009
Arabidopsis thaliana
-
Zhou, X.R.; Shrestha, P.; Yin, F.; Petrie, J.R.; Singh, S.P.
AtDGAT2 is a functional acyl-CoA:diacylglycerol acyltransferase and displays different acyl-CoA substrate preferences than AtDGAT1
FEBS Lett.
587
2371-2376
2013
Arabidopsis thaliana
Ayme, L.; Baud, S.; Dubreucq, B.; Joffre, F.; Chardot, T.
Function and localization of the Arabidopsis thaliana diacylglycerol acyltransferase DGAT2 expressed in yeast
PLoS ONE
9
e92237
2014
Arabidopsis thaliana
Turchetto-Zolet, A.; Christoff, A.; Kulcheski, F.; Loss-Morais, G.; Margis, R.; Margis-Pinheiro, M.
Diversity and evolution of plant diacylglycerol acyltransferase (DGATs) unveiled by phylogenetic, gene structure and expression analyses
Genet. Mol. Biol.
39
524-538
2016
Glycine max (I1L4P1), Glycine max (I1MRZ6), Glycine max (K7LZ65), Arabidopsis thaliana (Q93ZR6), Arabidopsis thaliana (Q9C5W0)
Hatanaka, T.; Serson, W.; Li, R.; Armstrong, P.; Yu, K.; Pfeiffer, T.; Li, X.L.; Hildebrand, D.
A Vernonia diacylglycerol acyltransferase can increase renewable oil production
J. Agric. Food Chem.
64
7188-7194
2016
Vernonia galamensis (B1NM15), Vernonia galamensis (B1NM16), Vernonia galamensis, Glycine max (I1MSF2), Glycine max (Q5GKZ7), Glycine max, Arabidopsis thaliana (Q9SLD2), Euphorbia lagascae (T2HV99)
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
Lipids
53
663-688
2018
Arabidopsis thaliana, Arabidopsis thaliana (Q9ASU1), Arabidopsis thaliana (Q9C5W0), Arabidopsis thaliana (Q9SLD2), Arachis hypogaea, Arachis hypogaea (A0A0M3SGK9), Arachis hypogaea (Q2KP14), Chlamydomonas reinhardtii, Linum usitatissimum, Linum usitatissimum (V5LV83), Linum usitatissimum (V5LV86), Nicotiana tabacum, Nicotiana tabacum (Q9SEG9), Phaeodactylum tricornutum, Tropaeolum majus, Tropaeolum majus (Q8RX96), Triadica sebifera, Boechera stricta, Cuphea avigera var. pulcherrima (A0A193DVK9), Cuphea avigera (A0A193DVK9), Ricinus communis (A1A442), Ricinus communis (Q67C39), Zea mays (B0LF77), Echium pitardii (D9U3F8), Glycine max (I1MSF2), Glycine max (Q5GKZ7), Brassica napus (K9LL63), Brassica napus (Q9XGR5), Brassica napus (Q9XGV4), Sesamum indicum (M1E7W9), Vernicia fordii (Q0QJH9), Vernicia fordii (Q0QJI1), Euonymus alatus (Q5UEM2), Olea europaea (Q6ED63), Umbelopsis ramanniana (Q96UY1), Umbelopsis ramanniana (Q96UY2), Caenorhabditis elegans (Q9XUW0), Mus musculus (Q9Z2A7), Thraustochytrium aureum (R9QY77)
Chhikara, S.; Abdullah, H.M.; Akbari, P.; Schnell, D.; Dhankher, O.P.
Engineering Camelina sativa (L.) Crantz for enhanced oil and seed yields by combining diacylglycerol acyltransferase1 and glycerol-3-phosphate dehydrogenase expression
Plant Biotechnol. J.
16
1034-1045
2018
Arabidopsis thaliana (Q9SLD2), Arabidopsis thaliana
Tan, W.J.; Yang, Y.C.; Zhou, Y.; Huang, L.P.; Xu, L.; Chen, Q.F.; Yu, L.J.; Xiao, S.
Diacylglycerol acyltransferase and diacylglycerol kinase modulate triacylglycerol and phosphatidic acid production in the plant response to freezing stress
Plant Physiol.
177
1303-1318
2018
Arabidopsis thaliana (Q9SLD2), Arabidopsis thaliana Col-0 (Q9SLD2)
EXTERNAL LINKS (specific for EC-Number 2.3.1.20)
Transporter Classification Database (TCDB): 2.A.50.4.1, 2.A.50.4.10
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