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
-
2.3.1.20
-
triacylglycerols
-
triglyceride
-
adipose
-
milk
-
acyl-coas
-
lipoprotein
-
obesity
-
cholesterol
-
droplet
-
cattle
-
adipocytes
-
lipase
-
steatosis
-
lipogenesis
-
lipogenic
-
high-fat
-
holstein
-
oleic
-
dairy
-
proliferator-activated
-
phosphatidate
-
glycerolipids
-
lipolysis
-
oleaginous
-
glycerol-3-phosphate
-
chylomicron
-
biodiesel
-
srebf1
-
oilseed
-
lipotoxicity
-
stearoyl-coa
-
acaca
-
camelina
-
industry
-
insig1
-
biofuel production
-
oleosins
-
cholinephosphotransferase
-
elovl6
-
drug development
-
triacylglyceride
-
holstein-friesian
-
sn-1,2-diacylglycerols
-
analysis
-
glycerolphosphate
-
oleoyl-coa
-
protein-1c
-
lipin
-
lpaat
-
ricinoleic
-
medicine
-
baylyi
-
chylomicronemia
-
biotechnology
-
steryl
-
kennedy
- 2.3.1.20
- triacylglycerols
- triglyceride
- adipose
- milk
- acyl-coas
- lipoprotein
- obesity
- cholesterol
- droplet
- cattle
- adipocytes
- lipase
- steatosis
-
lipogenesis
-
lipogenic
-
high-fat
-
holstein
-
oleic
-
dairy
-
proliferator-activated
- phosphatidate
- glycerolipids
-
lipolysis
-
oleaginous
- glycerol-3-phosphate
- chylomicron
-
biodiesel
-
srebf1
-
oilseed
-
lipotoxicity
- stearoyl-coa
- acaca
- camelina
- industry
-
insig1
- biofuel production
-
oleosins
-
cholinephosphotransferase
- elovl6
- drug development
-
triacylglyceride
-
holstein-friesian
- sn-1,2-diacylglycerols
- analysis
- glycerolphosphate
- oleoyl-coa
- protein-1c
-
lipin
- lpaat
-
ricinoleic
- medicine
- baylyi
- chylomicronemia
- biotechnology
-
steryl
-
kennedy
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 (Substrates Products
Substrates Products on EC 2.3.1.20 - diacylglycerol O-acyltransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-diacyl-sn-glycerol + erucoyl-CoA
1,2-diacyl-3-erucoyl-sn-glycerol + CoA
-
-
-
-
?
1,2-diacyl-sn-glycerol + oleoyl-CoA
1,2-diacyl-3-oleoyl-sn-glycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + erucoyl-CoA
1,2-diacyl-3-erucoylglycerol + CoA
-
-
-
?
1,2-diacylglycerol + oleoyl-CoA
1,2-diacyl-3-oleoylglycerol + CoA
-
-
-
?
1,2-diacylglycerol + palmitoyl-CoA
1,2-diacyl-3-palmitoylglycerol + CoA
-
-
-
?
1,2-diacylglycerol + stearoyl-CoA
1,2-diacyl-3-stearoylglycerol + CoA
-
-
-
?
1,2-dilinolein + alpha-linolenoyl-CoA
1,2-dilinoleoyl-3-alpha-linolenoyl-sn-glycerol + CoA
-
-
-
?
1,2-dilinolein + linoleoyl-CoA
1,2,3-trilinoleoyl-sn-glycerol + CoA
-
-
-
?
1,2-dilinolein + oleoyl-CoA
1,2-dilinoleoyl-3-oleoyl-sn-glycerol + CoA
-
-
-
?
1,2-dilinolein + palmitoyl-CoA
1,2-dilinoleoyl-3-palmitoyl-sn-glycerol + CoA
-
-
-
?
1,2-dilinolenin + alpha-linolenoyl-CoA
1,2-dilinolenoyl-3-alpha-linolenoyl-sn-glycerol + CoA
-
-
-
?
1,2-dilinolenin + linoleoyl-CoA
1,2-dilinolenoyl-3-linoleoyl-sn-glycerol + CoA
-
-
-
?
1,2-dilinolenin + oleoyl-CoA
1,2-dilinolenoyl-3-oleoyl-sn-glycerol + CoA
-
-
-
?
1,2-dilinolenin + palmitoyl-CoA
1,2-dilinolenoyl-3-palmitoyl-sn-glycerol + CoA
-
-
-
?
1,2-diolein + alpha-linolenoyl-CoA
1,2-dioleoyl-3-alpha-linolenoyl-sn-glycerol + CoA
-
-
-
?
1,2-diolein + linoleoyl-CoA
1,2-dioleoyl-3-linoleoyl-sn-glycerol + CoA
-
-
-
?
1,2-diolein + oleoyl-CoA
1,2,3-trioleoyl-sn-glycerol + CoA
-
-
-
?
1,2-dioleoyl-sn-glycerol + oleoyl-CoA
1,2,3-trioleoyl-sn-glycerol + CoA
-
-
-
-
?
1,2-dioleoyl-sn-glycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-sn-glycerol + CoA
-
-
-
-
?
1,2-dioleoylglycerol + arachidonoyl-CoA
1,2-dioleoyl-3-arachidonoylglycerol + CoA
-
about 8% of the activity with palmitoyl-CoA
-
-
?
1,2-dioleoylglycerol + linoleoyl-CoA
1,2-dioleoyl-3-linoleoylglycerol + CoA
-
about 12% of the activity with palmitoyl-CoA
-
-
?
1,2-dioleoylglycerol + stearoyl-CoA
1,2-dioleoyl-3-stearoylglycerol + CoA
-
about 10% of the activity with palmitoyl-CoA
-
-
?
1,2-dipalmitoyl-rac-glycerol + palmitoyl-CoA
tripalmitoylglycerol + CoA
-
-
-
?
1,2-dipalmitoyl-sn-glycerol + oleoyl-CoA
1,2-dipalmitoyl-3-oleoyl-sn-glycerol + CoA
-
-
-
?
1,2-dipalmitoyl-sn-glycerol + palmitoyl-CoA
tripalmitin + CoA
-
-
-
?
1,2-dipalmitoyl-sn-glycerol + stearoyl-CoA
1,2-dipalmitoyl-3-stearoyl-sn-glycerol + CoA
-
-
-
?
1,2-diricinoleoyl-sn-glycerol + ricinoleoyl-CoA
triricinolein + CoA
-
-
-
-
?
1-palmitoyl-2-oleoylglycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
?
acyl-CoA + 1,2-di-alpha-linolenoyl-sn-glycerol
CoA + 1,2-di-alpha-linolenoyl-3-acylglycerol
acyl-CoA + 1,2-didecanoylglycerol
CoA + 3-acyl-1,2-didecanoylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dihexanoylglycerol
CoA + 3-acyl-1,2-dihexanoylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dilauroylglycerol
CoA + 3-acyl-1,2-dilauroylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dimyristoylglycerol
CoA + 3-acyl-1,2-dimyristoylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dioctanoylglycerol
CoA + 3-acyl-1,2-dioctanoylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dipalmitin
CoA + 3-acyl-1,2-dipalmitoylglycerol
-
no acceptor
-
-
?
acyl-CoA + 1,2-dipalmitoylglycerol
CoA + 3-acyl-1,2-dipalmitoylglycerol
-
membrane bound 1,2-dipalmitoylglycerol
-
-
?
acyl-CoA + 1,2-hexadec-9-enoyl-sn-glycerol
CoA + 1,2-dihexadec-9-enoyl-3-acylglycerol
-
-
-
?
acyl-CoA + 1-decanol
? + CoA
at 48% of the activity with hexanol
-
-
?
acyl-CoA + 1-oleoyl-2-palmitoyl-sn-glycerol
CoA + 1-oleoyl-2-palmitoyl-3-acylglycerol
-
-
-
?
acyl-CoA + 1-palmitoyl-2-oleoyl-sn-glycerol
CoA + 1-palmitoyl-2-oleoyl-3-acylglycerol
-
-
-
?
acyl-CoA + 2,3-dioleoyl-sn-glycerol
CoA + 1-acyl-2,3-dioleoyl-sn-glycerol
-
-
-
-
?
acyl-CoA + 2-cyclohexylethanol
? + CoA
at 45% of the activity with hexanol
-
-
?
acyl-CoA + 2-decanol
? + CoA
at 39% of the activity with hexanol
-
-
?
acyl-CoA + 4-decanol
? + CoA
at 15.6% of the activity with hexanol
-
-
?
acyl-CoA + cyclododecanol
? + CoA
at 80% of the activity with hexanol
-
-
?
acyl-CoA + cyclohexandiol
? + CoA
at 4.1% of the activity with hexanol
-
-
?
acyl-CoA + cyclohexanol
? + CoA
at 32% of the activity with hexanol
-
-
?
acyl-CoA + cyclohexanone oxime
? + CoA
at 5.2% of the activity with hexanol
-
-
?
acyl-CoA + lysophosphatidylcholine
CoA + acyllysophosphatidylcholine
-
-
-
-
?
acyl-CoA + phenol
? + CoA
at 4.1% of the activity with hexanol
-
-
?
acyl-CoA + phenylethanol
? + CoA
at 99% of the activity with hexanol
-
-
?
acyl-CoA + rac-1,2-diacetylglycerol
CoA + 3-acyl-rac-1,2-diacetylglycerol
-
no acceptor
-
-
?
acyl-CoA + rac-1,2-dibutyrylglycerol
CoA + 3-acyl-rac-1,2-dibutyrylglycerol
-
no acceptor
-
-
?
alpha-linolenoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linolenoyl-sn-glycerol
100% activity
-
-
?
caproyl-CoA + 1,2-dicaproyl-sn-glycerol
CoA + tricaproylglycerol
-
-
-
-
?
decanoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-decanoylglycerol
-
saturated fatty acyl-CoAs from C-8 to C-18 with decanoyl-CoA as the best
-
-
?
dihomo gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-dihomo-gamma-linolenoylglycerol
docosahexaenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-docosahexaenoylglycerol
-
-
-
?
eicosapentaenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-eicosapentaenoylglycerol
-
-
-
?
erucoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 3-erucoyl-1,2-dioleoyl-sn-glycerol
-
-
-
-
?
hexanoyl-CoA + 1,2-dipalmitoyl glycerol
coenzyme A + 1,2-dipalmitoyl-3-hexanoyl glycerol
-
-
-
-
r
lauroyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-lauroyl-sn-glycerol
-
-
-
?
lauryl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-lauryl-glycerol
-
-
-
-
?
lignoceryl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-lignocerylglycerol
-
-
-
?
linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linolenoyl-glycerol
-
-
-
?
linoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linoleoyl-glycerol
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
1,2-dioleoyl-3-linoleoyl-sn-glycerol + CoA
-
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 3-linoleoyl-1,2-dioleoylglycerol
-
i.e. diolein
-
?
N-[(7-nitro-2-1,3-benzoxadiazol-4-yl)]aminopalmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 3-[N-[(7-nitro-2-1,3-benzoxadiazol-4-yl)]-16-aminopalmitoyl]-1,2-dioleoyl-sn-glycerol
-
-
-
-
?
octanoyl-CoA + 1,2-di-(cis-9-octadecenoyl)-sn-glycerol
CoA + 1,2-di-(cis-9-octadecenoyl)-3-octanoyl-sn-glycerol
-
-
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoyl-sn-glycerol
BnaDGAT1 exhibits cooperative substrate binding behavior with oleoyl-CoA. The lipidated BnaDGAT1 exhibited a sigmoidal response to increasing concentrations of oleoyl-CoA
-
-
?
oleoyl-CoA + 1,2-dioleoylglycerol
CoA + 1,2,3-trioleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-dipalmitoylglycerol
CoA + 3-oleoyl-1,2-dipalmitoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-diricinoloylglycerol
CoA + 3-oleoyl-1,2-diricinoloylglycerol
best substrate
-
-
?
oleoyl-CoA + 1,2-divernoloyl-sn-glycerol
CoA + 1,2-divernoloyl-3-oleoyl-sn-glycerol
oleoyl-CoA and 1,2-dioleoyl-sn-glycerol are preferred substrates over vernoloyl-CoA and 1,2-divernoloyl-sn-glycerol
-
-
?
palmitoleoyl-CoA + 1,2-dipalmitoleoyl-sn-glycerol
CoA + tripalmitoleoylglycerol
-
preferred substrate for isoform DGAT2
-
-
?
palmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2,3-tripalmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-dipalmitoylglycerol
CoA + tripalmitin
approximately 10fold lower level of diacylglycerol acyltransferase activity
-
-
?
palmitoyl-CoA + 1,2-distearin
CoA + 3-palmitoyl-1,2-distearoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-oleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
usage of fluorescent NBD-tagged palmitoyl-CoA as substrate
-
-
?
palmitoyl-CoA + 1,3-diolein
CoA + 1,3-dioleoyl-2-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + didecanoylglycerol
CoA + 1,2-didecanoyl-3-palmitoylglycerol
-
i.e. dicaprin
-
-
?
palmitoyl-CoA + dihexanoylglycerol
CoA + dihexanoyl-palmitoylglycerol
-
i.e. dicaproin
-
-
?
palmitoyl-CoA + dipalmitoylglycerol
CoA + tripalmitoylglycerol
-
membrane-bound dipalmitoylglycerol
-
-
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-palmitoyl-2-oleoylglycerol
-
-
-
-
?
ricinoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
1,2-dioleoyl-3-ricinoleoyl-sn-glycerol + CoA
-
-
-
-
?
ricinoleoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
1,2-dipalmitoyl-3-ricinoleoyl-sn-glycerol + CoA
-
prefers acyl acceptor 1,2-dioleoyl-sn-glycerol over 1,2-dipalmitoyl-sn-glycerol
-
-
?
sn-1,2-diacylglycerol + erucoyl-CoA
triacylglycerol + CoA
-
i.e. a 22:1cisDELTA13-CoA
-
-
?
vernoloyl-CoA + 1,2-divernoloyl-sn-glycerol
CoA + trivernoloyl-sn-glycerol
oleoyl-CoA and 1,2-dioleoyl-sn-glycerol are preferred substrates over vernoloyl-CoA and 1,2-divernoloyl-sn-glycerol
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
role in leaf metabolism, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
the enzyme catalyzes the final step in triacylglycerol biosynthesis that acylates diacylglycerol to triacylglycerols
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
the enzyme catalyzes the final step in triacylglycerol biosynthesis that acylates diacylglycerol to triacylglycerols
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
DGAT catalyzes the transfer of an acyl moiety between two DAG molecules to form triacylglycerol and monoacylglycerol
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Cuphea sp.
-
microsomal DGAT from Cuphea exhibits high activity toward diacylglycerols containing unusual fatty acids, e.g. lauric acids, at both sn-1 and sn-2 positions, acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
microsomal DGAT from castor bean exhibited high activity toward diacylglycerols containing unusual fatty acids, e.g. ricinoleic acids, at both sn-1 and sn-2 positions, acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
acyl-CoA specificity, no acylation activity with phosphoatidylcholine or oleic acid, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
DGAT1 and DGAT2 are two unrelated enzymes that catalyze the committed step in triacylglycerol biosynthesis
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
DGAT1 catalyzes the committed step in triacylglycerol biosynthesis
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
DGAT2 catalyzes the committed step in triacylglycerol biosynthesis
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
acyl-CoA specificity, overview
-
-
?
1,2-diolein + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-sn-glycerol + CoA
-
-
-
-
?
1,2-diolein + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-sn-glycerol + CoA
-
-
-
?
1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
about 90% of the activity with palmitoyl-CoA
-
-
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-glycerol + CoA
-
-
-
-
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-glycerol + CoA
-
-
-
-
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
-
-
-
-
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
-
-
-
?
1,2-dipalmitoyl-rac-glycerol + palmitoyl-CoA
rac-tripalmitoylglycerol + CoA
-
-
-
?
1,2-dipalmitoyl-rac-glycerol + palmitoyl-CoA
rac-tripalmitoylglycerol + CoA
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
Cuphea sp.
-
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
-
?
acyl-CoA + 1,2-di-alpha-linolenoyl-sn-glycerol
CoA + 1,2-di-alpha-linolenoyl-3-acylglycerol
-
-
-
?
acyl-CoA + 1,2-di-alpha-linolenoyl-sn-glycerol
CoA + 1,2-di-alpha-linolenoyl-3-acylglycerol
low activity with the DAG substrate
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
E2RDN4
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Haematococcus lacustris UTEX 2505
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Nannochloropsis oceanica CCAP 849/10
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
isozyme RtDGATb prefers unsaturated fatty acids over saturated fatty acids, but not C18:3
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
RtDGATa has obvious preference for monounsaturated fatty acids. RtDGATa is active with C16:1 and C18:1 and shows poor activity for C16:0, C18:0, C18:2 and C18:3
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Rhodotorula toruloides CGMCC 2.1389
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Rhodotorula toruloides CGMCC 2.1389
RtDGATa has obvious preference for monounsaturated fatty acids. RtDGATa is active with C16:1 and C18:1 and shows poor activity for C16:0, C18:0, C18:2 and C18:3
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Rhodotorula toruloides CGMCC 2.1389
isozyme RtDGATb prefers unsaturated fatty acids over saturated fatty acids, but not C18:3
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
XP_011098009
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
Thraustochytrium roseum ATCC28210
-
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
isoform DGAT2b is catalytically more active than DGAt2a
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
isoform DGAT2b is catalytically more active than DGAt2a
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
isoforms DGAT1 and DGAT2 Can compensate for each other to synthesize triacylglycerol
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
saturated fatty acyl-CoAs from C-4 to C-18
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
broad range of donors from C-12 to C-22, broad range of acceptors from C12 to C-22
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
enzyme catalyzing the final reaction in the sn-glycerol-3-phosphate pathway leading to TAG
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
acceptors: 1,2-diacylglycerol containing oleic acid and 1,2-diacylglycerol containing capric acid
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
last step of triacylglycerol synthesis
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
acceptors: overview
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
DGAT1 is more involved in fat absorption in the intestine and DGAT2 plays important role in assembly of de novo synthesized fatty acids into VLDL particles in liver
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
endogenously and exogenously synthesized diacylglycerol
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
acyl-donors: broad specificity, saturated, mono-, di- and tetraenoic thioesters
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
saturated fatty acyl-CoAs from C-8 to C-12
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
2,3-diacylglycerol is acylated at 20% the rate of 1,2-isomer
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
last reaction in triacylglycerol synthesis
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
endogenous 1,2-diacylglycerol
-
-
?
acyl-CoA + 1,2-dilinoleoyl-sn-glycerol
CoA + 1,2-dilinoleoyl-3-acylglycerol
-
-
-
?
acyl-CoA + 1,2-dilinoleoyl-sn-glycerol
CoA + 1,2-dilinoleoyl-3-acylglycerol
low activity with the DAG substrate
-
-
?
acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
-
-
-
?
acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
low activity with the DAG substrate
-
-
?
acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dioleoylglycerol
CoA + 3-acyl-1,2-dioleoylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dioleoylglycerol
CoA + 3-acyl-1,2-dioleoylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dioleoylglycerol
CoA + 3-acyl-1,2-dioleoylglycerol
-
-
-
-
?
acyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-acylglycerol
-
-
-
?
acyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-acylglycerol
low activity with the DAG substrate
-
-
?
acyl-CoA + 1,3-dioleoyl-sn-glycerol
CoA + 1,3-dioleoyl-2-acylglycerol
-
-
-
?
acyl-CoA + 1,3-dioleoyl-sn-glycerol
CoA + 1,3-dioleoyl-2-acylglycerol
low activity with the DAG substrate
-
-
?
acyl-CoA + 1,3-dioleoylglycerol
CoA + 2-acyl-1,3-dioleoylglycerol
-
no acceptor
-
-
?
acyl-CoA + 1,3-dioleoylglycerol
CoA + 2-acyl-1,3-dioleoylglycerol
-
-
-
-
?
acyl-CoA + rac-1,2-dioleoylglycerol
CoA + 3-acyl-rac-1,2-dioleoylglycerol
-
-
-
-
?
acyl-CoA + rac-1,2-dioleoylglycerol
CoA + 3-acyl-rac-1,2-dioleoylglycerol
-
-
-
-
?
alpha-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-alpha-linolenoylglycerol
-
-
-
?
alpha-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-alpha-linolenoylglycerol
best acyl-CoA substrate
-
-
?
arachidonoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-arachidnoylglycerol
A0A2D2CI94, KY859195
-
-
-
?
arachidonoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-arachidnoylglycerol
-
-
-
?
arachidonoyl-CoA + 1,2-diacylglycerol
CoA + 3-arachidonoyl-1,2-diacylglycerol
-
-
-
?
arachidonoyl-CoA + 1,2-diacylglycerol
CoA + 3-arachidonoyl-1,2-diacylglycerol
-
-
-
-
?
butyryl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-butyrylglycerol
-
-
-
-
?
butyryl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-butyrylglycerol
-
-
-
-
?
butyryl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-butyrylglycerol
-
-
-
-
?
dihomo gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-dihomo-gamma-linolenoylglycerol
A0A2D2CI94, KY859195
-
-
-
?
dihomo gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-dihomo-gamma-linolenoylglycerol
-
-
-
?
erucoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
-
Jet Neuf enzyme displays an enhanced specificity for erucoyl-CoA over oleoyl-CoA
-
-
?
erucoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
-
-
-
-
?
gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-gamma-linolenoylglycerol
-
-
-
?
gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-gamma-linolenoylglycerol
A0A2D2CI94, KY859195
-
-
-
?
gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-gamma-linolenoylglycerol
-
-
-
?
hexadec-9-enoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-hexadec-9-enoylglycerol
-
-
-
?
hexadec-9-enoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-hexadec-9-enoylglycerol
best acyl-CoA subbstrate
-
-
?
hexadec-9-enoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-hexadec-9-enoylglycerol
preferred acyl-CoA substrate
-
-
?
lauroyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-lauroylglycerol
-
-
-
-
?
lauroyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-lauroylglycerol
-
-
-
-
?
linoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
-
-
?
linoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
A0A2D2CI94, KY859195
-
-
-
?
linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
-
-
-
?
linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
-
-
?
linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
-
-
?
linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
-
-
-
?
linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
poor donor
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoyl-sn-glycerol
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoyl-sn-glycerol
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoyl-sn-glycerol
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoyl-sn-glycerol
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoylglycerol
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoylglycerol
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoylglycerol
-
-
-
?
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linoleoylglycerol
-
-
-
?
myristoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-myristoylglycerol
-
-
-
-
?
myristoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-myristoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoyl-glycerol
-
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoyl-glycerol
-
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoyl-glycerol
-
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
assay with radioactive oleoyl-CoA and DAG from microsome preparation of the recombinant yeast cells
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
assay with radioactive oleoyl-CoA and DAG from microsome preparation of the recombinant yeast cells
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
low activity
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Rhodotorula toruloides CGMCC 2.1389
-
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
Rhodotorula toruloides CGMCC 2.1389
low activity
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
about 85% activity compared to alpha-linolenoyl-CoA
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
Haematococcus lacustris UTEX 2505
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoyl-sn-glycerol
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
oleoyl-CoA and 1,2-dioleoyl-sn-glycerol are preferred substrates over vernoloyl-CoA and 1,2-divernoloyl-sn-glycerol
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
i.e. diolein, at 34% the rate of the acylation with stearoyl-CoA
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
-
-
-
?
oleoyl-CoA + 1,2-oleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-oleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
-
-
-
?
oleoyl-CoA + diolein
CoA + triolein
-
-
-
?
oleoyl-CoA + diolein
CoA + triolein
-
-
-
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1,2-dioleoyl-sn-glycerol
-
-
-
-
?
palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
best substrate
-
-
?
palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
low activity
-
-
?
palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
Rhodotorula toruloides CGMCC 2.1389
best substrate
-
-
?
palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
Rhodotorula toruloides CGMCC 2.1389
low activity
-
-
?
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoyl-sn-glycerol
-
-
-
?
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoyl-sn-glycerol
-
-
-
?
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
-
-
?
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
good acyl-CoA substrate
-
-
?
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
high activity
-
-
?
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
-
-
?
palmitoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
Thraustochytrium roseum ATCC28210
-
-
-
-
?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
-
diacylglycerol diluted in ethanol
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
about 85% activity compared to alpha-linolenoyl-CoA
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
-
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
-
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
-
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
-
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
-
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoylglycerol
-
i.e. diolein
-
-
?
palmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + tripalmitoylglycerol
-
preferred substrate for isoform DGAT1
-
-
?
palmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + tripalmitoylglycerol
Marinobacter nauticus
-
-
-
-
?
sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
the final step in triacylglycerol synthesis is catalyzed by the acyl-CoA:diacylglycerol acyltransferase enzymes, DGAT1 and DGAT2
-
-
?
sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
the enzyme contains a neutral lipid binding sequence 80FLVLGVAC87 residing in the first transmembrane domain
-
-
?
stearoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-stearoylglycerol
-
-
-
?
stearoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-stearoylglycerol
high activity
-
-
?
stearoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-stearoylglycerol
-
weak donor
-
-
?
stearoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-stearoylglycerol
-
weak donor
-
-
?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
-
-
-
?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
fluorescent assay method using NBD-tagged diglycerol substrate
-
-
?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
fluorescent assay method using NBD-tagged diglycerol substrate
-
-
?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
fluorescent assay method using NBD-tagged diglycerol substrate
-
-
?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoylglycerol
-
-
-
-
?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoylglycerol
-
-
-
-
?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoylglycerol
-
i.e. diolein
-
-
?
additional information
?
-
ATfA exhibits a clear preference for the acylation of the sn-2 position of sn-1,2-dipalmitoylglycerol rather than the sn-2 position of sn-1,3-dipalmitoylglycerol
-
-
?
additional information
?
-
enzyme also has acyl-CoA-monoacylglycerol acyltransferase activity, sn-1 and sn-3 positions are accepted with higher specificity than sn-2 position
-
-
?
additional information
?
-
-
the bifunctional wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1 mediates the biosyntheses of wax esters and triacylglycerols
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes the reactions of the diacylglycerol transferase, EC 2.3.1.20, and of the wax synthase, EC 2.3.1.75
-
-
?
additional information
?
-
-
the bifunctional wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1 mediates the biosyntheses of wax esters and triacylglycerols
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes the reactions of the diacylglycerol transferase, EC 2.3.1.20, and of the wax synthase, EC 2.3.1.75
-
-
?
additional information
?
-
rate of activity is highly dependent on acyl composition with highest activities for acyl groups containing several double bonds, epoxy, or hydroxy groups. Enzyme uses both sn-positions of phosphatidylcholine with 3fold preference for sn-2 position
-
-
?
additional information
?
-
-
bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
-
-
-
additional information
?
-
bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
-
-
-
additional information
?
-
bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
-
-
-
additional information
?
-
bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
-
-
-
additional information
?
-
-
substrate specificity of native and recombinant enzyme, the native and the recombinant enzyme do not show wax ester synthase activity in contrast to other DGATs, no activity with hexadecanol, glycerol-3-phosphate, monoacylglycerol, lysophosphatidic acid, and lysophosphatidylcholine, oleoyl-CoA is the preferred acyl donor as compared to palmitoyl- and stearoyl-CoAs
-
-
?
additional information
?
-
substrate specificity of native and recombinant enzyme, the native and the recombinant enzyme do not show wax ester synthase activity in contrast to other DGATs, no activity with hexadecanol, glycerol-3-phosphate, monoacylglycerol, lysophosphatidic acid, and lysophosphatidylcholine, oleoyl-CoA is the preferred acyl donor as compared to palmitoyl- and stearoyl-CoAs
-
-
?
additional information
?
-
substrate specificity of native and recombinant enzyme, the native and the recombinant enzyme do not show wax ester synthase activity in contrast to other DGATs, no activity with hexadecanol, glycerol-3-phosphate, monoacylglycerol, lysophosphatidic acid, and lysophosphatidylcholine, oleoyl-CoA is the preferred acyl donor as compared to palmitoyl- and stearoyl-CoAs
-
-
?
additional information
?
-
although the four forms of recombinant microsomal BnaDGAT1 display enhanced specificity for palmitoyl (16:0)-CoA over oleoyl (18:1DELTA9cis, i.e. 18:1), the enzymes exhibit an enhanced selectivity for 18:1-CoA when assayed with a 3:1 ratio of 18:1-CoA to 16:0-CoA. Substrate specificity and selectivity properties of the recombinant enzymes
-
-
-
additional information
?
-
although the four forms of recombinant microsomal BnaDGAT1 display enhanced specificity for palmitoyl (16:0)-CoA over oleoyl (18:1DELTA9cis, i.e. 18:1), the enzymes exhibit an enhanced selectivity for 18:1-CoA when assayed with a 3:1 ratio of 18:1-CoA to 16:0-CoA. Substrate specificity and selectivity properties of the recombinant enzymes
-
-
-
additional information
?
-
-
although the four forms of recombinant microsomal BnaDGAT1 display enhanced specificity for palmitoyl (16:0)-CoA over oleoyl (18:1DELTA9cis, i.e. 18:1), the enzymes exhibit an enhanced selectivity for 18:1-CoA when assayed with a 3:1 ratio of 18:1-CoA to 16:0-CoA. Substrate specificity and selectivity properties of the recombinant enzymes
-
-
-
additional information
?
-
interaction of CoA and oleoyl-CoA with the cytoplasmic N-terminal region (BnaDGAT11-113) of isoform BnaC.DGAT1.a. Truncated forms BnaDGAT11-113 and BnaDGAT11-80 interact with oleoyl-CoA or CoA with micromolar affinity, docking study and kinetics. The N-terminal domain of BnaDGAT1 has a higher affinity for thioester than free CoA. Interestingly, BnaDGAT11-80 also interacts with both ligands but with lower affinity. Ligand binding results in gain of secondary structure in mutants BnaDGAT11-113 and BnaDGAT11-80
-
-
-
additional information
?
-
-
interaction of CoA and oleoyl-CoA with the cytoplasmic N-terminal region (BnaDGAT11-113) of isoform BnaC.DGAT1.a. Truncated forms BnaDGAT11-113 and BnaDGAT11-80 interact with oleoyl-CoA or CoA with micromolar affinity, docking study and kinetics. The N-terminal domain of BnaDGAT1 has a higher affinity for thioester than free CoA. Interestingly, BnaDGAT11-80 also interacts with both ligands but with lower affinity. Ligand binding results in gain of secondary structure in mutants BnaDGAT11-113 and BnaDGAT11-80
-
-
-
additional information
?
-
relative increase in activity of microsomal BnaDGAT1, BnaDGAT181-501, and BnaDGAT2 at different concentrations of oleoyl-CoA upon addition of 18:1/18:1-phosphatidate in the reaction mixture. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA, kinetics, overview
-
-
-
additional information
?
-
-
relative increase in activity of microsomal BnaDGAT1, BnaDGAT181-501, and BnaDGAT2 at different concentrations of oleoyl-CoA upon addition of 18:1/18:1-phosphatidate in the reaction mixture. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA, kinetics, overview
-
-
-
additional information
?
-
the acyl-CoA binding site is located at N-terminal domain of DGAT1 along amino acid residues 81 to 113
-
-
-
additional information
?
-
-
the acyl-CoA binding site is located at N-terminal domain of DGAT1 along amino acid residues 81 to 113
-
-
-
additional information
?
-
-
no activity with sn-1,3-diacylglycerols, water-soluble diacylglycerols, including rac-1,2-diacetylglycerol and rac-1,2-dibutyrylglycerol, are poor substrates of DGAT from safflower seeds, acyl-CoA specificity, overview
-
-
?
additional information
?
-
distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT2 exhibits a preference for monounsaturated acyl CoAs over saturated ones. When supplied with acyl CoAs of the same acyl chain length, CrDGTT2, unlike CrDGTT1, shows only a slight preference for polyunsaturated acyl CoAs over monounsaturated ones. CrDGTT2 shows comparable activities toward C16:0 and C18:0 CoAs, for unsaturated acyl CoAs, it has similar activity toward C16:1 and C18:1 CoAs. CrDGTT2 also shows strong activity toward C20:5n3 and C22:6n3 CoAs
-
-
-
additional information
?
-
distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT2 exhibits a preference for monounsaturated acyl CoAs over saturated ones. When supplied with acyl CoAs of the same acyl chain length, CrDGTT2, unlike CrDGTT1, shows only a slight preference for polyunsaturated acyl CoAs over monounsaturated ones. CrDGTT2 shows comparable activities toward C16:0 and C18:0 CoAs, for unsaturated acyl CoAs, it has similar activity toward C16:1 and C18:1 CoAs. CrDGTT2 also shows strong activity toward C20:5n3 and C22:6n3 CoAs
-
-
-
additional information
?
-
distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT2 exhibits a preference for monounsaturated acyl CoAs over saturated ones. When supplied with acyl CoAs of the same acyl chain length, CrDGTT2, unlike CrDGTT1, shows only a slight preference for polyunsaturated acyl CoAs over monounsaturated ones. CrDGTT2 shows comparable activities toward C16:0 and C18:0 CoAs, for unsaturated acyl CoAs, it has similar activity toward C16:1 and C18:1 CoAs. CrDGTT2 also shows strong activity toward C20:5n3 and C22:6n3 CoAs
-
-
-
additional information
?
-
-
distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT2 exhibits a preference for monounsaturated acyl CoAs over saturated ones. When supplied with acyl CoAs of the same acyl chain length, CrDGTT2, unlike CrDGTT1, shows only a slight preference for polyunsaturated acyl CoAs over monounsaturated ones. CrDGTT2 shows comparable activities toward C16:0 and C18:0 CoAs, for unsaturated acyl CoAs, it has similar activity toward C16:1 and C18:1 CoAs. CrDGTT2 also shows strong activity toward C20:5n3 and C22:6n3 CoAs
-
-
-
additional information
?
-
distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT3 shows low activity toward polyunsaturated acyl CoAs and prefers C16 CoAs, particularly C16:1 CoA, over C18 and other longer-chain fatty acyl CoAs
-
-
-
additional information
?
-
distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT3 shows low activity toward polyunsaturated acyl CoAs and prefers C16 CoAs, particularly C16:1 CoA, over C18 and other longer-chain fatty acyl CoAs
-
-
-
additional information
?
-
distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT3 shows low activity toward polyunsaturated acyl CoAs and prefers C16 CoAs, particularly C16:1 CoA, over C18 and other longer-chain fatty acyl CoAs
-
-
-
additional information
?
-
-
distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. CrDGTT3 shows low activity toward polyunsaturated acyl CoAs and prefers C16 CoAs, particularly C16:1 CoA, over C18 and other longer-chain fatty acyl CoAs
-
-
-
additional information
?
-
distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. Unsaturated acyl CoAs, particularly polyunsaturated acyl CoAs, are the preferred substrates for CrDGTT1. CrDGTT1 has a considerably higher activity toward C16:1 than C16:0. For C18 CoAs, CrDGTT1 has the greatest activity toward C18:3n, followed by C18:2, C18:1n9, and C18:0. CrDGTT1 prefers shorter-chain acyl CoAs when the number of double bonds is the same, for instance, C16:0 and C16:1 result in a greater level of TAG accumulation than C18:0 and C18:1, respectively. CrDGTT1 is also shown to have strong activity toward C20:5n3 and C22:6n3 CoAs. When using C18:3n6(d6) CoA as the acyl donor, CrDGTT1 shows strong and comparable activity toward C16:1/C16:1, C18:1n9/C16:0, C16:0/C18:1n9, and C18:1n9/C18:1n9 DAGs, but weak or no activity toward C16:0/C16:0, 1,3-C18:1n9/C18:1n9, C18:2/C18:2, and C18:3n3/C18:3n3 DAGs
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additional information
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distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. Unsaturated acyl CoAs, particularly polyunsaturated acyl CoAs, are the preferred substrates for CrDGTT1. CrDGTT1 has a considerably higher activity toward C16:1 than C16:0. For C18 CoAs, CrDGTT1 has the greatest activity toward C18:3n, followed by C18:2, C18:1n9, and C18:0. CrDGTT1 prefers shorter-chain acyl CoAs when the number of double bonds is the same, for instance, C16:0 and C16:1 result in a greater level of TAG accumulation than C18:0 and C18:1, respectively. CrDGTT1 is also shown to have strong activity toward C20:5n3 and C22:6n3 CoAs. When using C18:3n6(d6) CoA as the acyl donor, CrDGTT1 shows strong and comparable activity toward C16:1/C16:1, C18:1n9/C16:0, C16:0/C18:1n9, and C18:1n9/C18:1n9 DAGs, but weak or no activity toward C16:0/C16:0, 1,3-C18:1n9/C18:1n9, C18:2/C18:2, and C18:3n3/C18:3n3 DAGs
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additional information
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distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. Unsaturated acyl CoAs, particularly polyunsaturated acyl CoAs, are the preferred substrates for CrDGTT1. CrDGTT1 has a considerably higher activity toward C16:1 than C16:0. For C18 CoAs, CrDGTT1 has the greatest activity toward C18:3n, followed by C18:2, C18:1n9, and C18:0. CrDGTT1 prefers shorter-chain acyl CoAs when the number of double bonds is the same, for instance, C16:0 and C16:1 result in a greater level of TAG accumulation than C18:0 and C18:1, respectively. CrDGTT1 is also shown to have strong activity toward C20:5n3 and C22:6n3 CoAs. When using C18:3n6(d6) CoA as the acyl donor, CrDGTT1 shows strong and comparable activity toward C16:1/C16:1, C18:1n9/C16:0, C16:0/C18:1n9, and C18:1n9/C18:1n9 DAGs, but weak or no activity toward C16:0/C16:0, 1,3-C18:1n9/C18:1n9, C18:2/C18:2, and C18:3n3/C18:3n3 DAGs
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additional information
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distinct substrate specificities of three DGTT isozymes, overview. CrDGTT1 prefers polyunsaturated acyl CoAs, CrDGTT2 prefers monounsaturated acyl CoAs, and CrDGTT3 prefers C16 CoAs. When diacylglycerol is used as the substrate, CrDGTT1 prefers C16 over C18 in the sn-2 position of the glycerol backbone, but CrDGTT2 and CrDGTT3 prefer C18 over C16. Unsaturated acyl CoAs, particularly polyunsaturated acyl CoAs, are the preferred substrates for CrDGTT1. CrDGTT1 has a considerably higher activity toward C16:1 than C16:0. For C18 CoAs, CrDGTT1 has the greatest activity toward C18:3n, followed by C18:2, C18:1n9, and C18:0. CrDGTT1 prefers shorter-chain acyl CoAs when the number of double bonds is the same, for instance, C16:0 and C16:1 result in a greater level of TAG accumulation than C18:0 and C18:1, respectively. CrDGTT1 is also shown to have strong activity toward C20:5n3 and C22:6n3 CoAs. When using C18:3n6(d6) CoA as the acyl donor, CrDGTT1 shows strong and comparable activity toward C16:1/C16:1, C18:1n9/C16:0, C16:0/C18:1n9, and C18:1n9/C18:1n9 DAGs, but weak or no activity toward C16:0/C16:0, 1,3-C18:1n9/C18:1n9, C18:2/C18:2, and C18:3n3/C18:3n3 DAGs
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additional information
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isozyme CzDGAT2C displays typical DGAT activity
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additional information
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isozyme CzDGAT2C displays typical DGAT activity
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additional information
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isozyme CzDGAT2C displays typical DGAT activity
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additional information
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isozyme CzDGAT2C displays typical DGAT activity, substrate specificity of isozyme CzDGAT2C, overview
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additional information
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isozyme CzDGAT2C displays typical DGAT activity, substrate specificity of isozyme CzDGAT2C, overview
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additional information
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isozyme CzDGAT2C displays typical DGAT activity, substrate specificity of isozyme CzDGAT2C, overview
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additional information
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the enzyme exhibits substrate preference for two unsaturated fatty acids (UFAs), palmitoleic acid (C16:1) and oleic acid (C18:1)
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additional information
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isozyme CeDGAT2b from Cyperus esculentus might have a preference for unsaturated fatty acids such as oleic acid as substrates for the production of triacylglycerol (TAG) in tubers
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additional information
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increased lipid synthesis has variable effects on diacylglycerol accumulation, overview, regulation of lipid biosynthesis in cultures tissues, changes in the endogenous activity of DAGAT is unlikely to affect oil accumulation in oil palm crops, overview
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additional information
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substrate specificity of isozyme GmDGAT1A, comparison with isozyme GmDGAT2D, overview. GmDGAT1A prefers to use 18:3-acyl CoA for TAG synthesis
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additional information
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substrate specificity of isozyme GmDGAT1A, comparison with isozyme GmDGAT2D, overview. GmDGAT1A prefers to use 18:3-acyl CoA for TAG synthesis
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additional information
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substrate specificity of isozyme GmDGAT1A, comparison with isozyme GmDGAT2D, overview. GmDGAT1A prefers to use 18:3-acyl CoA for TAG synthesis
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additional information
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substrate specificity of isozyme GmDGAT2D, comparison with isozyme GmDGAT1A, overview. GmDGAT2D prefers to use oleoyl-acyl CoA and linoleoyl-acyl CoA for TAG synthesis
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additional information
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substrate specificity of isozyme GmDGAT2D, comparison with isozyme GmDGAT1A, overview. GmDGAT2D prefers to use oleoyl-acyl CoA and linoleoyl-acyl CoA for TAG synthesis
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additional information
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substrate specificity of isozyme GmDGAT2D, comparison with isozyme GmDGAT1A, overview. GmDGAT2D prefers to use oleoyl-acyl CoA and linoleoyl-acyl CoA for TAG synthesis
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additional information
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the TAG isolated from yeast producing HpDGAT2D contains about 80% of 18:1 and 16:1 and about 20% of 18:0 and 16:0, suggesting thatHpDGAT2D may have a lower preference for 16:0-containing substrate
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additional information
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the TAG isolated from yeast producing HpDGAT2D contains about 80% of 18:1 and 16:1 and about 20% of 18:0 and 16:0, suggesting thatHpDGAT2D may have a lower preference for 16:0-containing substrate
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additional information
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Haematococcus lacustris UTEX 2505
the TAG isolated from yeast producing HpDGAT2D contains about 80% of 18:1 and 16:1 and about 20% of 18:0 and 16:0, suggesting thatHpDGAT2D may have a lower preference for 16:0-containing substrate
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additional information
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the multifunctional enzyme plays an important role in lipid metabolism in human skin
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additional information
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DGAT1 is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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additional information
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the enzyme also performs the reaction of the retinol O-fatty-acyltransferase, EC 2.3.1.76
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additional information
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enzyme displays striking preference to palmitoyl-CoA and oleoyl-CoA as acyl donors and utilizes 1,2-diacylglycerol as acceptor
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additional information
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the enzyme interacts with monoacylglycerol acyltransferase-2
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additional information
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co-expressing flax diacylglycerol acyltransferase1-1 (DGAT1-1) and acyl-CoA:lysophosphatidylcholine acyltransferase1 (LPCAT1) in a yeast quintuple mutant significantly increases 18-carbon polyunsaturated fatty acids in triacylglycerol with a concomitant decrease of 18-carbon polyunsaturated fatty acids in phospholipid. The specific activity of overall LPCAT1 and DGAT1-1 coupling process exhibited a preference for transferring 14C-labeled linoleoyl or linolenoyl than oleoyl moieties from the sn-2 position of phosphatidylcholine to triacylglycerol
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additional information
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recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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additional information
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recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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additional information
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recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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additional information
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recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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additional information
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recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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additional information
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Lobosphaera incisa SAG 2468
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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additional information
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Lobosphaera incisa SAG 2468
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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additional information
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Lobosphaera incisa SAG 2468
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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additional information
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Lobosphaera incisa SAG 2468
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
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additional information
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the enzyme shows a substrate preference for monounsaturated over polyunsaturated fatty acids
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additional information
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the enzyme shows a substrate preference for monounsaturated over polyunsaturated fatty acids
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additional information
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the enzyme MtDGAT1 has a substrate preference for monounsaturated over polyunsaturated fatty acids
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additional information
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the enzyme MtDGAT1 has a substrate preference for monounsaturated over polyunsaturated fatty acids
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additional information
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Marinobacter nauticus
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the enzyme shows very low activity with ethanol, methanol, butanol, and glycerol
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additional information
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substrate specificity study, overview. The enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates for esterification into triacylglycerol (TAG). TAG fraction of the codon-optimized mMaDGAT2 transformant contains endogenous saturated fatty acids (C16:0 and C18:0) and monounsaturated fatty acids (palmitoleic acid; C16:1DELTA9 and oleic acid; C18:1DELTA9) as major proportions, which is a usual fatty acid profile of Saccharomyces cerevisiae. Medium-chain saturated fatty acids with 15- to 18-carbon atoms are substrates for mMaDGAT2. n-6 polyunsaturated fatty acids (PUFAs), linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic and arachidonic acid, are highly accumulated in TAG fraction of the mMaDGAT2 culture as compared to the n-3 PUFAs (alpha-linolenic and docosahexaenoic acid) except for C20:5 n-3 (eicosapentaenoic acid). Similar results are also obtained in the cultures fed with mixtures of n-3 PUFAs, demonstrating that mMaDGAT2 prefers eicosapentaenoic acid over gamma-linolenic and docosahexaenoic acid, respectively
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additional information
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KY859195
substrate specificity study, overview. The enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates for esterification into triacylglycerol (TAG). TAG fraction of the codon-optimized mMaDGAT2 transformant contains endogenous saturated fatty acids (C16:0 and C18:0) and monounsaturated fatty acids (palmitoleic acid; C16:1DELTA9 and oleic acid; C18:1DELTA9) as major proportions, which is a usual fatty acid profile of Saccharomyces cerevisiae. Medium-chain saturated fatty acids with 15- to 18-carbon atoms are substrates for mMaDGAT2. n-6 polyunsaturated fatty acids (PUFAs), linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic and arachidonic acid, are highly accumulated in TAG fraction of the mMaDGAT2 culture as compared to the n-3 PUFAs (alpha-linolenic and docosahexaenoic acid) except for C20:5 n-3 (eicosapentaenoic acid). Similar results are also obtained in the cultures fed with mixtures of n-3 PUFAs, demonstrating that mMaDGAT2 prefers eicosapentaenoic acid over gamma-linolenic and docosahexaenoic acid, respectively
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additional information
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substrate specificity study, overview. The enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates for esterification into triacylglycerol (TAG). TAG fraction of the codon-optimized mMaDGAT2 transformant contains endogenous saturated fatty acids (C16:0 and C18:0) and monounsaturated fatty acids (palmitoleic acid; C16:1DELTA9 and oleic acid; C18:1DELTA9) as major proportions, which is a usual fatty acid profile of Saccharomyces cerevisiae. Medium-chain saturated fatty acids with 15- to 18-carbon atoms are substrates for mMaDGAT2. n-6 polyunsaturated fatty acids (PUFAs), linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic and arachidonic acid, are highly accumulated in TAG fraction of the mMaDGAT2 culture as compared to the n-3 PUFAs (alpha-linolenic and docosahexaenoic acid) except for C20:5 n-3 (eicosapentaenoic acid). Similar results are also obtained in the cultures fed with mixtures of n-3 PUFAs, demonstrating that mMaDGAT2 prefers eicosapentaenoic acid over gamma-linolenic and docosahexaenoic acid, respectively
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additional information
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substrate specificity study, overview. The recombinant enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates with different position and number of double bonds in their acyl chains for esterification into triacylglycerol (TAG). The n-6 polyunsaturated fatty acids (PUFAs) with 18 and 20 carbon atoms, including linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic acid (DGLA ) and arachidonic acid are incorporated into the TAG fraction in recombinantly expressing yeast cells. Among n-3 PUFAs tested, the MaDGAT2 enzyme prefers eicosapentaenoic acid (EPA) substrate regarding its highly proportion found in the TAG fraction. DGLA and EPA can be efficiently used as substrates by MaDGAT2
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additional information
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KY859195
substrate specificity study, overview. The recombinant enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates with different position and number of double bonds in their acyl chains for esterification into triacylglycerol (TAG). The n-6 polyunsaturated fatty acids (PUFAs) with 18 and 20 carbon atoms, including linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic acid (DGLA ) and arachidonic acid are incorporated into the TAG fraction in recombinantly expressing yeast cells. Among n-3 PUFAs tested, the MaDGAT2 enzyme prefers eicosapentaenoic acid (EPA) substrate regarding its highly proportion found in the TAG fraction. DGLA and EPA can be efficiently used as substrates by MaDGAT2
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additional information
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substrate specificity study, overview. The recombinant enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates with different position and number of double bonds in their acyl chains for esterification into triacylglycerol (TAG). The n-6 polyunsaturated fatty acids (PUFAs) with 18 and 20 carbon atoms, including linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic acid (DGLA ) and arachidonic acid are incorporated into the TAG fraction in recombinantly expressing yeast cells. Among n-3 PUFAs tested, the MaDGAT2 enzyme prefers eicosapentaenoic acid (EPA) substrate regarding its highly proportion found in the TAG fraction. DGLA and EPA can be efficiently used as substrates by MaDGAT2
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additional information
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substrate specificity study, overview. The recombinant enzyme expressed in yeast mutant cells has a broad specificity on saturated and unsaturated fatty acid substrates with different position and number of double bonds in their acyl chains for esterification into triacylglycerol (TAG). The n-6 polyunsaturated fatty acids (PUFAs) with 18 and 20 carbon atoms, including linoleic acid, gamma-linolenic acid, dihomo gamma-linolenic acid (DGLA ) and arachidonic acid are incorporated into the TAG fraction in recombinantly expressing yeast cells. Among n-3 PUFAs tested, the MaDGAT2 enzyme prefers eicosapentaenoic acid (EPA) substrate regarding its highly proportion found in the TAG fraction. DGLA and EPA can be efficiently used as substrates by MaDGAT2
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additional information
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increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
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additional information
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increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
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additional information
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increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
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additional information
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DGAT is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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additional information
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DGAT is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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additional information
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DGAT1 is also catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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additional information
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DGAT1 is also catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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additional information
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DGAT1 is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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additional information
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DGAT1 is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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additional information
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enzyme mediates the transesterification of diacylglycerol using long-chain acyl-CoA as acyl donors. In addition, it functions as mycolyltransferase, a docking model suggests that palmitoleoyl-coenzyme A and 1,2-dipalmitin occupy the same active site as trehalose 6,6-dimycolate and trehalose 6-monomycolate
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additional information
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enzyme mediates the transesterification of diacylglycerol using long-chain acyl-CoA as acyl donors. In addition, it functions as mycolyltransferase, a docking model suggests that palmitoleoyl-coenzyme A and 1,2-dipalmitin occupy the same active site as trehalose 6,6-dimycolate and trehalose 6-monomycolate
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additional information
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enzyme mediates the transesterification of diacylglycerol using long-chain acyl-CoA as acyl donors. In addition, it functions as mycolyltransferase, a docking model suggests that palmitoleoyl-coenzyme A and 1,2-dipalmitin occupy the same active site as trehalose 6,6-dimycolate and trehalose 6-monomycolate
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additional information
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increased lipid synthesis has variable effects on diacylglycerol accumulation, overview, regulation of lipid biosynthesis in cultures tissues, changes in the endogenous activity of DAGAT is unlikely to affect oil accumulation in oil palm crops, overview
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additional information
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DGAT3 protein has two catalytic domains: a wax ester synthase-like acyl-CoA acyltransferase domain and a bacteria-specific acyltransferase domain and shows a significant preference to endogenous benzeneacetic acid and octadecenoic acid
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additional information
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in vitro and in vivo assays reveals that PtWS/DGAT, functioning as either a wax synthase (WS) or a diacylglycerol acyltransferase (DGAT), exhibits a preference on saturated fatty acid substrate
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additional information
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in vitro and in vivo assays reveals that PtWS/DGAT, functioning as either a wax synthase (WS) or a diacylglycerol acyltransferase (DGAT), exhibits a preference on saturated fatty acid substrate
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additional information
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in vitro and in vivo assays reveals that PtWS/DGAT, functioning as either a wax synthase (WS) or a diacylglycerol acyltransferase (DGAT), exhibits a preference on saturated fatty acid substrate
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additional information
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no activity with sn-1,3-diacylglycerols, acyl-CoA specificity, overview
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additional information
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the enzyme prefers unsaturated fatty acids over saturated ones
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additional information
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the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
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additional information
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the enzyme prefers unsaturated fatty acids over saturated ones
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additional information
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the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
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additional information
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isozyme substrate specificities, overview
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additional information
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isozyme substrate specificities, overview
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additional information
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Rhodotorula toruloides CGMCC 2.1389
isozyme substrate specificities, overview
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additional information
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Rhodotorula toruloides CGMCC 2.1389
isozyme substrate specificities, overview
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additional information
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in castor bean DGAT2 is more likely to play a major role in seed triacylglycerol biosynthesis than DGAT1
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additional information
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mechanism for the degradation of the DGAT protein, overview
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additional information
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the purified enzyme AtfG25 shows acyltransferase activity with C12- or C16-acyl-CoA, C12 to C18 alcohols (ethanol, butanol, hexanol, octanol, decanol, dodecanol, tetradecanol, hexadecanol, palmitoleyl alcohol, and octadecanol, cf. EC 2.3.1.75), and dipalmitoyl glycerol. Substrate specificity, overview. The DGAT activity of AtfG25 corresponds to about 70% of its wax synthase activity
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additional information
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docking of palmitoyl-CoA into the donor pocket of the predicted tDGAT structure shows that the palmitoyl moiety is sandwiched between alpha5 helix and the beta sheet formed by beta9 and beta10 strands
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additional information
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docking of palmitoyl-CoA into the donor pocket of the predicted tDGAT structure shows that the palmitoyl moiety is sandwiched between alpha5 helix and the beta sheet formed by beta9 and beta10 strands
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additional information
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docking of palmitoyl-CoA into the donor pocket of the predicted tDGAT structure shows that the palmitoyl moiety is sandwiched between alpha5 helix and the beta sheet formed by beta9 and beta10 strands
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additional information
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the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
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additional information
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the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
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additional information
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the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
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additional information
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the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity of wax synthase activity, overview
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additional information
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the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity of wax synthase activity, overview
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additional information
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the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity of wax synthase activity, overview
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additional information
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Thraustochytrium roseum ATCC28210
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the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity of wax synthase activity, overview
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additional information
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recombinant TmDGAT1 protein is capable of utilizing a range of (14)C-labelled fatty acyl-CoA donors and diacylglycerol acceptors, and can synthesize (14)C-trierucin
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additional information
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recombinant TmDGAT1 protein is capable of utilizing a range of (14)C-labelled fatty acyl-CoA donors and diacylglycerol acceptors, and can synthesize (14)C-trierucin
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additional information
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DGAT is also catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22
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additional information
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acyl-CoA substrate specificity analysis of wild-type and mutant enzymes, overview. Dga1p enzymes can integrate saturated substrates of different length. Dga1p prefers long chain saturated acyl-CoAs as acyl donors in vitro. Also mutant Dga1pDELTA85 is less efficiently with the C12:0-CoA substrate than with longer substrates
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additional information
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acyl-CoA substrate specificity analysis of wild-type and mutant enzymes, overview. Dga1p enzymes can integrate saturated substrates of different length. Dga1p prefers long chain saturated acyl-CoAs as acyl donors in vitro. Also mutant Dga1pDELTA85 is less efficiently with the C12:0-CoA substrate than with longer substrates
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additional information
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acyl-CoA substrate specificity analysis of wild-type and mutant enzymes, overview. Dga1p enzymes can integrate saturated substrates of different length. Dga1p prefers long chain saturated acyl-CoAs as acyl donors in vitro. Also mutant Dga1pDELTA85 is less efficiently with the C12:0-CoA substrate than with longer substrates
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additional information
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acyl-CoA substrate specificity analysis of wild-type and mutant enzymes, overview. Dga1p enzymes can integrate saturated substrates of different length. Dga1p prefers long chain saturated acyl-CoAs as acyl donors in vitro. Also mutant Dga1pDELTA85 is less efficiently with the C12:0-CoA substrate than with longer substrates
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