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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 + acyl-CoA
triacylglycerol + 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-diolein + palmitoyl-CoA
1,2-dioleoyl-3-palmitoyl-sn-glycerol + CoA
1,2-dioleoyl-sn-glycerol + oleoyl-CoA
1,2,3-trioleoyl-sn-glycerol + CoA
-
-
-
-
?
1,2-dioleoyl-sn-glycerol + oleoyl-CoA
triolein + 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 + oleoyl-CoA
triolein + 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 + stearoyl-CoA
1,2-dioleoyl-3-stearoylglycerol + CoA
-
about 10% of the activity with palmitoyl-CoA
-
-
?
1,2-dipalmitoyl-rac-glycerol + palmitoyl-CoA
rac-tripalmitoylglycerol + 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-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
1-palmitoyl-2-oleoylglycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
?
2,3-diacylglycerol + acyl-CoA
triacylglycerol + CoA
acetyl-CoA + 1,2-diacetyl-sn-glycerol
CoA + triacetylglycerol
-
-
-
-
?
acyl-CoA + 1,2-di-alpha-linolenoyl-sn-glycerol
CoA + 1,2-di-alpha-linolenoyl-3-acylglycerol
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-diacylglycerol
CoA + triacylglycerol
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-dilinoleoyl-sn-glycerol
CoA + 1,2-dilinoleoyl-3-acylglycerol
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-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
acyl-CoA + 1,2-dioleoylglycerol
CoA + 3-acyl-1,2-dioleoylglycerol
acyl-CoA + 1,2-dipalmitin
CoA + 3-acyl-1,2-dipalmitoylglycerol
-
no acceptor
-
-
?
acyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-acylglycerol
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 + 1,3-dioleoyl-sn-glycerol
CoA + 1,3-dioleoyl-2-acylglycerol
acyl-CoA + 1,3-dioleoylglycerol
CoA + 2-acyl-1,3-dioleoylglycerol
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 + 2-monoacylglycerol
CoA + diacylglycerol
-
-
-
-
?
acyl-CoA + 2-oleoylglycerol
CoA + 3-acyl-2-oleoylglyerol
-
-
-
-
?
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 + glycerol
CoA + acylglycerol
-
-
-
-
?
acyl-CoA + hexadecanol
? + CoA
-
-
-
?
acyl-CoA + hexadecanol
CoA + ?
-
-
-
-
?
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
-
-
?
acyl-CoA + rac-1,2-dioleoylglycerol
CoA + 3-acyl-rac-1,2-dioleoylglycerol
acyl-CoA + sn-1,2-diolein
CoA + acyl-sn-1,2-diolein
acyl-CoA + sn-2-monoolein
CoA + ?
alpha-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-alpha-linolenoylglycerol
alpha-linolenoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-linolenoyl-sn-glycerol
100% activity
-
-
?
arachidonoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-arachidnoylglycerol
arachidonoyl-CoA + 1,2-diacylglycerol
CoA + 3-arachidonoyl-1,2-diacylglycerol
butyryl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-butyrylglycerol
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
diolein + hexacosanoyl-CoA
?
-
-
-
-
?
diolein + oleoyl-CoA
triolein + CoA
-
-
-
-
?
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-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
erucoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 3-erucoyl-1,2-dioleoyl-sn-glycerol
-
-
-
-
?
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
hexanoyl-CoA + 1,2-dipalmitoyl glycerol
coenzyme A + 1,2-dipalmitoyl-3-hexanoyl glycerol
-
-
-
-
r
lauroyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-lauroylglycerol
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-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
linoleoyl-CoA + 1,2-dioleoyl-sn-glycerol
1,2-dioleoyl-3-linoleoyl-sn-glycerol + CoA
-
-
-
-
?
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 + 3-linoleoyl-1,2-dioleoylglycerol
-
i.e. diolein
-
?
myristoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-myristoylglycerol
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-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-diacyl-sn-glycerol
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
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
triolein + 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
-
-
?
oleoyl-CoA + 1,2-oleoyl-sn-glycerol
CoA + 1,2,3-trioleoylglycerol
oleoyl-CoA + diolein
CoA + triolein
oleoyl-CoA + sn-1,2-dioleoylglycerol
triolein + CoA
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1,2-dioleoyl-sn-glycerol
palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
palmitoleoyl-CoA + 1,2-dipalmitoleoyl-sn-glycerol
CoA + tripalmitoleoylglycerol
-
preferred substrate for isoform DGAT2
-
-
?
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-diacylglycerol
CoA + 1,2-diacyl-3-palmitoylglycerol
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-dipalmitin
CoA + tripalmitin
palmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2,3-tripalmitoylglycerol
-
-
-
-
?
palmitoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 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 + 1,3-dipalmitin
CoA + tripalmitin
-
-
-
-
?
palmitoyl-CoA + 1-monoolein
CoA + ?
-
-
-
-
?
palmitoyl-CoA + 1-monopalmitin
CoA + ?
-
-
-
-
?
palmitoyl-CoA + 1-monostearin
CoA + ?
-
-
-
-
?
palmitoyl-CoA + 11-cis-retinol
?
-
-
-
-
?
palmitoyl-CoA + 13-cis-retinol
?
-
-
-
-
?
palmitoyl-CoA + all-trans-retinol
?
-
-
-
-
?
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 + hexadecanol
hexadecyl palmitate + CoA
Marinobacter nauticus
-
-
-
-
?
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 + acyl-CoA
triacylglycerol + CoA
sn-1,2-diacylglycerol + erucoyl-CoA
triacylglycerol + CoA
-
i.e. a 22:1cisDELTA13-CoA
-
-
?
stearoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-stearoylglycerol
stearoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-stearoylglycerol
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-stearoylglycerol
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
-
-
?
additional information
?
-
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
role in leaf metabolism, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Cuphea sp.
-
-
-
-
?
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
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
?
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
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
acyl-CoA specificity, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
-
-
?
1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
about 90% of the activity with palmitoyl-CoA
-
-
?
1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
-
-
-
?
1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
-
-
-
?
1,2-dioleoylglycerol + oleoyl-CoA
triolein + 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
-
-
-
-
?
2,3-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
2,3-diacylglycerol + acyl-CoA
triacylglycerol + 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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
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
-
-
-
?
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 + 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
-
-
-
?
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-diacyl-sn-glycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
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
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
?
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
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
last step of triacylglycerol synthesis
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
?
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
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
?
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-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
-
-
-
-
?
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
-
-
-
-
?
acyl-CoA + sn-1,2-diolein
CoA + acyl-sn-1,2-diolein
-
-
-
-
?
acyl-CoA + sn-1,2-diolein
CoA + acyl-sn-1,2-diolein
-
-
-
-
?
acyl-CoA + sn-2-monoolein
CoA + ?
-
-
-
-
?
acyl-CoA + sn-2-monoolein
CoA + ?
-
-
-
-
?
acyl-CoA + sn-2-monoolein
CoA + ?
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
dihomo gamma-linolenoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-dihomo-gamma-linolenoylglycerol
-
-
-
?
diolein + acyl-CoA
?
-
-
-
?
diolein + acyl-CoA
?
-
-
-
?
diolein + acyl-CoA
?
-
-
-
-
?
diolein + acyl-CoA
?
Cuphea sp.
-
-
-
-
?
diolein + acyl-CoA
?
-
-
-
-
?
diolein + acyl-CoA
?
-
-
-
?
diolein + acyl-CoA
?
-
-
-
-
?
diolein + acyl-CoA
?
-
-
-
-
?
diolein + acyl-CoA
?
-
-
-
?
diolein + acyl-CoA
?
-
-
-
-
?
diolein + acyl-CoA
?
-
-
-
-
?
diolein + acyl-CoA
?
-
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
-
?
dipalmitin + acyl-CoA
?
Cuphea sp.
-
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
-
?
dipalmitin + acyl-CoA
?
-
-
-
-
?
erucoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
-
-
-
-
?
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
-
-
-
-
?
erucoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-erucoylglycerol
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
lauroyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-lauroylglycerol
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
oleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-oleoylglycerol
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-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
-
-
-
?
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 + 1,2-dioleoyl-sn-glycerol
CoA + triolein
-
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
-
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + triolein
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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-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-1,2-dioleoylglycerol
triolein + CoA
-
-
-
-
?
oleoyl-CoA + sn-1,2-dioleoylglycerol
triolein + CoA
-
-
-
-
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1,2-dioleoyl-sn-glycerol
-
-
-
-
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1,2-dioleoyl-sn-glycerol
-
-
-
-
?
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
best substrate
-
-
?
palmitoleoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-palmitoleoylglycerol
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
-
-
-
-
?
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-dipalmitin
CoA + tripalmitin
-
-
-
-
?
palmitoyl-CoA + 1,2-dipalmitin
CoA + tripalmitin
-
-
-
-
?
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
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sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
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sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
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the final step in triacylglycerol synthesis is catalyzed by the acyl-CoA:diacylglycerol acyltransferase enzymes, DGAT1 and DGAT2
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sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
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the enzyme contains a neutral lipid binding sequence 80FLVLGVAC87 residing in the first transmembrane domain
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stearoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-stearoylglycerol
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stearoyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2-diacyl-3-stearoylglycerol
high activity
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stearoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-stearoylglycerol
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weak donor
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stearoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-stearoylglycerol
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weak donor
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
fluorescent assay method using NBD-tagged diglycerol substrate
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
fluorescent assay method using NBD-tagged diglycerol substrate
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoyl-sn-glycerol
fluorescent assay method using NBD-tagged diglycerol substrate
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?
stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoylglycerol
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoylglycerol
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stearoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-stearoylglycerol
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i.e. diolein
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additional information
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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
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additional information
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enzyme also has acyl-CoA-monoacylglycerol acyltransferase activity, sn-1 and sn-3 positions are accepted with higher specificity than sn-2 position
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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acyl-CoA specificity, overview
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additional information
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acyl-CoA specificity, overview
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additional information
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bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
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additional information
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bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
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additional information
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bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
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additional information
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bifunctional wax synthase/DGAT, which predominantly catalyzes the formation of wax esters, cf. EC 2.3.1.75
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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acyl-CoA specificity, overview
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additional information
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acyl-CoA specificity, overview
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additional information
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acyl-CoA specificity, overview
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the acyl-CoA binding site is located at N-terminal domain of DGAT1 along amino acid residues 81 to 113
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additional information
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the acyl-CoA binding site is located at N-terminal domain of DGAT1 along amino acid residues 81 to 113
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additional information
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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
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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. 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
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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. 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
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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. 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
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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. 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
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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. 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
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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. 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
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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. 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
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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. 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
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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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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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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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acyl-CoA specificity, overview
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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
?
-
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
-
-
-
additional information
?
-
-
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
-
-
-
additional information
?
-
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
-
-
-
additional information
?
-
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
-
-
-
additional information
?
-
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
-
-
-
additional information
?
-
recombinant isozyme LiDGAT2.2 shows significant triacylglycerol (TAG) production in response to exogenous arachidonic acid
-
-
-
additional information
?
-
the enzyme shows a substrate preference for monounsaturated over polyunsaturated fatty acids
-
-
?
additional information
?
-
-
the enzyme shows a substrate preference for monounsaturated over polyunsaturated fatty acids
-
-
?
additional information
?
-
the enzyme MtDGAT1 has a substrate preference for monounsaturated over polyunsaturated fatty acids
-
-
-
additional information
?
-
-
the enzyme MtDGAT1 has a substrate preference for monounsaturated over polyunsaturated fatty acids
-
-
-
additional information
?
-
Marinobacter nauticus
-
the enzyme shows very low activity with ethanol, methanol, butanol, and glycerol
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
-
-
?
additional information
?
-
increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
-
-
?
additional information
?
-
-
increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
calnexin is a DGAT2-interacting protein
-
-
-
additional information
?
-
-
calnexin is a DGAT2-interacting protein
-
-
-
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
no activity with sn-1,3-diacylglycerols, acyl-CoA specificity, overview
-
-
?
additional information
?
-
-
the enzyme prefers unsaturated fatty acids over saturated ones
-
-
?
additional information
?
-
-
the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
-
-
?
additional information
?
-
-
the enzyme prefers unsaturated fatty acids over saturated ones
-
-
?
additional information
?
-
-
the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
-
-
?
additional information
?
-
isozyme substrate specificities, overview
-
-
-
additional information
?
-
isozyme substrate specificities, overview
-
-
-
additional information
?
-
isozyme substrate specificities, overview
-
-
-
additional information
?
-
isozyme substrate specificities, overview
-
-
-
additional information
?
-
-
in castor bean DGAT2 is more likely to play a major role in seed triacylglycerol biosynthesis than DGAT1
-
-
?
additional information
?
-
-
mechanism for the degradation of the DGAT protein, overview
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
-
-
?
additional information
?
-
-
the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
-
-
?
additional information
?
-
the enzyme uses oleic, palmitic, stearic, and linoleic acid with different activities
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
DGAT is also catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
1,2-dioleoylglycerol + oleoyl-CoA
triolein + CoA
-
-
-
-
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
1,2-diricinoleoyl-sn-glycerol + ricinoleoyl-CoA
triricinolein + CoA
-
-
-
-
?
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-diacylglycerol
CoA + triacylglycerol
acyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + 1,2-oleoyl-3-acylglycerol
acyl-CoA + 2-monoacylglycerol
CoA + diacylglycerol
-
-
-
-
?
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-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-palmitoyl-2-oleoylglycerol
-
-
-
-
?
sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
additional information
?
-
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
role in leaf metabolism, overview
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
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
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
Cuphea sp.
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
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
-
-
-
-
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
-
-
-
-
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
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
-
-
-
?
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 + 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
-
-
-
?
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-diacyl-sn-glycerol
CoA + triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
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
-
last step of triacylglycerol synthesis
-
-
?
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
-
last reaction in triacylglycerol synthesis
-
-
?
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
-
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
-
-
?
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
CoA + trioleoylglycerol
-
-
-
?
sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
-
-
-
?
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
-
-
?
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 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
?
-
-
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
-
-
?
additional information
?
-
-
the multifunctional enzyme plays an important role in lipid metabolism in human skin
-
-
?
additional information
?
-
increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
-
-
?
additional information
?
-
increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
-
-
?
additional information
?
-
-
increasing the cytoplasmic triglyceride pool in hepatocytes does not directly influence VLDL triglyceride or apoB production, overview
-
-
?
additional information
?
-
calnexin is a DGAT2-interacting protein
-
-
-
additional information
?
-
-
calnexin is a DGAT2-interacting protein
-
-
-
additional information
?
-
-
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
-
-
?
additional information
?
-
-
in castor bean DGAT2 is more likely to play a major role in seed triacylglycerol biosynthesis than DGAT1
-
-
?
additional information
?
-
-
mechanism for the degradation of the DGAT protein, overview
-
-
?
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(1R,2R)-2-[4'-[(phenylcarbamoyl)amino][1,1'-biphenyl]-4-carbonyl]cyclopentane-1-carboxylic acid
-
(2alpha,3beta)-2,3-dihydroxyurs-12-en-28-oic acid
-
IC50: 0.0443 mM
(2E)-1-[2,4-dihydroxy-6-methoxy-3-[(2R)-5-methyl-2-(1-methylethenyl)hex-4-en-1-yl]phenyl]-3-(2,4-dihydroxyphenyl)prop-2-en-1-one
-
IC50: 0.0098 mM
(2E,4Z,8E)-N-[9-(3,4-methylenedioxyphenyl)-2,4,8-nonatrienoyl]piperidine
-
IC50: 0.0298 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
(2R,3R)-2-(2,4-Dihydroxy-phenyl)-3,7-dihydroxy-8-((R)-5-hydroxy-2-isopropenyl-5-methyl-hexyl)-5-methoxy-chroman-4-one
-
i.e. kushenol H, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.142 mM
(2R,3S)-2-(2,4-Dihydroxy-phenyl)-3,7-dihydroxy-8-((R)-5-hydroxy-2-isopropenyl-5-methyl-hexyl)-5-methoxy-chroman-4-one
-
i.e. kushenol K, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.250 mM
(2S)-1-(3-[[(2S)-1-ethoxy-4-phenylbutan-2-yl]sulfamoyl]anilino)-4-methyl-1-oxopentan-2-yl 2,2-dimethylpropanoate
-
-
(2S)-1-[(1-[[(1S)-1-(3-cyclopropyl-1,2,4-oxadiazol-5-yl)-3-phenylpropyl]carbamoyl]cyclopentyl)amino]-4-methyl-1-oxopentan-2-yl 2,2-dimethylpropanoate
-
-
(4-[4-[4-(2-amino-5-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
-
(4-[4-[4-(3-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
-
(4-[4-[4-(5-chloro-2-nitrobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
-
(4-[4-[4-([[2-fluoro-5-(trifluoromethyl)phenyl]carbamoyl]amino)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)acetic acid
-
(4S,7R)-4-(5,5-dimethyl-4-oxo-4,5-dihydrofuran-2-yl)-2,2-dimethyl-4,7-bis[(4E)-4-methyl-5-[(2R)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]pent-4-en-1-yl]-4,5,6,7-tetrahydro-1-benzofuran-3(2H)-one
89.23% inhibition
(trans-4-(4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
inhibitor displays good metabolic stability and high intestinal permeability values
(trans-4-(4-[(5-cyclopentylethyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
-
(trans-4-(4-[(5-cyclopentylmethyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
-
(trans-4-(4-[(5-[1-fluorobenzyl]-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
inhibitor displays good metabolic stability and high intestinal permeability values
(trans-4-(4-[(5-[2-chlorobenzyl]-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
inhibitor displays good metabolic stability and high intestinal permeability values
(trans-4-(4-[(5-[2-fluorobenzyl]-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl)cyclohexyl)acetic acid
-
inhibitor displays good metabolic stability and high intestinal permeability values
(trans-4-[4-[(3-benzyl-1,2,4-oxadiazol-5-yl)carbamoyl]phenyl]cyclohexyl)acetic acid
-
-
(trans-4-[4-[(5-benzyl-1,2,4-oxadiazol-3-yl)carbamoyl]phenyl]cyclohexyl)acetic acid
-
-
(trans-4-[4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenyl]cyclohexyl)acetic acid
-
-
1,2-diacyl-sn-glycerol
-
dicaprin, dimyristin, dipalmitin, high concentration
1-acyl-sn-glycero-3-phosphocholine
-
activation, at low concentrations, inhibition above 0.2 mM
1-O-Hexadecyl-2-oleoyl-sn-glycerol
-
competitive
1-O-Hexadecylpropanediol-3-phosphocholine
-
activation, low concentration, inhibitory at high concentration
1-[2,4-dihydroxy-3-(2-isopropenyl-5-methyl-hex-4-enyl)-6-methoxy-phenyl]-3-(2,4-dihydroxy-phenyl)-propenone
-
i.e. kuraridin, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.099 mM
2-(2,4-dihydroxy-phenyl)-7-hydroxy-8-(2-isopropenyl-5-methyl-hex-4-enyl)-5-methoxy-chroman-4-one
-
i.e. kurarinone, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.0109 mM
2-(2,4-dihydroxy-phenyl)-7-hydroxy-8-[2-(3-hydroxy-3-methyl-butyl)-3-methyl-but-3-enyl]-5-methoxy-chroman-4-one
-
i.e. kurarinol, prenylflavonoid from Sophora flavescens, 50% inhibition at 0.0086 mM
3,5-dimethyl-6-([(6E)-6-methyl-7-[(2S)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]hept-6-en-1-yl]oxy)pyrazine-2-carboxamide
-
3-(4-[4-[4-(3-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexyl)propanoic acid
-
3-oxoolean-12-en-27-oic acid
-
the compound exhibits strong inhibition efficacy towards diacylglycerol acyltransferases 1 and 2, and acts competitively against oleoyl-CoA in vitro
3alpha-hydroxyolean-12-en-27-oic acid
-
-
3beta-hydroxyolean-12-en-27-oic acid
-
-
4-amino-6-[(4E)-4-methyl-5-[(2R)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]pent-4-en-2-yn-1-yl]-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-5(6H)-one
-
4-amino-6-[(4E)-4-methyl-5-[(2S)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]pent-4-en-2-yn-1-yl]-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-5(6H)-one
-
4-[(4-chloro-3-fluorophenyl)methyl]-N-[2-(3,4-diethoxyphenyl)ethyl]-4H-thieno[3,2-b]pyrrole-5-carboxamide
-
EC value is 0.000009 mM
4-[4-(4-[[2-phenyl-5-(trifluoromethyl)-1,3-oxazole-4-carbonyl]amino]phenyl)piperidine-1-carbonyl]cyclohexane-1-carboxylic acid
-
4-[4-[4-(3-chlorobenzamido)phenyl]thieno[3,2-d]pyrimidin-7-yl]cyclohexane-1-carboxylic acid
-
5,5'-dithio-bis(2-nitrobenzoic acid)
6,8-diprenylgenistein
-
IC50: 0.0067 mg/ml
7beta-(3-ethyl-cis-crotonoyloxy)-1alpha-(2-methylbutyryloxy)-3,14-dehydro-Z-notonipetranone
8-angeloyloxy-3,4-epoxy-bisabola-7(14),10-dien-2-one
8-prenylleutone
-
IC50: 0.015 mg/ml
aceriphyllic acid A
-
the compound exhibits strong inhibition efficacy towards diacylglycerol acyltransferases 1 and 2, and acts competitively against oleoyl-CoA in vitro
alpinumisoflavone
-
23% inhibition at 0.0125 mg/ml
ATP
-
ATP-dependent activity reduces activity in vitro by 30-40%
auriculatin
-
IC50: 0.0072 mg/ml
brachynereolide
-
IC50: 0.25 mM, above
cetyltrimethylammonium bromide
-
-
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetic acid
-
cis-4-(4-[[5-(cyclopentylamino)-1,3,4-thiadiazol-2-yl]carbamoyl]phenoxy)cyclohexane-1-carboxylic acid
-
-
cis-4-([5-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]pyridin-2-yl]oxy)cyclohexane-1-carboxylic acid
-
-
cis-4-[4-([3-[(3,5-difluorophenyl)methyl]-1,2,4-oxadiazol-5-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-([5-[(3,5-difluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-([5-[(cyclopentyloxy)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-[(3-benzyl-1,2,4-oxadiazol-5-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-[(5-anilino-1,3,4-thiadiazol-2-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
-
-
cis-4-[[5-([5-[(3-chlorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)pyridin-2-yl]oxy]cyclohexane-1-carboxylic acid
-
-
crepidiaside C
-
IC50: 0.25 mM, above
cryptotanshinone
-
IC50: 0.0273 mM
dehydropipernonaline
-
noncompetitive inhibition, IC50: 0.0212 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
derrone
-
IC50: 0.0151 mg/ml
erysenegalensein D
-
IC50: 0.0015 mg/ml
erysenegalensein N
-
28% inhibition at 0.0125 mg/ml
erysenegalensein O
-
IC50: 0.0011 mg/ml
ethanol
-
43% inhibition when 0.04 ml are added to reaction mixture
ethyl 1-(1-[[(2-chlorophenyl)carbamoyl]amino]cyclohexane-1-carbonyl)piperidine-4-carboxylate
-
EC value is 0.0015 mM
ethyl 1-[N-[(2,4-dichlorophenyl)carbamoyl]-2-methylalanyl]piperidine-4-carboxylate
-
EC value is 0.00025 mM
germanicol acetate
-
IC50: 0.25 mM, above
HgCl2
-
90% at 0.03-0.05 mM, reversible by DTT
I-
-
substantial inhibition
iodoacetamide
-
15% inhibition at 1 mM, DTT protects
ixerin Y
-
IC50: 0.25 mM, above
KCl
-
500 mM, inhibits purified enzyme
lysophosphatidylcholine
-
activation at low concentrations, optimum at 0.075 mM, inhibitory above 0.2 mM
methyl 1-benzyl-3-[(furan-3-carbonyl)amino]-5-[(2-methylbutyl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 1-benzyl-3-[(furan-3-carbonyl)amino]-5-[[(thiophen-3-yl)methyl]amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 2-(4-(4-(4-((tert-butoxycarbonyl)amino)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohex-3-en-1-yl)acetate
-
methyl 2-(4-(4-(4-((tert-butoxycarbonyl)amino)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl) acetate
-
methyl 2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
methyl 2-(4-(4-(4-aminophenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
methyl 3-benzamido-1-[(furan-2-yl)methyl]-5-[(2-methylbutyl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 3-[(furan-2-carbonyl)amino]-1-(3-methylbutyl)-5-[(pentan-3-yl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 3-[(furan-3-carbonyl)amino]-1-(2-methylpropyl)-5-[(pentan-3-yl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 5-[(2,3-dihydro-1H-inden-2-yl)amino]-3-[(furan-3-carbonyl)amino]-1-(2-methylpropyl)-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 5-[[(4-acetamidophenyl)methyl]amino]-1-benzyl-3-[(furan-3-carbonyl)amino]-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl 5-[[(furan-3-yl)methyl]amino]-1-(2-methylpropyl)-3-(2-phenylacetamido)-1H-pyrrolo[2,3-b]pyridine-2-carboxylate
-
-
methyl cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
methyl trans-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
methyl ursolate
-
IC50: 0.0264 mM
Mn2+
-
73% inhibition at 2.5 mM
N-(1-[[5-tert-butyl-1-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]amino]-2-methyl-1-oxopropan-2-yl)-4-fluorobenzamide
-
-
N-(4,5-dihydronaphtho[1,2-d]thiazol-2-yl)-2-(3,4-dimethoxy phenyl)acetamide
selective inhibitor of isoform DGAT2 when used at low concentrations; selective inhibitor of isoform DGAT2 when used at low concentrations
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-(trans-4-carbamoylcyclohexyl)benzamide
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-(trans-4-[[2-(dimethylamino)ethyl]carbamoyl]cyclohexyl)benzamide
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-(trans-4-[[2-(morpholin-4-yl)ethyl]carbamoyl]cyclohexyl)benzamide
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-[trans-4-[(2,3-dihydroxypropyl)carbamoyl]cyclohexyl]benzamide
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-[trans-4-[(2-hydroxy-2-methylpropyl)carbamoyl]cyclohexyl]benzamide
-
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-[trans-4-[(2-methoxyethyl)carbamoyl]cyclohexyl]benzamide
-
-
n-octyl-beta-D-glucopyranoside
-
weak
N-[(2S)-1-ethoxy-4-phenylbutan-2-yl]-1-[2-(tricyclo[3.3.1.1~3,7~]decan-2-yl)acetamido]cyclopentane-1-carboxamide
-
-
N-[1,5-bis(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
-
-
N-[1-(3,5-dimethylphenyl)-4,5,6,7-tetrahydro-1H-indazol-4-yl]-1,2,3-thiadiazole-4-carboxamide
-
EC value is 0.10 mM
N-[1-(4-fluoro-2-methylphenyl)-5-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
-
-
N-[1-(4-fluorophenyl)-5-[2-(4-fluorophenyl)propan-2-yl]-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
-
-
N-[1-(4-hydroxyphenyl)-4,5,6,7-tetrahydro-1H-indazol-4-yl]pyridine-2-carboxamide
-
EC value is 0.00000034 mM
N-[2-(3,4-diethoxyphenyl)ethyl]-4-methyl-4H-thieno[3,2-b]pyrrole-5-carboxamide
-
EC value is 0.011 mM
N-[5-tert-butyl-1-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-(1-methylcyclopropane-1-carbonyl)alaninamide
-
-
N-[5-tert-butyl-1-(4-fluorophenyl)-1H-1,2,4-triazol-3-yl]-2-methyl-N~2~-[1-(trifluoromethyl)cyclopropane-1-carbonyl]alaninamide
-
-
oleate
-
noncompetitive inhibition, IC50: 0.0545 mM
p-chloromercuribenzene sulfonate
-
complete inhibition, DTT protects
p-chloromercuribenzoate
-
complete inhibition, DTT protects
palmitoyl-CoA
-
high concentration
phenylpyropene C
-
noncompetitive
phosphatidylethanolamine
-
-
pipernonaline
-
IC50: 0.0372 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
piperrolein B
-
IC50: 0.0201 mM, isolated from the extracts of fruits of Piper longum and Piper nigrum
retrofractamide C
-
IC50: 0.9 mM, above, isolated from the extracts of fruits of Piper longum and Piper nigrum
sesquiterpenoids
-
weak inhibition
-
Soybean trypsin inhibitor
-
-
Tergitol NP-40
-
microsomal preparation
tert-butyl (2S)-2-[[1-([(2S)-2-[(2,2-dimethylpropanoyl)oxy]-4-methylpentanoyl]amino)cyclopentane-1-carbonyl]amino]-4-phenylbutanoate
-
-
tert-butyl (4-(7-bromothieno[3,2-d]pyrimidin-4-yl)phenyl)carbamate
-
trans-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
trans-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetic acid
-
trans-4-[4-([5-[(3,5-difluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenoxy]cyclohexane-1-carboxylic acid
-
-
trans-4-[4-[(5-benzyl-1,3,4-thiadiazol-2-yl)carbamoyl]phenoxy]cyclohexane-1-carboxylic acid
-
-
Trifluoperazine
-
0.5 mM, in the presence of suboptimal phosphatidic acid concentration
[(1r,4r)-4-(4-[[5-(3,4-difluoroanilino)-1,3,4-oxadiazole-2-carbonyl]amino]phenyl)cyclohexyl]acetic acid
-
[(1r,4r)-4-[4-(4-amino-5-oxo-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-6(5H)-yl)phenyl]cyclohexyl]acetic acid
-
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
[(1r,4r)-4-[4-(6-carbamoyl-3,5-dimethylpyrazin-2-yl)phenyl]cyclohexyl]acetic acid
89.32% inhibition
[4-(4-[4-[(naphthalene-2-carbonyl)amino]phenyl]thieno[3,2-d]pyrimidin-7-yl)cyclohexyl]acetic acid
-
[4-[4-(4-[[(3-chlorophenyl)carbamoyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[4-[4-(4-[[(4-chloropyridin-2-yl)carbamoyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[4-[4-(4-[[(5-bromopyridin-3-yl)carbamoyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[4-[4-(4-[[2-phenyl-5-(trifluoromethyl)-1,3-oxazole-4-carbonyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[4-[4-(4-[[6-(trifluoromethyl)pyridine-3-carbonyl]amino]phenyl)thieno[3,2-d]pyrimidin-7-yl]cyclohexyl]acetic acid
-
[trans-4-(4-[[5-(2-cyclopentylethyl)-1,3,4-thiadiazol-2-yl]carbamoyl]phenyl)cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[(3,5-difluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[(4-fluorophenyl)methyl]-1,3,4-oxadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[(4-fluorophenyl)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[(cyclopentyloxy)methyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[2-(oxolan-2-yl)ethyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
[trans-4-[4-([5-[2-(oxolan-3-yl)ethyl]-1,3,4-thiadiazol-2-yl]carbamoyl)phenyl]cyclohexyl]acetic acid
-
-
2-Bromooctanoate
-
50% inhibition at 1.5 mM
2-Bromooctanoate
-
specific inhibition
2-Bromooctanoate
-
specific inhibition
5,5'-dithio-bis(2-nitrobenzoic acid)
-
i.e. DTNB, complete inhibition, DTT protects
5,5'-dithio-bis(2-nitrobenzoic acid)
-
11% inhibition at 1 mM
7beta-(3-ethyl-cis-crotonoyloxy)-1alpha-(2-methylbutyryloxy)-3,14-dehydro-Z-notonipetranone
-
-
7beta-(3-ethyl-cis-crotonoyloxy)-1alpha-(2-methylbutyryloxy)-3,14-dehydro-Z-notonipetranone
-
-
8-angeloyloxy-3,4-epoxy-bisabola-7(14),10-dien-2-one
-
-
8-angeloyloxy-3,4-epoxy-bisabola-7(14),10-dien-2-one
-
-
acyl-CoA
substrate inhibition is observed at higher concentrations of acyl-CoA
acyl-CoA
substrate inhibition of DGAT1, acyl-CoA binding protein AtACBP6 from Arabidopsis thaliana slightly enhances the substrate inhibition of DGAT1 at the acyl-CoA concentrations above 0.01 mM
acyl-CoA
-
C-10-CoA to C-16-CoA, high concentration
betulinic acid
-
a lupane-type triterpenoid, isolated from methanolic extracts of Alnus hirsuta, inhibition of Hep-G2 cell triacyglycerol biosynthesis
betulinic acid
-
a lupane-type triterpenoid, isolated from methanolic extracts of Alnus hirsuta, noncompetitive inhibition, IC50: 0.0096 mM
bovine serum albumin
-
binds palmitoyl-CoA and decreases activity towards palmitoyl-CoA, but not butyryl-CoA
-
bovine serum albumin
-
strong inhibition
-
bovine serum albumin
-
activation at 0.1%, inhibition at 2.5%
-
Ca2+
-
-
Ca2+
-
48% inhibition at 2.5 mM
CaCl2
5 mM, 30% inhibition
CaCl2
-
2 mM, inhibits purified enzyme but not activity in lipid body fraction
CHAPS
-
-
cholate
-
-
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
E2RDN4
-
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
CoA
above 50 mM, about 70% inhibition above 300 mM
CoA
noncompetitively inhibits isozyme BnaC.DGAT1.a. The N-terminal domain of isoform BnaA.DGAT1.b can interact with acyl-CoA at a possible allosteric site, and CoA can displace the thioester
CoA
an allosteric modulator of DGAT1, interaction with the cytoplasmic N-terminal region, overview
deoxycholate
-
-
DTT
-
above 2 mM
DTT
-
microsomal preparation
kuraridin
-
IC50: 0.0098 mM
kurarinone
-
-
kurarinone
-
IC50: 0.0048 mg/ml
Mg2+
-
-
Mg2+
-
10% inhibition at 2.5 mM, 40% at 8.0 mM
MgCl2
5 mM, 17% inhibition
MgCl2
-
5 mM, inhibits purified enzyme but not activity in lipid body fraction
MnCl2
5 mM, 30% inhibition
N-ethylmaleimide
-
95% loss of activity after preincubation with 40 mM
N-ethylmaleimide
-
inhibits solubilized enzyme, but not membrane-bound enzyme
niacin
-
30% inhibition
niacin
a specific noncompetitive DGAT2 inhibitor. Dga1p enzyme mutant versions exhibit DGAT2 specific activity, which is inhibited by niacin. The decrease is 70% for Dga1pDELTA19 and up to 99.5% for Dga1pDELTA85
oleanolic acid
-
-
oleanolic acid
-
IC50: 0.0317 mM
oleoyl-CoA
substrate inhibition
oleoyl-CoA
BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition. BnaDGAT1 is less susceptible to substrate inhibition at 0.005-0.020 mM oleoyl-CoA in the presence of 1 mg/ml BSA
oleoyl-CoA
an allosteric modulator of DGAT1, interaction with the cytoplasmic N-terminal region, overview
oleoyl-CoA
substrate inhibition
oleoyl-CoA
-
substrate inhibition
oleoyl-CoA
substrate inhibition; substrate inhibition
sodiumdodecyl sulfate
-
-
sodiumdodecyl sulfate
-
-
sodiumdodecyl sulfate
-
irreversible denaturation
Triton X-100
-
microsomal preparation
Triton X-100
-
50% inhibition at 0.1-0.2%
Triton X-100
-
above 0.05 mM
Triton X-100
-
microsomal preparation
tussilagone
-
-
tussilagonone
-
-
Tween 20
-
-
Tween 20
-
99% inhibition at 5 mg/ml, 89% inhibition at 1 mg/ml, 49% inhibition at 0.5 mg/ml
XP620
-
dihydrothiopyrancarboxamide
XP620
-
dihydrothiopyrancarboxamide
XP620
-
dihydrothiopyrancarboxamide
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
E2RDN4
-
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
-
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
-
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
-
additional information
the intrinsically disordered region (IDR) of the N-terminal domain encompasses an autoinhibitory motif. Purified BnaDGAT1 can be phosphorylated and inactivated by SnRK1
-
additional information
the intrinsically disordered region (IDR) of the N-terminal domain encompasses an autoinhibitory motif. Purified BnaDGAT1 can be phosphorylated and inactivated by SnRK1
-
additional information
the intrinsically disordered region (IDR) of the N-terminal domain encompasses an autoinhibitory motif. Purified BnaDGAT1 can be phosphorylated and inactivated by SnRK1
-
additional information
phosphorylation downregulates the activity of the enzyme
-
additional information
-
phosphorylation downregulates the activity of the enzyme
-
additional information
the highly disordered segment at the enzyme's N-terminus is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif
-
additional information
-
the highly disordered segment at the enzyme's N-terminus is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif
-
additional information
the cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites, conformational heterogeneity in the N-terminal domain of DGAT1
-
additional information
-
the cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites, conformational heterogeneity in the N-terminal domain of DGAT1
-
additional information
E2RDN4
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
additional information
-
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
additional information
-
no inhibition by Ca2+
-
additional information
design and synthesis of diacylglycerol acyltransferase 1 inhibitors based on aphadilactone C. The lactone group of aphadilactone C is introduced into the [(1r,4r)-4-[4-(4-amino-5-oxo-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-6(5H)-yl)phenyl]cyclohexyl]acetic acid and [(1r,4r)-4-[4-(6-carbamoyl-3,5-dimethylpyrazin-2-yl)phenyl]cyclohexyl]acetic acid (which have entered into clinical research) to verify whether the lactone in aphadilactone C plays the same role as carboxylic group in [(1r,4r)-4-[4-(4-amino-5-oxo-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-6(5H)-yl)phenyl]cyclohexyl]acetic acid and [(1r,4r)-4-[4-(6-carbamoyl-3,5-dimethylpyrazin-2-yl)phenyl]cyclohexyl]acetic acid. The final in vitro assay shows that the synthesized compounds have not the inhibition activity to DGAT1. This might suggest that the inhibition mechanism of aphadilactone C is not the same as of [(1r,4r)-4-[4-(4-amino-5-oxo-7,8-dihydropyrimido[5,4-f][1,4]oxazepin-6(5H)-yl)phenyl]cyclohexyl]acetic acid and [(1r,4r)-4-[4-(6-carbamoyl-3,5-dimethylpyrazin-2-yl)phenyl]cyclohexyl]acetic acid. No inhibition by 3,5-dimethyl-6-[(1E)-1-[(2S)-4-methyl-6-oxo-3,6-dihydro-2H-pyran-2-yl]prop-1-en-2-yl]pyrazine-2-carboxamide
-
additional information
-
high-throughput screening for enzyme inhibitors, quantitative-high throughput image-based assay, overview. The activity of the identified lipid storage inhibitors is evolutionary conserved. Three scaffolds: structures are characterized by a tetrahydroindazole (CT1), thienopyrrole (CT2) or arylureido (CT3) core, phenotypic analysis of thienopyrrole (CT2) treated cells
-
additional information
a series of thieno[3,2-d]pyrimidine derivatives are synthesized and their inhibitory effects against diacylglycerol acyltransferase 1 (DGAT-1) are assessed
-
additional information
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
additional information
-
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
additional information
no inhibition by selective DGAT1 inhibitor PF-04620110
-
additional information
-
no inhibition by selective DGAT1 inhibitor PF-04620110
-
additional information
DGAT2 inhibitor alone has very modest effect but inhibition of both isoforms substantially reduced 13C fatty acid incorporation into triglyceride (TG) pool in the heart. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function. A DGAT2 inhibitor does not further change substrate oxidation in DGAT1 iKO mice
-
additional information
DGAT2 inhibitor alone has very modest effect but inhibition of both isoforms substantially reduced 13C fatty acid incorporation into triglyceride (TG) pool in the heart. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function. A DGAT2 inhibitor does not further change substrate oxidation in DGAT1 iKO mice
-
additional information
-
DGAT2 inhibitor alone has very modest effect but inhibition of both isoforms substantially reduced 13C fatty acid incorporation into triglyceride (TG) pool in the heart. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function. A DGAT2 inhibitor does not further change substrate oxidation in DGAT1 iKO mice
-
additional information
-
diethyl-p-nitrophenylphosphate, diisopropyl fluorophosphate
-
additional information
-
10% v/v acetone, sn-2-monoolein
-
additional information
-
not inhibitory: hesperetin, naringenin, quercetin, kaempferol up to 0.8 mM
-
additional information
-
an ethylacetic extract of Youngia koidzumiana, a plant endemic to the Mount Chiri region of Korea, significantly inhibits the liver microsome enzyme
-
additional information
-
inhibition mechanism, the inhibitory activity of Piper fruits is influenced by the presence of the piperidine group rather than by isobutyl group, overview
-
additional information
in vivo inhibitory activity thieno[3,2-d]pyrimidine derivatives against diacylglycerol acyltransferase 1 (DGAT-1) and effects on microsomes and cytochrome P-450, overview
-
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evolution
DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOATs). The DGAT1 family is highly conserved. DGAT1 possesses a very hydrophilic N-terminal region corresponding to about the first 100 residues, which is followed by eight to ten predicted transmembrane segments
evolution
distinct evolutionary origin of Thraustochytrium roseum bifunctional wax ester synthase/acyl-CoA diacylglycerol acyltransferases (WS/DGATs) from that of plant and bacterial WS/DGATs. Both TrWSD4 and TrWSD5 contain the conserved acyltransferase active-site motif (HHXXXDG), whose first histidine residue is substituted to serine and aspartate, respectively
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 genes is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 gene is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 genes is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
evolution
diversity and evolution of plant diacylglycerol acyltransferase (DGATs), phylogenetic, gene structure, and expression analyses, overview. While one or two putative DGAT3 genes are identified in all species, a larger number of putative WS/DGAT genes are found in the majority of plant species. The pattern of gene duplication is distinct within each DGAT1, DGAT2, DGAT3 and WS/DGAT. While WS/DGAT is the most diversified gene with all plants presenting more than two WS/DGATs, DGAT3 gene is maintained as single copy in plants, except for Glycine max that has suffered gene duplication
evolution
enzyme MtDGAT1 belongs to the DGAT1 family
evolution
genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2 (isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3), and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
evolution
genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2, i.e. isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3, and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
evolution
in Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGA T3s
evolution
in Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGAT3s
evolution
phylogeny of these BnaDGAT1 gene forms. Two clades of DGAT1, which appear to have diverged relatively early in Brassicaceae's history, differ in preference for linoleoyl (18:2DELTA9cis12cis, i.e. 18:2-CoA). Phylogenetic analysis
evolution
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the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75)
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75)
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75)
evolution
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the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75)
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT1 belongs to a family of enzymes named membrane-bound O-acyltransferases (MBOAT), which are proposed to have highly conserved arginine and histidine residues
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases
evolution
the acyl-CoA-dependent formation of triacylglycerol (TAG) is performed by three DGAT gene families, DGAT1, DGAT2, and DGAT3, as well by the bifunctional enzyme WS/DGAT, that also shows wax synthase activity (EC 2.3.1.75). DGAT2 is a member of the DGAT2/acyl-CoA:monoacylglycerol acyltransferase family, which also includes acyl-CoA:monoacylglycerol acyltransferases and wax synthases
evolution
the evolutionary and sequence analyses revealed that CzDGAT1 and other green microalgal DGAT1 are closely related to the plant DGAT1 clade. But algal DGAT1 may have different evolutionary and structural features from plant and animal DGAT1 with respect to the hydrophilic N-terminal domain. This domain is predicted to be present in a less disordered state in CzDGAT1 than that of animal/plant DGAT1. The two isoforms of DGAT1 from the green microalga Chromochloris zofingiensis have very distinct features. They share 39.9% amino acid pairwise identity and have very different lengths mainly attributable to the variable N-terminal regions
evolution
the genome of oleaginous yeast Rhodosporidium toruloides contains two putative DGAT genes, RtDGATa and RtDGATb, which share little conserved amino acid coding sequence with each other. Phylogeny tree analysis shows that RtDGATa belongs to DGAT1 family and RtDGATb belongs to DGAT2 family
evolution
the major triglycerol synthesizing enzyme in Yarrowia lipolytica is Dga1p which belongs to the DGAT2 family
evolution
the principal activity of DGATs has been defined as a single-function enzyme catalyzing the esterification of diacylglycerol with acyl-CoA. A dual-function PtWS/DGAT associated with diatom Phaeodactylum tricornutum is discovered in the current study. Distinctive to documented microalgal DGAT types, PtWS/DGAT exhibits activities of both a wax ester synthase (WS) and a DGAT. WS/DGATs are broadly distributed in microalgae, with different topology and phylogeny from those of DGAT1s, DGAT2s, and DGAT3s. In Phaeodactylum tricornutum, a group of acyl-CoA:diacylglycerol acyltransferases (designated as PtDGATX) is discovered with an identity high to dual-function WS/DGAT and low to DGAT1s, DGAT2s, and DGAT3s in amino acid sequence. This suggests that the function of DGATXs differs from those of the remaining types of DGATs. In terms of topology and phylogeny, PtDGATX is more similar to WS/DGATs than to DGAT1s, DGAT2s, and DGA T3s
evolution
Thermomonospora curvata acyltransferase ACY99349 belongs to the WS/DGAT family. tDGAT contains all the conserved motifs characteristic of WS/DGAT, mainly the catalytic site 140HHaavDG146, motif I 118PLW120, and motif II 281ND282. Like in other acyl-CoA-dependent acyltransferases the catalytic motif 140HHaavDG146, in the N-terminal domain of tDGAT, is predicted to be located in the hydrophobic pocket or channel that restricts the accessibility of hydrophilic substrates
evolution
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the genome of oleaginous yeast Rhodosporidium toruloides contains two putative DGAT genes, RtDGATa and RtDGATb, which share little conserved amino acid coding sequence with each other. Phylogeny tree analysis shows that RtDGATa belongs to DGAT1 family and RtDGATb belongs to DGAT2 family
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evolution
-
the major triglycerol synthesizing enzyme in Yarrowia lipolytica is Dga1p which belongs to the DGAT2 family
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evolution
-
the major triglycerol synthesizing enzyme in Yarrowia lipolytica is Dga1p which belongs to the DGAT2 family
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evolution
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genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2, i.e. isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3, and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
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evolution
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genome analysis reveals the presence of five putative DGAT isoforms in Lobosphaera incisa, including one DGAT of type 1, three DGATs of type 2 (isozymes LiDGAT2.1, LiDGAT2.2, and LiDGAT2.3), and a single isoform of a type 3 DGAT. Five DGATs encoded by the Lobosphaera incisa genome cluster differently within the eukaryotic DGAT family
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evolution
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Thermomonospora curvata acyltransferase ACY99349 belongs to the WS/DGAT family. tDGAT contains all the conserved motifs characteristic of WS/DGAT, mainly the catalytic site 140HHaavDG146, motif I 118PLW120, and motif II 281ND282. Like in other acyl-CoA-dependent acyltransferases the catalytic motif 140HHaavDG146, in the N-terminal domain of tDGAT, is predicted to be located in the hydrophobic pocket or channel that restricts the accessibility of hydrophilic substrates
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evolution
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distinct evolutionary origin of Thraustochytrium roseum bifunctional wax ester synthase/acyl-CoA diacylglycerol acyltransferases (WS/DGATs) from that of plant and bacterial WS/DGATs. Both TrWSD4 and TrWSD5 contain the conserved acyltransferase active-site motif (HHXXXDG), whose first histidine residue is substituted to serine and aspartate, respectively
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malfunction
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enzyme-deficient mice show no effect on retinal anatomy or the ultrastructure of photoreceptor outer-segments. Enzyme loss affects retinyl-ester synthesis and total acyl-coenzyme A:retinol acyl-transferase activityin the eye
malfunction
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Isoform DGAT1 inactivation promotes large lipid droplet formation. Inhibition of isoform DGAT2 augments fatty acid oxidation, whereas inhibition of DGAT1 increases triacylglycerol secretion. Triacylglycerol secretion is significantly reduced on DGAT2 inhibition without altering extracellular apolipoprotein B levels
malfunction
a Rv3371 deletion mutant of Mtb shows impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant shows reduced formation of TAG containing extracellular vesicles
malfunction
although the N-terminal domain of algal DGAT1 is not necessary for acyltransferase activity of CzDGAT1, its removal leads to huge decreases in CzDGAT1 enzyme activity, which cannot be restored by fusion with an acyl-CoA binding protein AtACBP6 from Arabidopsis thaliana. Replacement of the N-terminal region by ACBP in CzDGAT1 (ACBP-fused CzDGAT1107-550) is not able to restore or improve the enzyme activity suggesting that the N-terminus may function as a regulatory domain rather than as an acyl-CoA binding site
malfunction
BnaDGAT161-501 and BnaDGAT181-501 exhibit higher normalized specific activity compared with the full-length enzyme. Despite the lower production level of BnaDGAT161-501 and BnaDGAT181-501, these enzyme forms are able to generate TAG amounting to about 60% of the total triacylglycerol (TAG) produced by the full-length enzyme in situ. Mutant BnaDGAT1114-501, which is devoid of the entire N-terminal domain, is about 10fold less active than the full-length enzyme. The affinity of BnaDGAT1114-501 for acyl-CoA is much lower than that of the full-length BnaDGAT1 or BnaDGAT181-501. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site
malfunction
calnexin-deficient mouse embryonic fibroblasts have reduced intracellular triacylglycerol levels and fewer large lipid droplets
malfunction
DGAT1 overexpression during seed development in Brassica napus decreases the penalty on seed oil content caused by drought
malfunction
enhanced DGAT1 expression leads to increased freezing tolerance in Arabidopsis thaliana, whereas DGAT1 deficient mutant lines are sensitive to freezing. The overexpression of DGAT1 with the mutated SnRK1 site translated to higher seed TAG levels in Arabidopsis thaliana when compared to an unmodified enzyme
malfunction
in vivo knockdown of CrDGTT1, CrDGTT2 or CrDGTT3 results in 20-35% decreases in TAG content and a reduction of specific TAG fatty acids, in agreement with the findings of the in vitro assay and fatty acid feeding test
malfunction
inactivation of DGAT1 or DGAT2 in adult mouse heart results in a moderate suppression of triglyceride (TG) synthesis and turnover. Partial inhibition of DGAT activity increases cardiac fatty acid oxidation without affecting PPARalpha signaling, myocardial energetics or contractile function. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function
malfunction
inactivation of DGAT1 or DGAT2 in adult mouse heart results in a moderate suppression of triglyceride (TG) synthesis and turnover. Partial inhibition of DGAT activity increases cardiac fatty acid oxidation without affecting PPARalpha signaling, myocardial energetics or contractile function. Coinhibition of DGAT1/2 in the heart abrogates TG turnover and protects the heart against high fat diet-induced lipid accumulation with no adverse effects on basal or dobutamine-stimulated cardiac function. Triglyceride storage is unaffected in DGAT1 inducible knockout (iKO) mice
malfunction
overexpression of PtWS/DGAT in the diatom results in increased levels of total lipids (TL) and triacylglycerol (TAG) regardless of nitrogen availability
malfunction
overexpression of YlDGA2 in a Q4 context under neosynthesis conditions causes the formation of large lipid bodies (LBs). DGAT overexpression affects LB segregation
malfunction
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phenotypic analysis of thienopyrrole (CT2) inhibitor treated cells, overview
malfunction
the overexpression of YlDGA1 generates smaller but more numerous lipid bodies (LBs), a phenotype which can be enhanced by increasing the copy number of the overexpressed gene. DGAT overexpression affects LB segregation
malfunction
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the respective gene, atfG25, is inactivated in Streptomyces sp. strain G25, cells of the insertion mutant still exhibit DGAT activity and are able to store TAG, albeit in lower quantities and at lower rates than the wild-type strain
malfunction
with or without cold acclimation, the dgat1 mutants exhibit higher sensitivity upon freezing exposure compared with the wild-type. Under cold conditions, the dgat1 mutants show reduced expression of C-REPEAT/DRE binding factor 2 and its regulons, which are essential for the acquisition of cold tolerance. Lipid profiling reveals that freezing significantly increases the levels of phosphatidic acid (PA) and diacylglycerol (DAG) while decreasing triacylglycerol (TAG) in the rosettes of dgat1 mutant plants. During freezing stress, the accumulation of PA in dgat1 mutant plants stimulates NADPH oxidase activity and enhances RbohD-dependent hydrogen peroxide production compared with the wild-type. Moreover, the cold-inducible transcripts of DGK2, DGK3, and DGK5, encoding diacylglycerol kinases, are significantly more upregulated in the dgat1 mutants than in the wild-type during cold stress. H2O2 and salicylic acid accumulate in the dgat1 mutants upon exposure to freezing temperatures. The dgat1 mutants show decreased expression of CBF2 and its target genes. Comparisons of lipid compositions and contents in wild-type and mutant leaves and seeds, phenotypes, detailed overview
malfunction
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the overexpression of YlDGA1 generates smaller but more numerous lipid bodies (LBs), a phenotype which can be enhanced by increasing the copy number of the overexpressed gene. DGAT overexpression affects LB segregation
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malfunction
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with or without cold acclimation, the dgat1 mutants exhibit higher sensitivity upon freezing exposure compared with the wild-type. Under cold conditions, the dgat1 mutants show reduced expression of C-REPEAT/DRE binding factor 2 and its regulons, which are essential for the acquisition of cold tolerance. Lipid profiling reveals that freezing significantly increases the levels of phosphatidic acid (PA) and diacylglycerol (DAG) while decreasing triacylglycerol (TAG) in the rosettes of dgat1 mutant plants. During freezing stress, the accumulation of PA in dgat1 mutant plants stimulates NADPH oxidase activity and enhances RbohD-dependent hydrogen peroxide production compared with the wild-type. Moreover, the cold-inducible transcripts of DGK2, DGK3, and DGK5, encoding diacylglycerol kinases, are significantly more upregulated in the dgat1 mutants than in the wild-type during cold stress. H2O2 and salicylic acid accumulate in the dgat1 mutants upon exposure to freezing temperatures. The dgat1 mutants show decreased expression of CBF2 and its target genes. Comparisons of lipid compositions and contents in wild-type and mutant leaves and seeds, phenotypes, detailed overview
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malfunction
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a Rv3371 deletion mutant of Mtb shows impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant shows reduced formation of TAG containing extracellular vesicles
-
malfunction
-
a Rv3371 deletion mutant of Mtb shows impaired non-replicating persistence in vitro and altered sensitivity to anti-mycobacterial drugs. In low iron medium, the Rv3371 deletion mutant shows reduced formation of TAG containing extracellular vesicles
-
malfunction
-
the overexpression of YlDGA1 generates smaller but more numerous lipid bodies (LBs), a phenotype which can be enhanced by increasing the copy number of the overexpressed gene. DGAT overexpression affects LB segregation
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metabolism
the enzyme is responsible for neutral lipid biosynthesis
metabolism
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the triacylglycerol pool generated by DGAT1 is preferentially used for supplying substrates for oxidation, whereas DGAt2-derived triacylglycerol is more favored for secretion
metabolism
acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis
metabolism
acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis. PtDGAT2B gene may contribute more to TAG synthesis in the early stage than during the later stages
metabolism
acyl-CoA:diacylglycerol acyltransferases (DGATs) catalyze the final and committed step in TAG biosynthesis. PtDGATX gene may contribute more to TAG synthesis in the later stage than during the earlier stages
metabolism
DGAT is considered as rate-limiting enzyme of TAG synthesis and accumulation in animals, plants and microbes
metabolism
DGAT-2 atalyzes the final step of triacylglycerol (TG) biosynthesis
metabolism
DGAT1 enzyme is evidenced to be a major determining factor for oil quantity and fatty acid composition of seed oils in several crops
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
-
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
-
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. Involvement of DGAT3 in TAG biosynthesis in microalgae and diatoms confirmed by heterologous expression in Saccharomyces cerevisiae TAG-deficient mutant strain H1246
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. The activation of DGAT1 in the maize is responsible for the increased embryo oil content in a high-oil maize line
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of sn-1, 2-DAG to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and committed step in the acyl-CoA-dependent biosynthesis of triacylglycerol (TAG), which appears to represent a bottleneck in oil accumulation in some oilseed species. Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of sn-1,2-DAG to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1, 2-DAG to yield TAG
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last and final committed step of the TAG biosynthesis pathway and this is the rate-limiting step for lipid accumulation in plants
metabolism
diacylglycerol acyltransferase (DGAT) catalyzes the last step of the acyl-CoA-dependent triacylglycerol (TAG) biosynthesis and appears to represent a bottleneck in algal TAG formation. In Haematococcus pluvialis, the fatty acid composition of total lipids and TAG is changed when the algae cells are subjected to light stress, in which 16:0, 18:1, and 18:2 increase with the concomitant decreases in 18:3
metabolism
diacylglycerol acyltransferase 1 (DGAT1) catalyzes the final and committed step in the Kennedy pathway for triacylglycerol (TAG) biosynthesis
metabolism
diacylglycerol acyltransferase and diacylglycerol kinase modulate triacylglycerol and phosphatidic acid production in the plant response to freezing stress
metabolism
in the oleaginous yeast Yarrowia lipolytica, the diacylglycerol acyltransferases (DGATs) are major factors for triacylglycerol (TAG) synthesis
metabolism
seed-specific CpuDGAT1 is associated with medium-chain fatty acid metabolism
metabolism
specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoA dependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
-
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
-
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
-
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
the enzyme catalyzes the last and committed step in the acyl-CoAdependent biosynthesis of triacylglycerol. Substantial contribution of DGAT1 to seed oil accumulation. Membrane-bound and soluble forms of the enzyme show very different amino-acid sequences and biochemical properties
metabolism
-
the final step in triacylglycerol (TAG) biosynthesis is catalyzed by diacylglycerol acyltransferase (DGAT)
metabolism
-
the isozyme of DGAT in Cyperus esculentus are involved in the triacylglycerol (TAG) biosynthesis
metabolism
the last step in triglyceride (TG) synthesis is catalyzed by diacylglycerol:acyltransferase (DGAT) which esterifies the diacylglycerol with a fatty acid
metabolism
-
the primary metabolic enzyme DGAT1 catalyzes the final step in assembly of triacylglycerol (TAG) by acyl transfer from acyl-CoA to diacylglycerol
metabolism
-
type 2 diacylglycerol acyltransferase (DGAT2) is one of the key enzymes involved in triacylglycerol (TAG) biosynthesis
metabolism
-
in the oleaginous yeast Yarrowia lipolytica, the diacylglycerol acyltransferases (DGATs) are major factors for triacylglycerol (TAG) synthesis
-
metabolism
-
diacylglycerol acyltransferase (DGAT) catalyzes the last step of the acyl-CoA-dependent triacylglycerol (TAG) biosynthesis and appears to represent a bottleneck in algal TAG formation. In Haematococcus pluvialis, the fatty acid composition of total lipids and TAG is changed when the algae cells are subjected to light stress, in which 16:0, 18:1, and 18:2 increase with the concomitant decreases in 18:3
-
metabolism
-
diacylglycerol acyltransferase and diacylglycerol kinase modulate triacylglycerol and phosphatidic acid production in the plant response to freezing stress
-
metabolism
-
diacylglycerol acyltransferase (DGAT) catalyzes the last and final committed step of the TAG biosynthesis pathway and this is the rate-limiting step for lipid accumulation in plants
-
metabolism
-
in the oleaginous yeast Yarrowia lipolytica, the diacylglycerol acyltransferases (DGATs) are major factors for triacylglycerol (TAG) synthesis
-
metabolism
-
DGAT is considered as rate-limiting enzyme of TAG synthesis and accumulation in animals, plants and microbes
-
physiological function
enzyme makes a major contribution to triacylglycerol synthesis via an acyl-CoA-dependent mechanism and is not involved in steryl ester synthesis
physiological function
in isoforms dgat1, dgat2, dgat1/dgat2 double mutant and dgat1/dgat2/phospholipid:diacylglycerol acyltransferase triple mutant the total lipid% dry cell weight as a percentage of the wild-type strain is 57%, 36%, 18% and 13%, respectively
physiological function
inhibition of isoform DGAT1 affects equally the incorporation of glycerol and exogenous preformed oleate into cellular and secreted triacylglycerol. Data indicate that isoform DGAT2 acts upstream of isoform DGAT1, and DGAT1 functions in the re-esterification of partial glycerides generated by intracellular lipolysis, using preformed fatty acids
physiological function
isoform DGAT2 activity accounts for a modest fraction of less than 20% of overall cellular DGAT activity. Inhibition of DGAT2 activity specifically inhibits and is rate-limiting for the incorporation of de novo synthesized fatty acids and of glycerol into cellular and secreted triglyceride to a much greater extent than it affects the incorporation of exogenously added oleate. Isoform DGAT2 acts upstream of isoform DGAT1, largely determines the rate of de novo synthesis of triglyceride, and uses nascent diacylglycerol and de novo synthesized fatty acids as substrates
physiological function
overexpression of the enzyme gene in Saccharomyces cerevisiae leads to accumulation of full-length prtein in wild-type and accumulation of full-length protein and a N-terminally truncated protein in a snf2 disruption mutant, lacking a DNA-dependent ATPase that forms the SWI/SNF chromatin remodeling complex. Proteolytic cleavage at the N-terminal region is involved in enzyme activation in the snf2 disruptant, a major cleavage site lies between residues Lys29 and Ser30
physiological function
upon overexpression in Mycobacterium smegmatis mc2155, cell morphology is changed and the cells become grossly enlarged. A massive formation of lipid bodies and a change in lipid pattern is observed simultaneously
physiological function
-
the enzyme interacts with lipid droplets presumably to catalyze localized triacylglycerol synthesis for lipid droplet expansion
physiological function
analysis of functional and cellular nature of type 1 and type 2 DGATs from Lobosphaera incisa, with LiDGAT1 being a major contributor to the TAG pool. LiDGATs of type 2 might be in turn involved in the incorporation of unusual fatty acids into TAG and thus regulate the composition of TAG
physiological function
DGAT1 appears to play a role in freezing and/or drought stress responses in Arabidopsis thaliana. DGAT1 is suggested to be involved in maintaining a balance of DAG and acyl-CoA for the biosynthesis of membrane lipids and recycling of fatty acids to TAG under conditions where catabolic reactions are halted. Regulation of the enzyme, overview
physiological function
DGAT1 appears to play a role in freezing and/or drought stress responses in Brassica napus. Regulation of the enzyme, overview
physiological function
-
DGAT1 confers freezing tolerance in plants by supporting SFR2 (sensitive-to-freezing2)-mediated remodeling of chloroplast membranes, recombinant overexpression of AtDGAT1 leads to increased freezing tolerance in seedlings
physiological function
DGAT2 catalyzes the formation of triacylglycerol (TG) using fatty acyl coenzyme A (CoA) and 1,2-diacylglycerol (DG) as substrates. TG is the major form of stored metabolic energy in eukaryotic organisms that is sequestered in the hydrophobic core of cytosolic lipid droplets until it is needed. DGAT-2 catalyzes TG synthesis for lipid droplet growth
physiological function
diacylglycerol acyltransferase (DGAT) is an acyl-CoA-dependent enzyme which converts diacylglycerol (DAG) to triacylglycerol (TAG)
physiological function
-
diacylglycerol acyltransferase 1 (DGAT1) is a key enzyme in the production of triacylglycerols
physiological function
diacylglycerol acyltransferase 1 (DGAT1) is an integral membrane enzyme catalyzing the final and committed step in the acylcoenzyme A (CoA)-dependent biosynthesis of triacylglycerol (TAG). Proposed model for BnaDGAT1 regulation involving the hydrophilic N-terminal domain (NTD), overview
physiological function
-
enzyme AtfG25 has an important, but not exclusive, role in triacylglycerol (TAG) biosynthesis in the Streptomyces sp. G25 isolate, suggesting the presence of alternative metabolic pathways for lipid accumulation
physiological function
intrinsic disorder in plant proteins has been reported to be essential for the stress response. An intrinsically disordered region (IDR) spanning the N-terminal cytosolic domain of the intramembrane enzyme diacylglycerol acyltransferase1 (DGAT1) from canola-type Brassica napus, has been identified. The IDR spans amino acid residues 1-80, while residues 81-113 have a folded structure. DGAT1 (EC 2.3.1.20) catalyzes the acyl-coenzyme A (CoA)-dependent acylation of sn-1, 2-diacylglycerol (DAG) to produce triacylglycerol (TAG) and CoA. TAG serves as an energy source for germination in plants, a component of edible oil. This enzyme has a substantial effect on carbon flux into seed oil
physiological function
isozyme GmDGAT1A may play a role in usual seed triacylglycerol (TAG) production. Isozymes GmDGAT1A and 2D are differentially regulated by jasmonate during insect and wounding responses and abscisic acid for cold and heat stress response, indicating their different functions in soybean stress responses
physiological function
isozyme GmDGAT2D plays a role in usual seed triacylglycerol (TAG) production and is also involved in other tissues in responses to environmental and hormonal cues. Isozymes GmDGAT1A and 2D are differentially regulated by jasmonate during insect and wounding responses and abscisic acid for cold and heat stress response, indicating their different functions in soybean stress responses. Ectopic expression of GmDGATs in soybean hairy roots promotes TAG accumulation
physiological function
isozymes CrDGTT1, CrDGTT2 and CrDGTT3 possess distinct specificities toward acyl CoAs and diacylglycerols, and may work in concert spatially and temporally to synthesize diverse triacylglycerol (TAG) species in Chlamydomonas reinhardtii
physiological function
isozymes CrDGTT1, CrDGTT2 and CrDGTT3 possess distinct specificities toward acyl CoAs and diacylglycerols, and may work in concert spatially and temporally to synthesize diverse triacylglycerol (TAG) species in Chlamydomonas reinhardtii. rDGTT1 is shown to prefer prokaryotic lipid substrates and probably resides in both the endoplasmic reticulum and chloroplast envelope, indicating its role in prokaryotic and eukaryotic TAG biosynthesis. Role of isozyme CrDGTT1 in TAG biosynthesis, overview
physiological function
regardless of N availability, PtWS/DGAT exhibits a DGAT activity with a preference on saturated fatty acids. PtWS/DGAT exhibits activities of both a wax ester synthase (WS, EC 2.3.1.75) and a diacylglycerol acyltransferase (DGAT, EC 2.3.1.20)
physiological function
-
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview
physiological function
-
regulation of the enzyme, overview
physiological function
regulation of the enzyme, overview. Arabidopsis thaliana DGAT3 appears to be involved in recycling of linoleic acid (18:2DELTA9cis,12cis) and alpha-linolenic acid (18:3DELTA9cis, 12cis,15cis) into for triacylglycerol (TAG) when TAG breakdown is blocked
physiological function
role of diacylglycerol acyltransferase (DGAT) 1 and 2 in cardiac metabolism and function
physiological function
role of diacylglycerol acyltransferase (DGAT) 1 and 2 in cardiac metabolism and function. The two DGAT isoforms in the heart have partially redundant function
physiological function
role of the DGAT3 and WS/DGAT genes in lipid accumulation during seed development, overview
physiological function
role of the DGAT3 and WS/DGAT genes in lipid accumulation during seed development, overview
physiological function
the conversion of diacylglycerol (DAG) to triacylglycerol (TAG) by DGAT1 is critical for plant freezing tolerance, acting by balancing TAG and phosphatidic acid (PA) production in Arabidopsis thaliana
physiological function
the diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations during persistence. It is involved in the biosynthesis of triacylglycerol (TAG). TAG is important to mycobacteria both as cell envelope component and energy reservoir
physiological function
the expression of isozyme RtDGATa shows non-involvement in triacylglycerol (TAG) accumulation according to its mRNA expression level in Rhodosporidium toruloides
physiological function
the expression pattern of isozyme RtDGATb is related to the process of fatty acid biosynthesis, suggesting that RtDGATb plays an important role in lipid accumulation in Rhodosporidium toruloides
physiological function
the MaDGAT2 gene encodes diacylglycerol acyltransferase 2, which is involved in the biosynthesis of neutral lipids and formation of lipid particle
physiological function
the specialized diacylglycerol acyltransferase DGAT1 contributes to the extreme medium-chain fatty acid content of Cuphea seed oil
physiological function
the type 2 diacylglycerol acyltransferase accelerates the triacylglycerol biosynthesis in heterokont oleaginous microalga Nannochloropsis oceanica
physiological function
two bifunctional enzymes, TrWSD4 and TrWSD5, from the marine protist Thraustochytrium roseum show wax ester synthase/acyl-CoA:diacylglycerol acyltransferase activity catalyzing wax ester and triacylglycerol synthesis. The WS/DGAT shows both in vitro wax synthase (WS) and DGAT activity, it is characterized as unspecific acyltransferase accepting a broad range of acyl-CoAs and fatty alcohols as substrates for WS activity but displaying substrate preference for medium-chain acyl-CoAs. In vivo characterization shows that the WS/DGAT predominantly functions as wax synthase
physiological function
type I diacylglycerol acyltransferase (MtDGAT1) is involved in triacylglycerol (TAG) biosynthesis and may contribute to biochemical mechanisms determining the particular fatty acid composition of Macadamia oil. Major contribution of DGAT enzymes to TAG biosynthesis in seed plants
physiological function
-
the MaDGAT2 gene encodes diacylglycerol acyltransferase 2, which is involved in the biosynthesis of neutral lipids and formation of lipid particle
-
physiological function
-
the expression of isozyme RtDGATa shows non-involvement in triacylglycerol (TAG) accumulation according to its mRNA expression level in Rhodosporidium toruloides
-
physiological function
-
the expression pattern of isozyme RtDGATb is related to the process of fatty acid biosynthesis, suggesting that RtDGATb plays an important role in lipid accumulation in Rhodosporidium toruloides
-
physiological function
-
the type 2 diacylglycerol acyltransferase accelerates the triacylglycerol biosynthesis in heterokont oleaginous microalga Nannochloropsis oceanica
-
physiological function
-
in isoforms dgat1, dgat2, dgat1/dgat2 double mutant and dgat1/dgat2/phospholipid:diacylglycerol acyltransferase triple mutant the total lipid% dry cell weight as a percentage of the wild-type strain is 57%, 36%, 18% and 13%, respectively
-
physiological function
-
the conversion of diacylglycerol (DAG) to triacylglycerol (TAG) by DGAT1 is critical for plant freezing tolerance, acting by balancing TAG and phosphatidic acid (PA) production in Arabidopsis thaliana
-
physiological function
-
the diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations during persistence. It is involved in the biosynthesis of triacylglycerol (TAG). TAG is important to mycobacteria both as cell envelope component and energy reservoir
-
physiological function
-
upon overexpression in Mycobacterium smegmatis mc2155, cell morphology is changed and the cells become grossly enlarged. A massive formation of lipid bodies and a change in lipid pattern is observed simultaneously
-
physiological function
-
the diacylglycerol acyltransferase Rv3371 of Mycobacterium tuberculosis is required for growth arrest and involved in stress-induced cell wall alterations during persistence. It is involved in the biosynthesis of triacylglycerol (TAG). TAG is important to mycobacteria both as cell envelope component and energy reservoir
-
physiological function
-
analysis of functional and cellular nature of type 1 and type 2 DGATs from Lobosphaera incisa, with LiDGAT1 being a major contributor to the TAG pool. LiDGATs of type 2 might be in turn involved in the incorporation of unusual fatty acids into TAG and thus regulate the composition of TAG
-
physiological function
-
two bifunctional enzymes, TrWSD4 and TrWSD5, from the marine protist Thraustochytrium roseum show wax ester synthase/acyl-CoA:diacylglycerol acyltransferase activity catalyzing wax ester and triacylglycerol synthesis. The WS/DGAT shows both in vitro wax synthase (WS) and DGAT activity, it is characterized as unspecific acyltransferase accepting a broad range of acyl-CoAs and fatty alcohols as substrates for WS activity but displaying substrate preference for medium-chain acyl-CoAs. In vivo characterization shows that the WS/DGAT predominantly functions as wax synthase
-
additional information
-
comparison and analysis of functional motifs and evolutionary relationships of DGAT2s, protein-protein interaction analysis among CzDGAT2s, overview. N- and C-terminals are important for the enzyme activity of isozyme CzDGAT2C. Membrane yeast two-hybrid assay reveals a possible DGAT2 activity modulation via the formation of homodimer/heterodimer among different DGAT2 isoforms
additional information
comparison and analysis of functional motifs and evolutionary relationships of DGAT2s, protein-protein interaction analysis among CzDGAT2s, overview. N- and C-terminals are important for the enzyme activity of isozyme CzDGAT2C. Membrane yeast two-hybrid assay reveals a possible DGAT2 activity modulation via the formation of homodimer/heterodimer among different DGAT2 isoforms
additional information
comparison and analysis of functional motifs and evolutionary relationships of DGAT2s, protein-protein interaction analysis among CzDGAT2s, overview. N- and C-terminals are important for the enzyme activity of isozyme CzDGAT2C. Membrane yeast two-hybrid assay reveals a possible DGAT2 activity modulation via the formation of homodimer/heterodimer among different DGAT2 isoforms
additional information
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
-
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
-
comparison of Glycine max and Corylus americana DGAT1 sequences
additional information
determination of conformational heterogeneity in the N-terminal domain of DGAT1, disorder propensity for the full-length BnaDGAT11-501 sequence, overview. A small gain of secondary structure is induced by ligand binding. The cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites
additional information
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determination of conformational heterogeneity in the N-terminal domain of DGAT1, disorder propensity for the full-length BnaDGAT11-501 sequence, overview. A small gain of secondary structure is induced by ligand binding. The cytoplasmic N-terminal domain of Brassica napus diacylglycerol acyltransferase, (DGAT1) includes an inhibitory module and allosteric binding sites
additional information
DGAT1 enzymes may be regulated through allosteric interactions. The self-association properties of DGAT1 enzymes are consistent with the fact that most allosteric enzymes exhibit quaternary structure, identification of CoA/acyl-CoA binding site in the hydrophilic N-terminal domain and specific interactions involved in CoA recognition, and analysis of structure and function of the hydrophilic N-terminal domain of Brassica napus DGAT1, overview. This domain is found to have an intrinsically disordered region (IDR) and a folded section. IDRs are recognized as important regions in proteins due to their roles in cellular signaling and regulation. The highly disordered segment is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif. Isozyme BnaC.DGAT1.a also exhibits positive cooperativity. The involvement of the N-terminal domain in self-association may mediate positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. The BnaDGAT1 N-terminal domain is not necessary for catalysis but contributes to modulating activity. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site. The BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction. The BnaDGAT1 N-terminal Domain is structurally flexible. The allosteric site also is needed for acyl-CoA-mediated homotropic allosteric activation
additional information
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DGAT1 enzymes may be regulated through allosteric interactions. The self-association properties of DGAT1 enzymes are consistent with the fact that most allosteric enzymes exhibit quaternary structure, identification of CoA/acyl-CoA binding site in the hydrophilic N-terminal domain and specific interactions involved in CoA recognition, and analysis of structure and function of the hydrophilic N-terminal domain of Brassica napus DGAT1, overview. This domain is found to have an intrinsically disordered region (IDR) and a folded section. IDRs are recognized as important regions in proteins due to their roles in cellular signaling and regulation. The highly disordered segment is involved in the downregulation of DGAT1 activity, suggesting the presence of an autoinhibitory motif. Isozyme BnaC.DGAT1.a also exhibits positive cooperativity. The involvement of the N-terminal domain in self-association may mediate positive cooperativity. The folded section of the enzyme is important to maintain high acyl-CoA affinity at the active site and activity. The BnaDGAT1 N-terminal domain is not necessary for catalysis but contributes to modulating activity. Residues 81 to 113 are important in maintaining high activity and affinity for the acyl donor at the active site. The BnaDGAT1 N-terminal region is required for interactions leading to the dimeric enzyme form, which may allow it to partially mediate positive cooperativity through intermolecular interaction. The BnaDGAT1 N-terminal Domain is structurally flexible. The allosteric site also is needed for acyl-CoA-mediated homotropic allosteric activation
additional information
DGAT2 is part of a high molecular weight (about 650 kD) complex. Calnexin, an endoplasmic reticulum chaperone, interacts with DGAT2. The interaction between calnexin and DGAT2 suggests that calnexin may play a role in lipid metabolism, including adipocyte differentiation. The subcellular localization and stability of DGAT2 are not altered by the absence of calnexin
additional information
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DGAT2 is part of a high molecular weight (about 650 kD) complex. Calnexin, an endoplasmic reticulum chaperone, interacts with DGAT2. The interaction between calnexin and DGAT2 suggests that calnexin may play a role in lipid metabolism, including adipocyte differentiation. The subcellular localization and stability of DGAT2 are not altered by the absence of calnexin
additional information
fatty acid composition of high-oil lines and cultivar Jack wild-type soybean seed oil, overview
additional information
fatty acid composition of high-oil lines and cultivar Jack wild-type soybean seed oil, overview
additional information
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fatty acid composition of high-oil lines and cultivar Jack wild-type soybean seed oil, overview
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
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in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
additional information
purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-beta-D-maltopyranoside micelles is lipidated to form mixed micelles. The degree of mixed micelle fluidity appears to influence acyltransferase activity. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition indicating that PA facilitates the transition of the enzyme into the more active state. PA is a key effector modulating lipid homeostasis, in addition to its well recognized role in lipid signaling
additional information
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purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-beta-D-maltopyranoside micelles is lipidated to form mixed micelles. The degree of mixed micelle fluidity appears to influence acyltransferase activity. BnaDGAT1 exhibits a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. In the presence of phosphatidic acid (PA), the oleoyl-CoA saturation plot becomes more hyperbolic and desensitized to substrate inhibition indicating that PA facilitates the transition of the enzyme into the more active state. PA is a key effector modulating lipid homeostasis, in addition to its well recognized role in lipid signaling
additional information
quantification of triacylglycerol and analysis of fatty acid composition
additional information
quantification of triacylglycerol and analysis of fatty acid composition
additional information
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quantification of triacylglycerol and analysis of fatty acid composition
additional information
relevant is the presence of the acyl-CoA binding signature R122-G141 close to residues R156-N161 that have been involved in the active site and a DAG/phorbol ester binding motif. Two amino acid changes, G155 and T152, are found in MtDGAT1 within the putative acyl-CoA binding domain, replacing the highly conserved Ala and Ser residues that might affect acyl specificity of the enzyme. A previously reported leucine zipper motif is also found
additional information
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relevant is the presence of the acyl-CoA binding signature R122-G141 close to residues R156-N161 that have been involved in the active site and a DAG/phorbol ester binding motif. Two amino acid changes, G155 and T152, are found in MtDGAT1 within the putative acyl-CoA binding domain, replacing the highly conserved Ala and Ser residues that might affect acyl specificity of the enzyme. A previously reported leucine zipper motif is also found
additional information
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
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sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
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sequence alignment of DGAT1 reveals that the PTMD9 is conserved in many plant species
additional information
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the expression of DGAT1 is found to be highly cold responsive and correlated with the cold tolerance in Boechera stricta lines
additional information
the N-terminal region plays a role in self-oligomerization. The hydrophilic N-terminal region of DGAT1 constitutes the enzyme's regulatory domain, which is not necessary for catalysis. This domain is comprised of two distinct segments, specifically an intrinsically disordered region (IDR) and a folded segment. The IDR can form interactions that are important for dimerization and may allow it to partially mediate positive cooperativity. Truncation of this IDR results in a more active enzyme form, suggesting the IDR encompasses an autoinhibitory motif. N-terminal structure-function analysis of Brassica napus DGAT1, overview
additional information
the N-terminal region plays a role in self-oligomerization. The hydrophilic N-terminal region of DGAT1 constitutes the enzyme's regulatory domain, which is not necessary for catalysis. This domain is comprised of two distinct segments, specifically an intrinsically disordered region (IDR) and a folded segment. The IDR can form interactions that are important for dimerization and may allow it to partially mediate positive cooperativity. Truncation of this IDR results in a more active enzyme form, suggesting the IDR encompasses an autoinhibitory motif. N-terminal structure-function analysis of Brassica napus DGAT1, overview
additional information
the N-terminal region plays a role in self-oligomerization. The hydrophilic N-terminal region of DGAT1 constitutes the enzyme's regulatory domain, which is not necessary for catalysis. This domain is comprised of two distinct segments, specifically an intrinsically disordered region (IDR) and a folded segment. The IDR can form interactions that are important for dimerization and may allow it to partially mediate positive cooperativity. Truncation of this IDR results in a more active enzyme form, suggesting the IDR encompasses an autoinhibitory motif. N-terminal structure-function analysis of Brassica napus DGAT1, overview
additional information
the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
additional information
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the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
additional information
three-dimensional model of the tDGAT protein, structure homology modeling
additional information
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three-dimensional model of the tDGAT protein, structure homology modeling
additional information
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the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
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additional information
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the putative N-terminal transmembrane domain of Dga1p appears important, but not necessary for enzyme activity
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additional information
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in silico analyses of Lobosphaera incisa transcriptome data reveal 3 isoforms of DGAT type 2
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additional information
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three-dimensional model of the tDGAT protein, structure homology modeling
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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
H132L/H133L
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highly conserved residues in acyltransferases
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
F449C
site-directed mutagenesis
I447F
site-directed mutagenesis
K289N
site-directed mutagenesis
L441P
site-directed mutagenesis
V125F
site-directed mutagenesis
I144F
site-directed mutagenesis
I466F
site-directed mutagenesis
L460P
site-directed mutagenesis
L460P/I466F
site-directed mutagenesis
P178I
-
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
W120A
Marinobacter nauticus
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inactive
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
F71A
mutant retains more than 40% of wild-type activity
H193A
almost complete loss of activity
H193E/G196S
mutation to corresponding motif found in plant, abolishes enzymic activity
H195A
complete loss of activity
L73A
mutant retains more than 40% of wild-type activity
Y129A/F130A/P131A
almost complete loss of activity
S126A
no detectable activity
S126A
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no detectable activity
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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
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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
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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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DGAT2 overexpression also increases wax monoester synthase activity in intact cells
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DGAT2 overexpression also increases wax monoester synthase activity in intact cells
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short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
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short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
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short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
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short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
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short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
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short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
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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
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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
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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
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
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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
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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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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 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
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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%)
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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
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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
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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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