Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOATs). The DGAT1 family is highly conserved. DGAT1 possesses a very hydrophilic N-terminal region corresponding to about the first 100 residues, which is followed by eight to ten predicted transmembrane segments
evolution
distinct evolutionary origin of Thraustochytrium roseum bifunctional wax ester synthase/acyl-CoA diacylglycerol acyltransferases (WS/DGATs) from that of plant and bacterial WS/DGATs. Both TrWSD4 and TrWSD5 contain the conserved acyltransferase active-site motif (HHXXXDG), whose first histidine residue is substituted to serine and aspartate, respectively
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
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
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 gene is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
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
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 gene is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
evolution
enzyme MtDGAT1 belongs to the DGAT1 family
evolution
genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2 (isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3), and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
evolution
genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2, i.e. isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3, and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
evolution
in Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGA T3s
evolution
in Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGAT3s
evolution
phylogeny of these BnaDGAT1 gene forms. Two clades of DGAT1, which appear to have diverged relatively early in Brassicaceae's history, differ in preference for linoleoyl (18:2DELTA9cis12cis, i.e. 18:2-CoA). Phylogenetic analysis
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)
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)
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). 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). 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). 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). 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). 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). 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). 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). 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). 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). 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). 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). 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). 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). 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
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
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
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
evolution
the evolutionary and sequence analyses revealed that CzDGAT1 and other green microalgal DGAT1 are closely related to the plant DGAT1 clade. But algal DGAT1 may have different evolutionary and structural features from plant and animal DGAT1 with respect to the hydrophilic N-terminal domain. This domain is predicted to be present in a less disordered state in CzDGAT1 than that of animal/plant DGAT1. The two isoforms of DGAT1 from the green microalga Chromochloris zofingiensis have very distinct features. They share 39.9% amino acid pairwise identity and have very different lengths mainly attributable to the variable N-terminal regions
evolution
the genome of oleaginous yeast Rhodosporidium toruloides contains two putative DGAT genes, RtDGATa and RtDGATb, which share little conserved amino acid coding sequence with each other. Phylogeny tree analysis shows that RtDGATa belongs to DGAT1 family and RtDGATb belongs to DGAT2 family
evolution
the major triglycerol synthesizing enzyme in Yarrowia lipolytica is Dga1p which belongs to the DGAT2 family
evolution
the principal activity of DGATs has been defined as a single-function enzyme catalyzing the esterification of diacylglycerol with acyl-CoA. A dual-function PtWS/DGAT associated with diatom Phaeodactylum tricornutum is discovered in the current study. Distinctive to documented microalgal DGAT types, PtWS/DGAT exhibits activities of both a wax ester synthase (WS) and a DGAT. WS/DGATs are broadly distributed in microalgae, with different topology and phylogeny from those of DGAT1s, DGAT2s, and DGAT3s. In Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGA T3s
evolution
Thermomonospora curvata acyltransferase ACY99349 belongs to the WS/DGAT family. tDGAT contains all the conserved motifs characteristic of WS/DGAT, mainly the catalytic site 140HHaavDG146, motif I 118PLW120, and motif II 281ND282. Like in other acyl-CoA-dependent acyltransferases the catalytic motif 140HHaavDG146, in the N-terminal domain of tDGAT, is predicted to be located in the hydrophobic pocket or channel that restricts the accessibility of hydrophilic substrates
evolution
-
the genome of oleaginous yeast Rhodosporidium toruloides contains two putative DGAT genes, RtDGATa and RtDGATb, which share little conserved amino acid coding sequence with each other. Phylogeny tree analysis shows that RtDGATa belongs to DGAT1 family and RtDGATb belongs to DGAT2 family
-
evolution
-
the major triglycerol synthesizing enzyme in Yarrowia lipolytica is Dga1p which belongs to the DGAT2 family
-
evolution
-
the major triglycerol synthesizing enzyme in Yarrowia lipolytica is Dga1p which belongs to the DGAT2 family
-
evolution
-
genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2, i.e. isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3, and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
-
evolution
-
genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2 (isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3), and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
-
evolution
-
Thermomonospora curvata acyltransferase ACY99349 belongs to the WS/DGAT family. tDGAT contains all the conserved motifs characteristic of WS/DGAT, mainly the catalytic site 140HHaavDG146, motif I 118PLW120, and motif II 281ND282. Like in other acyl-CoA-dependent acyltransferases the catalytic motif 140HHaavDG146, in the N-terminal domain of tDGAT, is predicted to be located in the hydrophobic pocket or channel that restricts the accessibility of hydrophilic substrates
-
evolution
-
distinct evolutionary origin of Thraustochytrium roseum bifunctional wax ester synthase/acyl-CoA diacylglycerol acyltransferases (WS/DGATs) from that of plant and bacterial WS/DGATs. Both TrWSD4 and TrWSD5 contain the conserved acyltransferase active-site motif (HHXXXDG), whose first histidine residue is substituted to serine and aspartate, respectively
-
malfunction
-
enzyme-deficient mice show no effect on retinal anatomy or the ultrastructure of photoreceptor outer-segments. Enzyme loss affects retinyl-ester synthesis and total acyl-coenzyme A:retinol acyl-transferase activityin the eye
malfunction
-
Isoform DGAT1 inactivation promotes large lipid droplet formation. Inhibition of isoform DGAT2 augments fatty acid oxidation, whereas inhibition of DGAT1 increases triacylglycerol secretion. Triacylglycerol secretion is significantly reduced on DGAT2 inhibition without altering extracellular apolipoprotein B levels
malfunction
a Rv3371 deletion mutant of Mtb shows impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant shows reduced formation of TAG containing extracellular vesicles
malfunction
although the N-terminal domain of algal DGAT1 is not necessary for acyltransferase activity of CzDGAT1, its removal leads to huge decreases in CzDGAT1 enzyme activity, which cannot be restored by fusion with an acyl-CoA binding protein AtACBP6 from Arabidopsis thaliana. Replacement of the N-terminal region by ACBP in CzDGAT1 (ACBP-fused CzDGAT1107-550) is not able to restore or improve the enzyme activity suggesting that the N-terminus may function as a regulatory domain rather than as an acyl-CoA binding site
malfunction
BnaDGAT161-501 and BnaDGAT181-501 exhibit higher normalized specific activity compared with the full-length enzyme. Despite the lower production level of BnaDGAT161-501 and BnaDGAT181-501, these enzyme forms are able to generate TAG amounting to about 60% of the total triacylglycerol (TAG) produced by the full-length enzyme in situ. Mutant BnaDGAT1114-501, which is devoid of the entire N-terminal domain, is about 10fold less active than the full-length enzyme. The affinity of BnaDGAT1114-501 for acyl-CoA is much lower than that of the full-length BnaDGAT1 or BnaDGAT181-501. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site
malfunction
calnexin-deficient mouse embryonic fibroblasts have reduced intracellular triacylglycerol levels and fewer large lipid droplets
malfunction
DGAT1 overexpression during seed development in Brassica napus decreases the penalty on seed oil content caused by drought
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
in vivo knockdown of CrDGTT1, CrDGTT2 or CrDGTT3 results in 20-35% decreases in TAG content and a reduction of specific TAG fatty acids, in agreement with the findings of the in vitro assay and fatty acid feeding test
malfunction
inactivation of DGAT1 or DGAT2 in adult mouse heart results in a moderate suppression of triglyceride (TG) synthesis and turnover. Partial inhibition of DGAT activity increases cardiac fatty acid oxidation without affecting PPARalpha signaling, myocardial energetics or contractile function. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function
malfunction
inactivation of DGAT1 or DGAT2 in adult mouse heart results in a moderate suppression of triglyceride (TG) synthesis and turnover. Partial inhibition of DGAT activity increases cardiac fatty acid oxidation without affecting PPARalpha signaling, myocardial energetics or contractile function. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function. Triglyceride storage is unaffected in DGAT1 inducible knockout (iKO) mice
malfunction
overexpression of PtWS/DGAT in the diatom results in increased levels of total lipids (TL) and triacylglycerol (TAG) regardless of nitrogen availability
malfunction
overexpression of YlDGA2 in a Q4 context under neosynthesis conditions causes the formation of large lipid bodies (LBs). DGAT overexpression affects LB segregation
malfunction
-
phenotypic analysis of thienopyrrole (CT2) inhibitor treated cells, overview
malfunction
the overexpression of YlDGA1 generates smaller but more numerous lipid bodies (LBs), a phenotype which can be enhanced by increasing the copy number of the overexpressed gene. DGAT overexpression affects LB segregation
malfunction
-
the respective gene, atfG25, is inactivated in Streptomyces sp. strain G25, cells of the insertion mutant still exhibit DGAT activity and are able to store TAG, albeit in lower quantities and at lower rates than the wild-type strain
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
malfunction
-
the overexpression of YlDGA1 generates smaller but more numerous lipid bodies (LBs), a phenotype which can be enhanced by increasing the copy number of the overexpressed gene. DGAT overexpression affects LB segregation
-
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
-
malfunction
-
a Rv3371 deletion mutant of Mtb shows impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant shows reduced formation of TAG containing extracellular vesicles
-
malfunction
-
a Rv3371 deletion mutant of Mtb shows impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant shows reduced formation of TAG containing extracellular vesicles
-
malfunction
-
the overexpression of YlDGA1 generates smaller but more numerous lipid bodies (LBs), a phenotype which can be enhanced by increasing the copy number of the overexpressed gene. DGAT overexpression affects LB segregation
-
metabolism
the enzyme is responsible for neutral lipid biosynthesis
metabolism
-
the triacylglycerol pool generated by DGAT1 is preferentially used for supplying substrates for oxidation, whereas DGAt2-derived triacylglycerol is more favored for secretion
metabolism
acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis
metabolism
acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis. PtDGAT2B gene may contribute more to TAG synthesis in the early stage than during the later stages
metabolism
acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis. PtDGATX gene may contribute more to TAG synthesis in the later stage than during the earlier stages
metabolism
DGAT is considered as rate-limiting enzyme of TAG synthesis and accumulation in animals, plants and microbes
metabolism
DGAT-2 atalyzes the final step of triacylglycerol (TG) biosynthesis
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 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 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 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 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 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 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 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 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 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 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 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 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 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 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
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
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 (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 (DGAT) catalyzes the last and final committed step of the TAG biosynthesis pathway and this is the rate-limiting step for lipid accumulation in plants
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last step of the acyl-CoA-dependent triacylglycerol (TAG) biosynthesis and appears to represent a bottleneck in algal TAG formation. In Haematococcus pluvialis, the fatty acid composition of total lipids and TAG is changed when the algae cells are subjected to light stress, in which 16:0, 18:1, and 18:2 increase with the concomitant decreases in 18:3
metabolism
diacylglycerol acyltransferase 1 (DGAT1) catalyzes the final and committed step in the Kennedy pathway for triacylglycerol (TAG) biosynthesis
metabolism
diacylglycerol acyltransferase and diacylglycerol kinase modulate triacylglycerol and phosphatidic acid production in the plant response to freezing stress
metabolism
in the oleaginous yeast Yarrowia lipolytica, the diacylglycerol acyltransferases (DGATs) are major factors for triacylglycerol (TAG) synthesis
metabolism
seed-specific CpuDGAT1 is associated with medium-chain fatty acid metabolism
metabolism
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol
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
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
metabolism
-
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
-
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
-
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
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
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
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
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
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
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
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
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
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
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
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
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
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
metabolism
-
the final step in triacylglycerol (TAG) biosynthesis is catalyzed by diacylglycerol acyltransferase (DGAT)
metabolism
-
the isozyme of DGAT in Cyperus esculentus are involved in the triacylglycerol (TAG) biosynthesis
metabolism
the last step in triglyceride (TG) synthesis is catalyzed by diacylglycerol:acyltransferase (DGAT) which esterifies the diacylglycerol with a fatty acid
metabolism
-
the primary metabolic enzyme DGAT1 catalyzes the final step in assembly of triacylglycerol (TAG) by acyl transfer from acyl-CoA to diacylglycerol
metabolism
-
type 2 diacylglycerol acyltransferase (DGAT2) is one of the key enzymes involved in triacylglycerol (TAG) biosynthesis
metabolism
-
in the oleaginous yeast Yarrowia lipolytica, the diacylglycerol acyltransferases (DGATs) are major factors for triacylglycerol (TAG) synthesis
-
metabolism
-
diacylglycerol acyltransferase (DGAT) catalyzes the last step of the acyl-CoA-dependent triacylglycerol (TAG) biosynthesis and appears to represent a bottleneck in algal TAG formation. In Haematococcus pluvialis, the fatty acid composition of total lipids and TAG is changed when the algae cells are subjected to light stress, in which 16:0, 18:1, and 18:2 increase with the concomitant decreases in 18:3
-
metabolism
-
diacylglycerol acyltransferase and diacylglycerol kinase modulate triacylglycerol and phosphatidic acid production in the plant response to freezing stress
-
metabolism
-
diacylglycerol acyltransferase (DGAT) catalyzes the last and final committed step of the TAG biosynthesis pathway and this is the rate-limiting step for lipid accumulation in plants
-
metabolism
-
in the oleaginous yeast Yarrowia lipolytica, the diacylglycerol acyltransferases (DGATs) are major factors for triacylglycerol (TAG) synthesis
-
metabolism
-
DGAT is considered as rate-limiting enzyme of TAG synthesis and accumulation in animals, plants and microbes
-
physiological function
enzyme makes a major contribution to triacylglycerol synthesis via an acyl-CoA-dependent mechanism and is not involved in steryl ester synthesis
physiological function
in isoforms dgat1, dgat2, dgat1/dgat2 double mutant and dgat1/dgat2/phospholipid:diacylglycerol acyltransferase triple mutant the total lipid% dry cell weight as a percentage of the wild-type strain is 57%, 36%, 18% and 13%, respectively
physiological function
inhibition of isoform DGAT1 affects equally the incorporation of glycerol and exogenous preformed oleate into cellular and secreted triacylglycerol. Data indicate that isoform DGAT2 acts upstream of isoform DGAT1, and DGAT1 functions in the re-esterification of partial glycerides generated by intracellular lipolysis, using preformed fatty acids
physiological function
isoform DGAT2 activity accounts for a modest fraction of less than 20% of overall cellular DGAT activity. Inhibition of DGAT2 activity specifically inhibits and is rate-limiting for the incorporation of de novo synthesized fatty acids and of glycerol into cellular and secreted triglyceride to a much greater extent than it affects the incorporation of exogenously added oleate. Isoform DGAT2 acts upstream of isoform DGAT1, largely determines the rate of de novo synthesis of triglyceride, and uses nascent diacylglycerol and de novo synthesized fatty acids as substrates
physiological function
overexpression of the enzyme gene in Saccharomyces cerevisiae leads to accumulation of full-length prtein in wild-type and accumulation of full-length protein and a N-terminally truncated protein in a snf2 disruption mutant, lacking a DNA-dependent ATPase that forms the SWI/SNF chromatin remodeling complex. Proteolytic cleavage at the N-terminal region is involved in enzyme activation in the snf2 disruptant, a major cleavage site lies between residues Lys29 and Ser30
physiological function
upon overexpression in Mycobacterium smegmatis mc2155, cell morphology is changed and the cells become grossly enlarged. A massive formation of lipid bodies and a change in lipid pattern is observed simultaneously
physiological function
-
the enzyme interacts with lipid droplets presumably to catalyze localized triacylglycerol synthesis for lipid droplet expansion
physiological function
analysis of functional and cellular nature of type 1 and type 2 DGATs from Lobosphaera incisa, with LiDGAT1 being a major contributor to the TAG pool. LiDGATs of type 2 might be in turn involved in the incorporation of unusual fatty acids into TAG and thus regulate the composition of TAG
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
DGAT1 appears to play a role in freezing and/or drought stress responses in Brassica napus. Regulation of the enzyme, overview
physiological function
-
DGAT1 confers freezing tolerance in plants by supporting SFR2 (sensitive-to-freezing2)-mediated remodeling of chloroplast membranes, recombinant overexpression of AtDGAT1 leads to increased freezing tolerance in seedlings
physiological function
DGAT2 catalyzes the formation of triacylglycerol (TG) using fatty acyl coenzyme A (CoA) and 1,2-diacylglycerol (DG) as substrates. TG is the major form of stored metabolic energy in eukaryotic organisms that is sequestered in the hydrophobic core of cytosolic lipid droplets until it is needed. DGAT-2 catalyzes TG synthesis for lipid droplet growth
physiological function
diacylglycerol acyltransferase (DGAT) is an acyl-CoA-dependent enzyme which converts diacylglycerol (DAG) to triacylglycerol (TAG)
physiological function
-
diacylglycerol acyltransferase 1 (DGAT1) is a key enzyme in the production of triacylglycerols
physiological function
diacylglycerol acyltransferase 1 (DGAT1) is an integral membrane enzyme catalyzing the final and committed step in the acylcoenzyme A (CoA)-dependent biosynthesis of triacylglycerol (TAG). Proposed model for BnaDGAT1 regulation involving the hydrophilic N-terminal domain (NTD), overview
physiological function
-
enzyme AtfG25 has an important, but not exclusive, role in triacylglycerol (TAG) biosynthesis in the Streptomyces sp. G25 isolate, suggesting the presence of alternative metabolic pathways for lipid accumulation
physiological function
intrinsic disorder in plant proteins has been reported to be essential for the stress response. An intrinsically disordered region (IDR) spanning the N-terminal cytosolic domain of the intramembrane enzyme diacylglycerol acyltransferase1 (DGAT1) from canola-type Brassica napus, has been identified. The IDR spans amino acid residues 1-80, while residues 81-113 have a folded structure. DGAT1 (EC 2.3.1.20) catalyzes the acyl-coenzyme A (CoA)-dependent acylation of sn-1, 2-diacylglycerol (DAG) to produce triacylglycerol (TAG) and CoA. TAG serves as an energy source for germination in plants, a component of edible oil. This enzyme has a substantial effect on carbon flux into seed oil
physiological function
isozyme GmDGAT1A may play a role in usual seed triacylglycerol (TAG) production. Isozymes GmDGAT1A and 2D are differentially regulated by jasmonate during insect and wounding responses and abscisic acid for cold and heat stress response, indicating their different functions in soybean stress responses
physiological function
isozyme GmDGAT2D plays a role in usual seed triacylglycerol (TAG) production and is also involved in other tissues in responses to environmental and hormonal cues. Isozymes GmDGAT1A and 2D are differentially regulated by jasmonate during insect and wounding responses and abscisic acid for cold and heat stress response, indicating their different functions in soybean stress responses. Ectopic expression of GmDGATs in soybean hairy roots promotes TAG accumulation
physiological function
isozymes CrDGTT1, CrDGTT2 and CrDGTT3 possess distinct specificities toward acyl CoAs and diacylglycerols, and may work in concert spatially and temporally to synthesize diverse triacylglycerol (TAG) species in Chlamydomonas reinhardtii
physiological function
isozymes CrDGTT1, CrDGTT2 and CrDGTT3 possess distinct specificities toward acyl CoAs and diacylglycerols, and may work in concert spatially and temporally to synthesize diverse triacylglycerol (TAG) species in Chlamydomonas reinhardtii. rDGTT1 is shown to prefer prokaryotic lipid substrates and probably resides in both the endoplasmic reticulum and chloroplast envelope, indicating its role in prokaryotic and eukaryotic TAG biosynthesis. Role of isozyme CrDGTT1 in TAG biosynthesis, overview
physiological function
regardless of N availability, PtWS/DGAT exhibits a DGAT activity with a preference on saturated fatty acids. PtWS/DGAT exhibits activities of both a wax ester synthase (WS, EC 2.3.1.75) and a diacylglycerol acyltransferase (DGAT, EC 2.3.1.20)
physiological function
-
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
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 diacylglycerol acyltransferase (DGAT) 1 and 2 in cardiac metabolism and function
physiological function
role of diacylglycerol acyltransferase (DGAT) 1 and 2 in cardiac metabolism and function. The two DGAT isoforms in the heart have partially redundant function
physiological function
role of the DGAT3 and WS/DGAT genes in lipid accumulation during seed development, overview
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
physiological function
the diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations during persistence. It is involved in the biosynthesis of triacylglycerol (TAG). TAG is important to mycobacteria both as cell envelope component and energy reservoir
physiological function
the expression of isozyme RtDGATa shows non-involvement in triacylglycerol (TAG) accumulation according to its mRNA expression level in Rhodosporidium toruloides
physiological function
the expression pattern of isozyme RtDGATb is related to the process of fatty acid biosynthesis, suggesting that RtDGATb plays an important role in lipid accumulation in Rhodosporidium toruloides
physiological function
the MaDGAT2 gene encodes diacylglycerol acyltransferase 2, which is involved in the biosynthesis of neutral lipids and formation of lipid particle
physiological function
the specialized diacylglycerol acyltransferase DGAT1 contributes to the extreme medium-chain fatty acid content of Cuphea seed oil
physiological function
the type 2 diacylglycerol acyltransferase accelerates the triacylglycerol biosynthesis in heterokont oleaginous microalga Nannochloropsis oceanica
physiological function
two bifunctional enzymes, TrWSD4 and TrWSD5, from the marine protist Thraustochytrium roseum show wax ester synthase/acyl-CoA:diacylglycerol acyltransferase activity catalyzing wax ester and triacylglycerol synthesis. The WS/DGAT shows both in vitro wax synthase (WS) and DGAT activity, it is characterized as unspecific acyltransferase accepting a broad range of acyl-CoAs and fatty alcohols as substrates for WS activity but displaying substrate preference for medium-chain acyl-CoAs. In vivo characterization shows that the WS/DGAT predominantly functions as wax synthase
physiological function
type I diacylglycerol acyltransferase (MtDGAT1) is involved in triacylglycerol (TAG) biosynthesis and may contribute to biochemical mechanisms determining the particular fatty acid composition of Macadamia oil. Major contribution of DGAT enzymes to TAG biosynthesis in seed plants
physiological function
-
the MaDGAT2 gene encodes diacylglycerol acyltransferase 2, which is involved in the biosynthesis of neutral lipids and formation of lipid particle
-
physiological function
-
the expression of isozyme RtDGATa shows non-involvement in triacylglycerol (TAG) accumulation according to its mRNA expression level in Rhodosporidium toruloides
-
physiological function
-
the expression pattern of isozyme RtDGATb is related to the process of fatty acid biosynthesis, suggesting that RtDGATb plays an important role in lipid accumulation in Rhodosporidium toruloides
-
physiological function
-
the type 2 diacylglycerol acyltransferase accelerates the triacylglycerol biosynthesis in heterokont oleaginous microalga Nannochloropsis oceanica
-
physiological function
-
in isoforms dgat1, dgat2, dgat1/dgat2 double mutant and dgat1/dgat2/phospholipid:diacylglycerol acyltransferase triple mutant the total lipid% dry cell weight as a percentage of the wild-type strain is 57%, 36%, 18% and 13%, respectively
-
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
-
physiological function
-
the diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations during persistence. It is involved in the biosynthesis of triacylglycerol (TAG). TAG is important to mycobacteria both as cell envelope component and energy reservoir
-
physiological function
-
upon overexpression in Mycobacterium smegmatis mc2155, cell morphology is changed and the cells become grossly enlarged. A massive formation of lipid bodies and a change in lipid pattern is observed simultaneously
-
physiological function
-
the diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations during persistence. It is involved in the biosynthesis of triacylglycerol (TAG). TAG is important to mycobacteria both as cell envelope component and energy reservoir
-
physiological function
-
analysis of functional and cellular nature of type 1 and type 2 DGATs from Lobosphaera incisa, with LiDGAT1 being a major contributor to the TAG pool. LiDGATs of type 2 might be in turn involved in the incorporation of unusual fatty acids into TAG and thus regulate the composition of TAG
-
physiological function
-
two bifunctional enzymes, TrWSD4 and TrWSD5, from the marine protist Thraustochytrium roseum show wax ester synthase/acyl-CoA:diacylglycerol acyltransferase activity catalyzing wax ester and triacylglycerol synthesis. The WS/DGAT shows both in vitro wax synthase (WS) and DGAT activity, it is characterized as unspecific acyltransferase accepting a broad range of acyl-CoAs and fatty alcohols as substrates for WS activity but displaying substrate preference for medium-chain acyl-CoAs. In vivo characterization shows that the WS/DGAT predominantly functions as wax synthase
-
additional information
-
comparison and analysis of functional motifs and evolutionary relationships of DGAT2s, protein-protein interaction analysis among CzDGAT2s, overview. N- and C-terminals are important for the enzyme activity of isozyme CzDGAT2C. Membrane yeast two-hybrid assay reveals a possible DGAT2 activity modulation via the formation of homodimer/heterodimer among different DGAT2 isoforms
additional information
comparison and analysis of functional motifs and evolutionary relationships of DGAT2s, protein-protein interaction analysis among CzDGAT2s, overview. N- and C-terminals are important for the enzyme activity of isozyme CzDGAT2C. Membrane yeast two-hybrid assay reveals a possible DGAT2 activity modulation via the formation of homodimer/heterodimer among different DGAT2 isoforms
additional information
comparison and analysis of functional motifs and evolutionary relationships of DGAT2s, protein-protein interaction analysis among CzDGAT2s, overview. N- and C-terminals are important for the enzyme activity of isozyme CzDGAT2C. Membrane yeast two-hybrid assay reveals a possible DGAT2 activity modulation via the formation of homodimer/heterodimer among different DGAT2 isoforms
additional information
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
-
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
-
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
determination of conformational heterogeneity in the N-terminal domain of DGAT1, disorder propensity for the full-length BnaDGAT11-501 sequence, overview. A small gain of secondary structure is induced by ligand binding. The cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites
additional information
-
determination of conformational heterogeneity in the N-terminal domain of DGAT1, disorder propensity for the full-length BnaDGAT11-501 sequence, overview. A small gain of secondary structure is induced by ligand binding. The cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites
additional information
DGAT1 enzymes may be regulated through allosteric interactions. The self-association properties of DGAT1 enzymes are consistent with the fact that most allosteric enzymes exhibit quaternary structure, identification of CoA/acyl-CoA binding site in the hydrophilic N-terminal domain and specific interactions involved in CoA recognition, and analysis of structure and function of the hydrophilic N-terminal domain of Brassica napus DGAT1, overview. This domain is found to have an intrinsically disordered region (IDR) and a folded section. IDRs are recognized as important regions in proteins due to their roles in cellular signaling and regulation. The highly disordered segment is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif. Isozyme BnaC.DGAT1.a also exhibits positive cooperativity. The involvement of the N-terminal domain in self-association may mediate positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. The BnaDGAT1 N-terminal domain is not necessary for catalysis but contributes to modulating activity. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site. The BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction. The BnaDGAT1 N-terminal Domain is structurally flexible. The allosteric site also is needed for acyl-CoA-mediated homotropic allosteric activation
additional information
-
DGAT1 enzymes may be regulated through allosteric interactions. The self-association properties of DGAT1 enzymes are consistent with the fact that most allosteric enzymes exhibit quaternary structure, identification of CoA/acyl-CoA binding site in the hydrophilic N-terminal domain and specific interactions involved in CoA recognition, and analysis of structure and function of the hydrophilic N-terminal domain of Brassica napus DGAT1, overview. This domain is found to have an intrinsically disordered region (IDR) and a folded section. IDRs are recognized as important regions in proteins due to their roles in cellular signaling and regulation. The highly disordered segment is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif. Isozyme BnaC.DGAT1.a also exhibits positive cooperativity. The involvement of the N-terminal domain in self-association may mediate positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. The BnaDGAT1 N-terminal domain is not necessary for catalysis but contributes to modulating activity. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site. The BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction. The BnaDGAT1 N-terminal Domain is structurally flexible. The allosteric site also is needed for acyl-CoA-mediated homotropic allosteric activation
additional information
DGAT2 is part of a high molecular weight (about 650 kD) complex. Calnexin, an endoplasmic reticulum chaperone, interacts with DGAT2. The interaction between calnexin and DGAT2 suggests that calnexin may play a role in lipid metabolism, including adipocyte differentiation. The subcellular localization and stability of DGAT2 are not altered by the absence of calnexin
additional information
-
DGAT2 is part of a high molecular weight (about 650 kD) complex. Calnexin, an endoplasmic reticulum chaperone, interacts with DGAT2. The interaction between calnexin and DGAT2 suggests that calnexin may play a role in lipid metabolism, including adipocyte differentiation. The subcellular localization and stability of DGAT2 are not altered by the absence of calnexin
additional information
fatty acid composition of high-oil lines and cultivar Jack wild-type soybean seed oil, overview
additional information
fatty acid composition of high-oil lines and cultivar Jack wild-type soybean seed oil, overview
additional information
-
fatty acid composition of high-oil lines and cultivar Jack wild-type soybean seed oil, overview
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
-
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-beta-D-maltopyranoside micelles is lipidated to form mixed micelles. The degree of mixed micelle fluidity appears to influence acyltransferase activity. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition indicating that PA facilitates the transition of the enzyme into the more active state. PA is a key effector modulating lipid homeostasis, in addition to its well recognized role in lipid signaling
additional information
-
purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-beta-D-maltopyranoside micelles is lipidated to form mixed micelles. The degree of mixed micelle fluidity appears to influence acyltransferase activity. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition indicating that PA facilitates the transition of the enzyme into the more active state. PA is a key effector modulating lipid homeostasis, in addition to its well recognized role in lipid signaling
additional information
quantification of triacylglycerol and analysis of fatty acid composition
additional information
quantification of triacylglycerol and analysis of fatty acid composition
additional information
-
quantification of triacylglycerol and analysis of fatty acid composition
additional information
relevant is the presence of the acyl-CoA binding signature R122-G141 close to residues R156-N161 that have been involved in the active site and a DAG/phorbol ester binding motif. Two amino acid changes, G155 and T152, are found in MtDGAT1 within the putative acyl-CoA binding domain, replacing the highly conserved Ala and Ser residues that might affect acyl specificity of the enzyme. A previously reported leucine zipper motif is also found
additional information
-
relevant is the presence of the acyl-CoA binding signature R122-G141 close to residues R156-N161 that have been involved in the active site and a DAG/phorbol ester binding motif. Two amino acid changes, G155 and T152, are found in MtDGAT1 within the putative acyl-CoA binding domain, replacing the highly conserved Ala and Ser residues that might affect acyl specificity of the enzyme. A previously reported leucine zipper motif is also found
additional information
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
-
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
-
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
-
the expression of DGAT1 is found to be highly cold responsive and correlated with the cold tolerance in Boechera stricta lines
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
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
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
additional information
the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
additional information
-
the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
additional information
three-dimensional model of the tDGAT protein, structure homology modeling
additional information
-
three-dimensional model of the tDGAT protein, structure homology modeling
additional information
-
the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
-
additional information
-
the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
-
additional information
-
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
-
additional information
-
three-dimensional model of the tDGAT protein, structure homology modeling
-