2.3.1.20: diacylglycerol O-acyltransferase
This is an abbreviated version!
For detailed information about diacylglycerol O-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.20
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2.3.1.20
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triacylglycerols
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triglyceride
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adipose
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milk
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acyl-coas
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lipoprotein
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obesity
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cholesterol
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droplet
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cattle
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adipocytes
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lipase
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steatosis
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lipogenesis
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lipogenic
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high-fat
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holstein
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oleic
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dairy
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proliferator-activated
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phosphatidate
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glycerolipids
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lipolysis
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oleaginous
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glycerol-3-phosphate
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chylomicron
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biodiesel
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srebf1
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oilseed
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lipotoxicity
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stearoyl-coa
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acaca
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camelina
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industry
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insig1
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biofuel production
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oleosins
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cholinephosphotransferase
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elovl6
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drug development
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triacylglyceride
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holstein-friesian
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sn-1,2-diacylglycerols
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analysis
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glycerolphosphate
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oleoyl-coa
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protein-1c
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lipin
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lpaat
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ricinoleic
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medicine
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baylyi
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chylomicronemia
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biotechnology
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steryl
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kennedy
- 2.3.1.20
- triacylglycerols
- triglyceride
- adipose
- milk
- acyl-coas
- lipoprotein
- obesity
- cholesterol
- droplet
- cattle
- adipocytes
- lipase
- steatosis
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lipogenesis
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lipogenic
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high-fat
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holstein
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oleic
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dairy
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proliferator-activated
- phosphatidate
- glycerolipids
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lipolysis
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oleaginous
- glycerol-3-phosphate
- chylomicron
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biodiesel
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srebf1
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oilseed
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lipotoxicity
- stearoyl-coa
- acaca
- camelina
- industry
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insig1
- biofuel production
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oleosins
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cholinephosphotransferase
- elovl6
- drug development
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triacylglyceride
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holstein-friesian
- sn-1,2-diacylglycerols
- analysis
- glycerolphosphate
- oleoyl-coa
- protein-1c
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lipin
- lpaat
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ricinoleic
- medicine
- baylyi
- chylomicronemia
- biotechnology
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steryl
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kennedy
Reaction
Synonyms
1,2-diacylglycerol acyltransferase, 2 diacylglycerol acyltransferase, ACY99349, acyl CoA:1,2-diacylglycerol acyltransferase, acyl CoA:diacylglycerol acyltransferase, acyl CoA:diacylglycerol acyltransferase 1, acyl CoA:diacylglycerol acyltransferase-2, acyl coenzyme A:diacylglycerol acyltransferase, acyl coenzyme A:diacylglycerol acyltransferase 1, acyl coenzyme A:diacylglycerol acyltransferase 2, acyl-CoA-dependent diacylglycerol acyltransferase, acyl-CoA: diacylglycerol acyltransferase, acyl-CoA:1,2-diacylglycerol O-acyltransferase, acyl-CoA:1,2-dioleoyl-sn-glycerol acyltransferase, acyl-CoA:diacylglycerol acyltransferase, acyl-CoA:diacylglycerol acyltransferase 1, acyl-CoA:diacylglycerol acyltransferase 2, acyl-CoA:diacylglycerol acyltransferase-2, acyl-CoA:diacylglycerol O-acyltransferase1, acyl-coenzyme A:diacylglycerol acyltransferase, acyltransferase, diacylglycerol, AtDGAT1A, AtDGAT3, AtfA, AtfG25, bifunctional DGAT/wax ester synthase, bifunctional wax synthase/DGAT, bifunctional WS/DGAT, BjDGAT1, BjDGAT2, BnaC.DGAT1.a, BnaDGAT1, BnaDGAT1.a, BnaDGAT1.b, BstDGAT1, CaDGAT1, CeDGAT1, CeDGAT2a, CeDGAT2b, CoDGAT2, CpuDGAT1, CrDGTT1, CrDGTT2, CrDGTT3, CsDGAT1B, CzDGAT1B, CzDGAT2, CzDGAT2A, CzDGAT2B, CzDGAT2C, CzDGAT2D, CzDGAT2E, CzDGAT2F, CzDGAT2G, DAG acyltransferase, DAGAT, DC3, DGA1, Dga1p, DGA2, DGAT, DGAT 1, DGAT 2, DGAT type 2, DGAT-1, DGAT-2, DGAT1, DGAT1-2, DGAT1-4, DGAT1-type enzyme, DGAT1.a, DGAT1A, DGAT1B, DGAT2, DGAT2-1, DGAT2.1, DGAT2.2, DGAT2.3, DGAT2A, DGAT2b, DGAT3, DGTT, diacylglycerol acyltransferase, diacylglycerol acyltransferase 1, diacylglycerol acyltransferase 2, diacylglycerol acyltransferase 3, diacylglycerol acyltransferase type 1, diacylglycerol acyltransferase type 2, diacylglycerol acyltransferase-1, diacylglycerol acyltransferase-2, diacylglycerol acyltransferase1, diacylglycerol acyltransferase2, diacylglycerol O-acyltransferase 1A, diacylglycerol O-acyltransferase 2, diacylglycerol O-acyltransferase 2D, diacylglycerol O-acyltransferase type-1, diacylglycerol O-acyltransferase-1, diglyceride acyltransferase, diglyceride O-acyltransferase, dual-function diacylglycerol acyltransferase, EC 2.3.1.124, ElDGAT1A, FBPA, Gat1, GmDGAT1A, GmDGAT1B, GmDGAT2D, GmDGAT3, HpDGAT2A, HpDGAT2B, HpDGAT2D, HpDGAT2E, Ma2, MaDGAT, MaDGAT2, MFAT, MGAT, mMaDGAT2, monoacylglycerol acyltransferase, More, MtDGAT1, multifunctional O-acyltransferase, NeoDGAT2, palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase, PDAT, PtDGATX, PtWS/DGAT, RtDGATa, RtDGATb, Rv3088 (TGS4), Rv3130c (TGS1), Rv3234c (TGS3), Rv3371, Rv3734 (TGS2), SAV7256, SCO0958, seed-specific DGAT1, SiDGAT1, SiDGAT2, TAG synthase, Tcur_3818, tDGAT, TmDGAT1, triacylglycerol:acyl-CoA:diacylglycerol acyltransferase, TrWSD4, TrWSD5, type 1 acyl-CoA: diacylglycerol acyltransferase, type 1 acyl-CoA:diacylglycerol acyltransferase, type 1 DGAT, type 1 diacylglycerol acyltransferase, type 2 acyl-CoA:diacylglycerol acyltransferase, type 2 DGAT, type 2 diacylglycerol acyltransferase, type I diacylglycerol acyltransferase, type II diacylglycerol acyltransferase, type-2 diacylglycerol acyltransferase, unspecific bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase, VgDGAT1A, VgDGAT1B, wax ester synthase/acyl CoA:diacylglycerol acyltransferase, wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase, wax ester synthase/acyl-CoA diacylglycerol acyltransferase, wax ester synthase/acyl-CoA:diacylglycerol acyltransferase, wax ester synthase/acyl-coenzyme A:diacylglycerol acyltransferase WSD1, wax ester synthase/triacylglycerol:acylCoA acyltransferase, Wdh3563-1, Wdh3563-2, Wdh3563-3, Wdh3563-4, Wdh3563-7, WS/DGAT, WSD1, WSD4, WSD5, YALI0D07986g, YALI0E32769g
ECTree
2.3.1.20 diacylglycerol O-acyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.20 - diacylglycerol O-acyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D137A
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highly conserved residue in acyltransferases, mutation does not result in a significant decrease of activity
G138A
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highly conserved residue in acyltransferases, mutation does not result in a significant decrease of activity
H132L
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highly conserved residue in acyltransferases, mutation results in strongly decreased activity
H133L
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highly conserved residue in acyltransferases, residue essential for catalytic activity
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
K232A
naturally occuring mutation, association with milk fatty acid composition
P178I
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mutation produces a drastic reduction of the neutral lipids content (yeast complementation experiment)
P178S
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in this position S is invariantly found for acyl-CoA:diacylglycerol acyltransferase 1 proteins in plants and animals, mutation P178S does not have an appreciable effect on the synthesis on triacylglycerol (yeast complementation experiment)
D145A
Marinobacter nauticus
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the mutant is 5fold less active with 1,2-dipalmitoyl-sn-glycerol compared to the wild type enzyme
D271A
Marinobacter nauticus
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the mutant shows reduced activity compared to the wild type enzyme
H140A
Marinobacter nauticus
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the mutant is 10fold less active with 1,2-dipalmitoyl-sn-glycerol compared to the wild type enzyme
H141A
Marinobacter nauticus
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the mutant is 5fold less active with 1,2-dipalmitoyl-sn-glycerol compared to the wild type enzyme
L119A
Marinobacter nauticus
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the mutant shows reduced activity compared to the wild type enzyme
N270A
Marinobacter nauticus
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the mutant shows reduced activity compared to the wild type enzyme
R305A
Marinobacter nauticus
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the mutant shows reduced activity compared to the wild type enzyme
C87S
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
H161A
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site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
H161A/P162G/H163A
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site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
H163A
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site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
P162G
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site-directed mutagenesis, the mutant shows about 40% reduced activity compared to the wild-type enzyme
S126A
H193E/G196S
mutation to corresponding motif found in plant, abolishes enzymic activity
additional information
additional information
expression of atfA in a quadruple mutant of Saccharomyces cerevisiae, lacking own DGAT and steryl ester synthase activites by disrupted DGA1, LRO1, ARE1 and ARE2, restores triacylglycerol but not steryl ester biosynthesis and results in the formation and accumulation of fatty acid ethyl and isoamyl esters, indicating that also eukaryotic systems are suitable hosts for atfA expression
additional information
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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
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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
additional information
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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
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additional information
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recombinant overexpression of AtDGAT1 leads to increased freezing tolerance in Boechera stricta seedlings, phenotypes. BstDGAT1 sequence polymorphisms in the upstream regulatory regions, the LTM allele contains several potential cis-regulatory elements involved in abiotic stress responses that are missing from SAD12 due to SNPs. Quantitative lipidomics analysis of control, cold-acclimated, and cold-acclimated freezing-treated plants, overview
additional information
construction of several truncated enzyme versions of isozyme BnaC.DGAT1.a, 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
additional information
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construction of several truncated enzyme versions of isozyme BnaC.DGAT1.a, 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
additional information
construction of truncated enzyme mutants, BnaDGAT11-113 comprises the full-length cytoplasmic domain, and BnaDGAT11-80 comprises the autoinhibitory domain, the truncated proteins are non-globular and monomeric in vitro
additional information
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construction of truncated enzyme mutants, BnaDGAT11-113 comprises the full-length cytoplasmic domain, and BnaDGAT11-80 comprises the autoinhibitory domain, the truncated proteins are non-globular and monomeric in vitro
additional information
construction of truncated enzyme versions, BnaDGAT11-113 and BnaDGAT181-501. Yeast transformed with BnaDGAT181-501 with N-terminal Nub tag and SnRK1 with N-terminal Cub tag grew on selective media. Truncated enzyme BnaDGAT11-113, comprising the N-terminus, interacts with increasing amounts of PA, allowing the soluble domain to be recovered together with the liposomes upon centrifugation
additional information
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construction of truncated enzyme versions, BnaDGAT11-113 and BnaDGAT181-501. Yeast transformed with BnaDGAT181-501 with N-terminal Nub tag and SnRK1 with N-terminal Cub tag grew on selective media. Truncated enzyme BnaDGAT11-113, comprising the N-terminus, interacts with increasing amounts of PA, allowing the soluble domain to be recovered together with the liposomes upon centrifugation
additional information
directed evolution of Brassica napus DGAT1 (BnaDGAT1) shows that one of the regions where amino acid residue substitutions lead to higher performance in BnaDGAT1 is in the ninth predicted transmembrane domain (PTMD9), generation of several BnaDGAT1 variants with amino acid residue substitutions in PTMD9, knock-in phenotypes, overview
additional information
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directed evolution of Brassica napus DGAT1 (BnaDGAT1) shows that one of the regions where amino acid residue substitutions lead to higher performance in BnaDGAT1 is in the ninth predicted transmembrane domain (PTMD9), generation of several BnaDGAT1 variants with amino acid residue substitutions in PTMD9, knock-in phenotypes, overview
additional information
directed evolution of Brassica napus DGAT1 (BnaDGAT1) shows that one of the regions where amino acid residue substitutions lead to higher performance in BnaDGAT1 is in the ninth predicted transmembrane domain (PTMD9), generation of analogous mutant variants of Camelina sativa with amino acid residue substitutions in PTMD9, knock-in phenotypes, overview
additional information
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directed evolution of Brassica napus DGAT1 (BnaDGAT1) shows that one of the regions where amino acid residue substitutions lead to higher performance in BnaDGAT1 is in the ninth predicted transmembrane domain (PTMD9), generation of analogous mutant variants of Camelina sativa with amino acid residue substitutions in PTMD9, knock-in phenotypes, overview
additional information
kinetic improvement of an algal diacylglycerol acyltransferase 1 via fusion with an acyl-CoA binding protein AtACBP6 from Arabidosis thaliana (UniProt ID P57752), generation of N-terminally truncated DGAT1 versions as fusion proteins: ACBP-CzDGAT11-550, ACBP-CzDGAT181-550, and ACBP-CzDGAT1107-550. The coding sequences of AtACBP6 and variant CzDGAT1s are individually amplified and the resulting amplicons are fused using overlap extension PCR. Fusion of ACBP to the N-terminus of the full-length CzDGAT1 not only augments the protein accumulation levels in yeast and tobacco leaves but also kinetically improves the enzyme. ACBP-fused DGAT1 is more effective in improving the oil contents of yeast cells and vegetative tissues than the native DGAT1
additional information
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kinetic improvement of an algal diacylglycerol acyltransferase 1 via fusion with an acyl-CoA binding protein AtACBP6 from Arabidosis thaliana (UniProt ID P57752), generation of N-terminally truncated DGAT1 versions as fusion proteins: ACBP-CzDGAT11-550, ACBP-CzDGAT181-550, and ACBP-CzDGAT1107-550. The coding sequences of AtACBP6 and variant CzDGAT1s are individually amplified and the resulting amplicons are fused using overlap extension PCR. Fusion of ACBP to the N-terminus of the full-length CzDGAT1 not only augments the protein accumulation levels in yeast and tobacco leaves but also kinetically improves the enzyme. ACBP-fused DGAT1 is more effective in improving the oil contents of yeast cells and vegetative tissues than the native DGAT1
additional information
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when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain H1246, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain H1246, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain H1246, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
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when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
when CzDGAT2s are individually expressed in a TAG-deficient Saccharomyces cerevisiae mutant strain, only CzDGAT2C can restore the TAG biosynthesis and complement the strain
additional information
the type 1 DGAT complementary DNA (cDNA) from Corylus americana is isolated, CaDGAT1, improved variants are created, library screening, and effect on Corylus americana seed composition, detailed overview. The corresponding amino acid substitutions are repeated in a Glycine max type 1 DGAT. Effects on soybean oil content and composition are determined following expression of the engineered GmDGAT1 in soybean somatic embryos of either the wild-type or the engineered variants of each DGAT, analysis of effect on soybean seed composition
additional information
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the type 1 DGAT complementary DNA (cDNA) from Corylus americana is isolated, CaDGAT1, improved variants are created, library screening, and effect on Corylus americana seed composition, detailed overview. The corresponding amino acid substitutions are repeated in a Glycine max type 1 DGAT. Effects on soybean oil content and composition are determined following expression of the engineered GmDGAT1 in soybean somatic embryos of either the wild-type or the engineered variants of each DGAT, analysis of effect on soybean seed composition
additional information
among the three DGAT2-like genes, only CpuDGAT2C functionally complements TAG biosynthesis in Saccharomyces cerevisiae mutant H1246 cells. Expression of CpuDGAT1 in the TAG-deficient Saccharomyces cerevisiae mutant strain H1246. CpuDGAT1 is able to rescue lipotoxicity of Saccharomyces cerevisiae H1246 cells grown in exogenous 0.25 mM C8:0 or C10:0, but not C18:1. Seed-specific recombinant CpuDGAT1 overexpression in Camelina sativa enhances C10:0 content in Camelina seeds. Coexpression of CpuDGAT1 and CvLPAT2 promotes accumulation of 10:0 at the TAG sn-2 position. Fatty acid composition of TAG and sn-2 position of TAG in mature seeds of wild-type camelina and camelina lines engineered for expression of CvFatB1 alone or with combinations of CpuDGAT1 and CvLPAT2, overview. CpuDGAT1 and CvLPAT2 coexpression increases 10:0 accumulation in DAG, but little 10:0 accumulation is detected in phosphatidylcholine (PC). Seed phenotype analysis
additional information
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functional overexpression of CeDGAT2b in yeast mutant and Arabidopsis TAG1 mutant and wild-type lines not only enhances TAG contents but also modifies the fatty acid compositions of TAG. The expression of CeDGAT2b rescues the seed phenotype of Arabidopsis thaliana TAG1 mutant ABX45
additional information
construction of an engineered strain of oleaginous microalga Neochloris oleoabundans with accelerated triacylglycerol production and altered fatty acid composition by overexpression of endogenous diacylglycerol acyltransferase 2, phenotype, overview
additional information
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construction of an engineered strain of oleaginous microalga Neochloris oleoabundans with accelerated triacylglycerol production and altered fatty acid composition by overexpression of endogenous diacylglycerol acyltransferase 2, phenotype, overview
additional information
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construction of an engineered strain of oleaginous microalga Neochloris oleoabundans with accelerated triacylglycerol production and altered fatty acid composition by overexpression of endogenous diacylglycerol acyltransferase 2, phenotype, overview
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additional information
a type 1 DGAT complementary DNA (cDNA) from Corylus americana is isolated, CaDGAT1, improved variants from a screened library are created, then the corresponding amino acid substitutions are made in a Glycine max type 1 DGAT. Effects on soybean oil content and composition are determined following expression of the engineered GmDGAT1 in soybean somatic embryos of either the wild-type or the engineered variants of each DGAT, effect on soybean seed composition, detailed overview
additional information
-
a type 1 DGAT complementary DNA (cDNA) from Corylus americana is isolated, CaDGAT1, improved variants from a screened library are created, then the corresponding amino acid substitutions are made in a Glycine max type 1 DGAT. Effects on soybean oil content and composition are determined following expression of the engineered GmDGAT1 in soybean somatic embryos of either the wild-type or the engineered variants of each DGAT, effect on soybean seed composition, detailed overview
additional information
TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT1A-transgenic hairy roots synthesize more 18:3-triacylglycerols. Overexpression of GmDGAT1A in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT1A enhances 18:3-TAG and reduces 20:1-TAG contents in rod1 mutant seeds
additional information
TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT1A-transgenic hairy roots synthesize more 18:3-triacylglycerols. Overexpression of GmDGAT1A in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT1A enhances 18:3-TAG and reduces 20:1-TAG contents in rod1 mutant seeds
additional information
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TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT1A-transgenic hairy roots synthesize more 18:3-triacylglycerols. Overexpression of GmDGAT1A in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT1A enhances 18:3-TAG and reduces 20:1-TAG contents in rod1 mutant seeds
additional information
TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT2D-transgenic hairy roots synthesize more linoleoyl- or oleoyl-triacylglycerols. Overexpression of GmDGAT2D in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT2D promotes linoleoyl-TAG in wild-type but enhances oleoyl-TAG production in rod1 mutant seeds
additional information
TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT2D-transgenic hairy roots synthesize more linoleoyl- or oleoyl-triacylglycerols. Overexpression of GmDGAT2D in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT2D promotes linoleoyl-TAG in wild-type but enhances oleoyl-TAG production in rod1 mutant seeds
additional information
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TAG biosynthesis and metabolic engineering of soybean oil with appropriate DGATs. GmDGAT2D-transgenic hairy roots synthesize more linoleoyl- or oleoyl-triacylglycerols. Overexpression of GmDGAT2D in Arabidopsis thaliana seeds enhances the TAG production, GmDGAT2D promotes linoleoyl-TAG in wild-type but enhances oleoyl-TAG production in rod1 mutant seeds
additional information
the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
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the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
additional information
Lobosphaera incisa SAG 2468
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the TAG-deficient Saccharomyces cerevisiae strain H1246 is complemented with LiDGAT1, LiDGAT2.1, LiDGAT2.2 and LiDGAT2.3 as well as with their double constructs followed by analysis of synthesized TAGs
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additional information
DGAT2 overexpression also increases wax monoester synthase activity in intact cells
additional information
DGAT2 overexpression also increases wax monoester synthase activity in intact cells
additional information
short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
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short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
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short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
the wax diester synthase activity of DGAT1 helps to explain the deficiency of type II wax diesters in the fur lipids of Dgat-/- mice, DGAT1 deficiency also perturbs retinol metabolism in the livers of Dgat-/- mice, hepatic levels of unesterified retinol are increased in Dgat-/- mice challenged with high-retinol diets
additional information
the wax diester synthase activity of DGAT1 helps to explain the deficiency of type II wax diesters in the fur lipids of Dgat-/- mice, DGAT1 deficiency also perturbs retinol metabolism in the livers of Dgat-/- mice, hepatic levels of unesterified retinol are increased in Dgat-/- mice challenged with high-retinol diets
additional information
an isoform DGAT2 mutant lacking both its transmembrane domains still associates with membranes, but is absent from the endoplasmic reticulum and instead localizes to mitochondria. The mutant is still active and capable of interacting with lipid droplets to promote triacylglycerol storage. Mutants, in which regions of the C-terminus are either truncated or specific regions are deleted, fail to co-localize with lipid droplets when cells are loaded with oleate to stimulate triacylglycerol synthesis
additional information
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an isoform DGAT2 mutant lacking both its transmembrane domains still associates with membranes, but is absent from the endoplasmic reticulum and instead localizes to mitochondria. The mutant is still active and capable of interacting with lipid droplets to promote triacylglycerol storage. Mutants, in which regions of the C-terminus are either truncated or specific regions are deleted, fail to co-localize with lipid droplets when cells are loaded with oleate to stimulate triacylglycerol synthesis
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construction of chimeric enzyme BioId/DGAT2, DGAT2 is fused in-frame to the C-terminus of a promiscuous biotin ligase, BirA. Like DGAT2, BioId/DGAT2 stimulates the formation of large lipid droplets. Fusing DGAT2 to the C-terminus does not appear to change its localization or function in cells. When biotin is added to the culture medium, with or without oleate, there is a strong biotinylation signal that co-localizes with BioId/DGAT2 both in the endoplasmic reticulum and around lipid droplets. Protein interaction analysis of biotinylated BioId/DGAT2 in recombinant HEK-293T cells, overview
additional information
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construction of chimeric enzyme BioId/DGAT2, DGAT2 is fused in-frame to the C-terminus of a promiscuous biotin ligase, BirA. Like DGAT2, BioId/DGAT2 stimulates the formation of large lipid droplets. Fusing DGAT2 to the C-terminus does not appear to change its localization or function in cells. When biotin is added to the culture medium, with or without oleate, there is a strong biotinylation signal that co-localizes with BioId/DGAT2 both in the endoplasmic reticulum and around lipid droplets. Protein interaction analysis of biotinylated BioId/DGAT2 in recombinant HEK-293T cells, overview
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generation of cardiac-specific constitutive and inducible DGAT1 KO mouse models (cKO and iKO, respectively). Both models show reduced DGAT1 mRNA and protein with no effects on DGAT2 mRNA expression or cardiac triglyceride (TG) content, no differences between genotypes for cardiac lipid droplet number and morphology. Cardiac TG synthesis is modestly reduced with loss of DGAT1, increased oxidation of exogenous fatty acids occurs in DGAT1 iKO hearts, DGAT1 iKO hearts respond normally to high fat diet
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generation of cardiac-specific constitutive and inducible DGAT1 KO mouse models (cKO and iKO, respectively). Both models show reduced DGAT1 mRNA and protein with no effects on DGAT2 mRNA expression or cardiac triglyceride (TG) content, no differences between genotypes for cardiac lipid droplet number and morphology. Cardiac TG synthesis is modestly reduced with loss of DGAT1, increased oxidation of exogenous fatty acids occurs in DGAT1 iKO hearts, DGAT1 iKO hearts respond normally to high fat diet
additional information
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generation of cardiac-specific constitutive and inducible DGAT1 KO mouse models (cKO and iKO, respectively). Both models show reduced DGAT1 mRNA and protein with no effects on DGAT2 mRNA expression or cardiac triglyceride (TG) content, no differences between genotypes for cardiac lipid droplet number and morphology. Cardiac TG synthesis is modestly reduced with loss of DGAT1, increased oxidation of exogenous fatty acids occurs in DGAT1 iKO hearts, DGAT1 iKO hearts respond normally to high fat diet
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disruption of gene tgs1, i.e. Rv3130c, leads to drastically reduced triacylglycerol accumulation
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generation of DGAT2 overexpressing cells of Nannochloropsis oceanica, expression analysis and lipid content determination, overview. The introduced transgene DGAT2 is successfully integrated,transcribed and translated in the transformed algal cells. The overexpressed DGAT2 does not have apparent effects on the growth and biomass accumulation of the engineered microalgae, analysis of neutral lipid content. There is a variation in terms of fatty acid composition between the engineered and wild-type cells. Saturated fatty acid (SFAs) content is significantly increased by 53.1% in engineered lines compared to wild-type. On the other hand,monounsaturated fatty acids (MUFAs) decrease by 52.9% in engineered cells. Similarly, polyunsaturated fatty acids (PUFAs) show an apparent decrease of 74.6%, including arachidonic acid (C20:4) and EPA (C20:5) in engineered cells
additional information
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generation of DGAT2 overexpressing cells of Nannochloropsis oceanica, expression analysis and lipid content determination, overview. The introduced transgene DGAT2 is successfully integrated,transcribed and translated in the transformed algal cells. The overexpressed DGAT2 does not have apparent effects on the growth and biomass accumulation of the engineered microalgae, analysis of neutral lipid content. There is a variation in terms of fatty acid composition between the engineered and wild-type cells. Saturated fatty acid (SFAs) content is significantly increased by 53.1% in engineered lines compared to wild-type. On the other hand,monounsaturated fatty acids (MUFAs) decrease by 52.9% in engineered cells. Similarly, polyunsaturated fatty acids (PUFAs) show an apparent decrease of 74.6%, including arachidonic acid (C20:4) and EPA (C20:5) in engineered cells
additional information
Nannochloropsis oceanica CCAP 849/10
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generation of DGAT2 overexpressing cells of Nannochloropsis oceanica, expression analysis and lipid content determination, overview. The introduced transgene DGAT2 is successfully integrated,transcribed and translated in the transformed algal cells. The overexpressed DGAT2 does not have apparent effects on the growth and biomass accumulation of the engineered microalgae, analysis of neutral lipid content. There is a variation in terms of fatty acid composition between the engineered and wild-type cells. Saturated fatty acid (SFAs) content is significantly increased by 53.1% in engineered lines compared to wild-type. On the other hand,monounsaturated fatty acids (MUFAs) decrease by 52.9% in engineered cells. Similarly, polyunsaturated fatty acids (PUFAs) show an apparent decrease of 74.6%, including arachidonic acid (C20:4) and EPA (C20:5) in engineered cells
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additional information
construction of N- and C-terminal truncation mutants N1(DELTA1-62), N2 (DELTA1-33), C1 (DELTA374-418), C2 (DELTA391-418), C3 (DELTA413-418), C4 (DELTA413-418, 413::A6). Mutant N1 lacking the entire hydrophilic N terminus presents minimal activity while maintaining a substantial expression level. Removal of the first 33 amino acid residues in the N-terminus, mutant N2, results in minor decrease in enzyme activity. Deletion of the last six amino acid residues from the C-terminus, mutant C3, causes a decrease in the enzyme activity of more than 80%. Deletion of the whole C-terminus, mutant C1, completely abolishes the enzyme activity and has a substantial impact on the protein accumulation. Mutant C2 lacking about half of the C-terminus, exhibits a complete loss of activity. In mutant C4, the last six amino acid residues are replaced with six alanine residues. This mutant retains similar activity and expression levels to C3. Deletion of the first putative TMD between residues 70 and 91 also results in the total loss of activity
additional information
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construction of N- and C-terminal truncation mutants N1(DELTA1-62), N2 (DELTA1-33), C1 (DELTA374-418), C2 (DELTA391-418), C3 (DELTA413-418), C4 (DELTA413-418, 413::A6). Mutant N1 lacking the entire hydrophilic N terminus presents minimal activity while maintaining a substantial expression level. Removal of the first 33 amino acid residues in the N-terminus, mutant N2, results in minor decrease in enzyme activity. Deletion of the last six amino acid residues from the C-terminus, mutant C3, causes a decrease in the enzyme activity of more than 80%. Deletion of the whole C-terminus, mutant C1, completely abolishes the enzyme activity and has a substantial impact on the protein accumulation. Mutant C2 lacking about half of the C-terminus, exhibits a complete loss of activity. In mutant C4, the last six amino acid residues are replaced with six alanine residues. This mutant retains similar activity and expression levels to C3. Deletion of the first putative TMD between residues 70 and 91 also results in the total loss of activity
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construction of a SCO0958 deletion mutant shows that the protein is responsible for biosynthesis of a significant amount of triacylglycerol
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generation of an atfG25OMEGAApr insertion mutant of Streptomyces sp. G25
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expression of recombinant TmDGAT1 in the yeast H1246MATalpha quadruple mutant (DGA1, LRO1, ARE1, ARE2) restores the capability of the mutant host to produce triacylglycerols
additional information
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expression of recombinant TmDGAT1 in the yeast H1246MATalpha quadruple mutant (DGA1, LRO1, ARE1, ARE2) restores the capability of the mutant host to produce triacylglycerols
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in plant transformation studies, seed-specific expression of TmDGAT1 is able to complement the low TAG/unusual fatty acid phenotype of the Arabidopsis AS11 (DGAT1) mutant
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in plant transformation studies, seed-specific expression of TmDGAT1 is able to complement the low TAG/unusual fatty acid phenotype of the Arabidopsis AS11 (DGAT1) mutant
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overexpression of TmDGAT1 in wild-type Arabidopsis and high-erucic-acid rapeseed (HEAR) and canola Brassica napus results in an increase in oil content (3.5%-10% on a dry weight basis, or a net increase of 11%-30%)
additional information
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overexpression of TmDGAT1 in wild-type Arabidopsis and high-erucic-acid rapeseed (HEAR) and canola Brassica napus results in an increase in oil content (3.5%-10% on a dry weight basis, or a net increase of 11%-30%)
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site-directed mutagenesis is conducted on six putative functional regions/motifs of the TmDGAT1 enzyme. Mutagenesis of a serine residue in a putative SnRK1 target site results in a 38%-80% increase in DGAT1 activity, and over-expression of the mutated TmDGAT1 in Arabidopsis results in a 20%-50% increase in oil content on a per seed basis
additional information
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site-directed mutagenesis is conducted on six putative functional regions/motifs of the TmDGAT1 enzyme. Mutagenesis of a serine residue in a putative SnRK1 target site results in a 38%-80% increase in DGAT1 activity, and over-expression of the mutated TmDGAT1 in Arabidopsis results in a 20%-50% increase in oil content on a per seed basis
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construction of enzyme mutants Dga1pDELTA19, lacking a region predicted to be disordered, and Dga1pDELTA85, lacking the 85 N-terminal residues predicted to contain a transmembrane domain. Mutant Dga1pDELTA19 shows reduced activity compared to wild-type, while mutant Dga1pDELTA85 is inactive
additional information
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construction of enzyme mutants Dga1pDELTA19, lacking a region predicted to be disordered, and Dga1pDELTA85, lacking the 85 N-terminal residues predicted to contain a transmembrane domain. Mutant Dga1pDELTA19 shows reduced activity compared to wild-type, while mutant Dga1pDELTA85 is inactive
additional information
the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. Overexpression of YlDGA2 in a Q4 context under neosynthesis conditions causes the formation of large lipid bodies
additional information
the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. Overexpression of YlDGA2 in a Q4 context under neosynthesis conditions causes the formation of large lipid bodies
additional information
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the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. Overexpression of YlDGA2 in a Q4 context under neosynthesis conditions causes the formation of large lipid bodies
additional information
the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
additional information
the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
additional information
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the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
additional information
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construction of enzyme mutants Dga1pDELTA19, lacking a region predicted to be disordered, and Dga1pDELTA85, lacking the 85 N-terminal residues predicted to contain a transmembrane domain. Mutant Dga1pDELTA19 shows reduced activity compared to wild-type, while mutant Dga1pDELTA85 is inactive
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additional information
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the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
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additional information
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construction of enzyme mutants Dga1pDELTA19, lacking a region predicted to be disordered, and Dga1pDELTA85, lacking the 85 N-terminal residues predicted to contain a transmembrane domain. Mutant Dga1pDELTA19 shows reduced activity compared to wild-type, while mutant Dga1pDELTA85 is inactive
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additional information
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the Q4 strain, in which the four acyltransferases have been deleted, is unable to accumulate lipids and to form lipid bodies (LBs). The expression of a single acyltransferase in this strain restores TAG accumulation and LB formation. Using this system, it becomes possible to characterize the activity and specificity of an individual DGAT. The effects of DGAT overexpression - isozymes DGAT1 or DGAT2 - on lipid accumulation and LB formation in Yarrowia lipolytica is analyzed. The overexpression of YlDGA1 generates smaller but more numerous lipid bodies, a phenotype which can be enhanced by increasing the copy number of the overexpressed gene
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