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Information on EC 2.3.1.20 - diacylglycerol O-acyltransferase and Organism(s) Mus musculus and UniProt Accession Q9Z2A7
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2.3.1.20 diacylglycerol O-acyltransferaseIUBMB Comments
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
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Word Map
- 2.3.1.20
- triacylglycerols
- triglyceride
- adipose
- milk
- acyl-coas
- lipoprotein
- obesity
- cholesterol
- droplet
- cattle
- adipocytes
- lipase
- steatosis
-
lipogenesis
-
lipogenic
-
high-fat
-
holstein
-
oleic
-
dairy
-
proliferator-activated
- phosphatidate
- glycerolipids
-
lipolysis
-
oleaginous
- glycerol-3-phosphate
- chylomicron
-
biodiesel
-
srebf1
-
oilseed
-
lipotoxicity
- stearoyl-coa
- acaca
- camelina
- industry
-
insig1
- biofuel production
-
oleosins
-
cholinephosphotransferase
- elovl6
- drug development
-
triacylglyceride
-
holstein-friesian
- sn-1,2-diacylglycerols
- analysis
- glycerolphosphate
- oleoyl-coa
- protein-1c
-
lipin
- lpaat
-
ricinoleic
- medicine
- baylyi
- chylomicronemia
- biotechnology
-
steryl
-
kennedy
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
dgat1, dgat2, dgat, diacylglycerol acyltransferase, diacylglycerol acyltransferase 1, diacylglycerol o-acyltransferase, dgat-1, monoacylglycerol acyltransferase, acyl-coa:diacylglycerol acyltransferase, diacylglycerol acyltransferase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,2-diacylglycerol acyltransferase
-
-
-
-
acyl CoA:diacylglycerol acyltransferase-2
acyl-CoA:1,2-dioleoyl-sn-glycerol acyltransferase
-
-
-
-
acyltransferase, diacylglycerol
-
-
-
-
DGAT
DGAT1
DGAT1A
-
-
-
-
DGAT2
DGAT2A
-
-
-
-
diacylglycerol acyltransferase
-
-
-
-
diacylglycerol acyltransferase-2
diglyceride acyltransferase
-
-
-
-
diglyceride O-acyltransferase
-
-
-
-
palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase
-
-
-
-
DGAT
-
-
-
-
DGAT1
-
-
-
-
DGAT2
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol
the conserved sequence 161HPHG164 is important for activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:1,2-diacyl-sn-glycerol O-acyltransferase
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
CAS REGISTRY NUMBER
COMMENTARY
9029-98-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
-
-
-
?
acyl-CoA + 1,2-diacylglycerol
CoA + triacylglycerol
acceptors: overview
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
?
1,2-dioleoylglycerol + palmitoyl-CoA
1,2-dioleoyl-3-palmitoylglycerol + CoA
-
-
-
?
1-palmitoyl-2-oleoyl glycerol + acyl-CoA
1-palmitoyl-2-oleoyl-3-acylglycerol + CoA
-
-
-
?
arachidonoyl-CoA + 1,2-diacylglycerol
CoA + 3-arachidonoyl-1,2-diacylglycerol
-
-
-
?
linoleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-linoleoylglycerol
-
-
-
?
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
-
-
-
-
?
oleoyl-CoA + 1,2-diacylglycerol
CoA + 1,2-diacyl-3-oleoylglycerol
-
-
-
?
palmitoyl-CoA + 1,2-oleoyl-sn-glycerol
CoA + 1,2-dioleoyl-3-palmitoyl-sn-glycerol
usage of fluorescent NBD-tagged palmitoyl-CoA as substrate
-
-
?
1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
acyl-CoA specificity, overview
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + 1,2,3-triacylglycerol
-
-
-
?
acyl-CoA + 1,2-diacyl-sn-glycerol
CoA + triacylglycerol
-
isoforms DGAT1 and DGAT2 Can compensate for each other to synthesize triacylglycerol
-
-
?
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
-
-
?
sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
the final step in triacylglycerol synthesis is catalyzed by the acyl-CoA:diacylglycerol acyltransferase enzymes, DGAT1 and DGAT2
-
-
?
sn-1,2-diacylglycerol + acyl-CoA
triacylglycerol + CoA
-
the enzyme contains a neutral lipid binding sequence 80FLVLGVAC87 residing in the first transmembrane domain
-
-
?
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 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
?
-
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
?
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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
-
-
?
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
-
-
?
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
-
isoforms DGAT1 and DGAT2 Can compensate for each other to synthesize triacylglycerol
-
-
?
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
?
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cis-2-(4-(4-(4-(3-(3-chlorophenyl)ureido)phenyl)thieno[3,2-d]pyrimidin-7-yl)cyclohexyl)acetate
-
[(1r,4r)-4-[4-(5-[[6-(trifluoromethyl)pyridin-3-yl]amino]pyridin-2-yl)phenyl]cyclohexyl]acetic acid
-
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
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
no inhibition by selective DGAT1 inhibitor PF-04620110
-
additional information
-
no inhibition by selective DGAT1 inhibitor PF-04620110
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calnexin
calnexin is a diacylglycerol acyltransferase-2 interacting protein
-
additional information
-
effectivity of detergents used in in vitro assays, overview
-
additional information
effectivity of detergents used in in vitro assays, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT1 overexpressing mice
additional information
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT1 overexpressing mice
additional information
-
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT1 overexpressing mice
additional information
recombinant enzyme in Sf9 cell membrane and in COS-7 cell membranes, multifunctional enzyme
additional information
recombinant enzyme in Sf9 cell membrane and in COS-7 cell membranes, multifunctional enzyme
additional information
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT2 overexpressing mice
additional information
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT2 overexpressing mice
additional information
-
plasma and liver lipid levels of wild-type mice compared to recombinant DGAT2 overexpressing mice
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
greater abundance of isozyme DGAT2 mRNA in the heart compared to isozyme DGAT1
additional information
greater abundance of isozyme DGAT2 mRNA in the heart compared to isozyme DGAT1
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
the endoplasmic reticulum targeting signal is present in the first transmembrane domain, TMD1, of isoform DGAT2
DGAT-2 is an integral membrane, it has two transmembrane domains separated by a short loop (about 5-8 amino acids) that extends into the endoplasmic reticulum (ER) lumen. The first transmembrane domain contains an ER targeting signal while the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol
the interaction of isoform DGAT2 with lipid droplets is dependent on the C-terminus. Mutants, in which regions of the C-terminus are either truncated or specific regions are deleted, failed to co-localize with lipid droplets when cells are oleate loaded to stimulate triacylglycerol synthesis
-
DGAT2 is an integral membrane protein with both the N and C terminus oriented toward the cytosol, the loop between the two transmembrane domains of DGAT2is not exposed to the cytosol
additional information
the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol. Although present in the ER, DGAT2 also co-localizes with lipid droplets
-
additional information
-
the bulk of DGAT2 C-terminal to its second transmembrane is exposed to the cytosol. Although present in the ER, DGAT2 also co-localizes with lipid droplets
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
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
malfunction
metabolism
physiological function
additional information
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 last step in triglyceride (TG) synthesis is catalyzed by diacylglycerol:acyltransferase (DGAT) which esterifies the diacylglycerol with a fatty acid
malfunction
-
enzyme-deficient mice show no effect on retinal anatomy or the ultrastructure of photoreceptor outer-segments. Enzyme loss affects retinyl-ester synthesis and total acyl-coenzyme A:retinol acyl-transferase activityin the eye
malfunction
-
Isoform DGAT1 inactivation promotes large lipid droplet formation. Inhibition of isoform DGAT2 augments fatty acid oxidation, whereas inhibition of DGAT1 increases triacylglycerol secretion. Triacylglycerol secretion is significantly reduced on DGAT2 inhibition without altering extracellular apolipoprotein B levels
malfunction
calnexin-deficient mouse embryonic fibroblasts have reduced intracellular triacylglycerol levels and fewer large lipid droplets
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
metabolism
-
the triacylglycerol pool generated by DGAT1 is preferentially used for supplying substrates for oxidation, whereas DGAt2-derived triacylglycerol is more favored for secretion
metabolism
DGAT-2 atalyzes the final step of triacylglycerol (TG) biosynthesis
metabolism
the last step in triglyceride (TG) synthesis is catalyzed by diacylglycerol:acyltransferase (DGAT) which esterifies the diacylglycerol with a fatty acid
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
role of diacylglycerol acyltransferase (DGAT) 1 and 2 in cardiac metabolism and function
additional information
DGAT2 is part of a high molecular weight (about 650 kD) complex. Calnexin, an endoplasmic reticulum chaperone, interacts with DGAT2. The interaction between calnexin and DGAT2 suggests that calnexin may play a role in lipid metabolism, including adipocyte differentiation. The subcellular localization and stability of DGAT2 are not altered by the absence of calnexin
additional information
-
DGAT2 is part of a high molecular weight (about 650 kD) complex. Calnexin, an endoplasmic reticulum chaperone, interacts with DGAT2. The interaction between calnexin and DGAT2 suggests that calnexin may play a role in lipid metabolism, including adipocyte differentiation. The subcellular localization and stability of DGAT2 are not altered by the absence of calnexin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DGAT1_MOUSE
498
8
56790
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47000
45000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
individual isoform DGAT2 subunits are capable of interacting as part of a multimeric complex. Multiple domains, both in the N and C termini, mediate subunit interaction
additional information
-
individual isoform DGAT2 subunits are capable of interacting as part of a multimeric complex. Multiple domains, both in the N and C termini, mediate subunit interaction
additional information
DGAT2 is part of a high molecular weight (about 650 kD) complex
additional information
-
DGAT2 is part of a high molecular weight (about 650 kD) complex
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
DGAT2 is degraded via the proteasome in a ubiquitin-dependent manner
additional information
-
DGAT2 is degraded via the proteasome in a ubiquitin-dependent manner
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C87S
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
H161A
-
site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
H161A/P162G/H163A
-
site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
H163A
-
site-directed mutagenesis, the mutant shows over 80% reduced activity compared to the wild-type enzyme
P162G
-
site-directed mutagenesis, the mutant shows about 40% reduced activity compared to the wild-type enzyme
additional information
additional information
short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
-
short-term overexpression of DGAT1 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
the wax diester synthase activity of DGAT1 helps to explain the deficiency of type II wax diesters in the fur lipids of Dgat-/- mice, DGAT1 deficiency also perturbs retinol metabolism in the livers of Dgat-/- mice, hepatic levels of unesterified retinol are increased in Dgat-/- mice challenged with high-retinol diets
additional information
the wax diester synthase activity of DGAT1 helps to explain the deficiency of type II wax diesters in the fur lipids of Dgat-/- mice, DGAT1 deficiency also perturbs retinol metabolism in the livers of Dgat-/- mice, hepatic levels of unesterified retinol are increased in Dgat-/- mice challenged with high-retinol diets
additional information
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
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
-
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
DGAT2 overexpression also increases wax monoester synthase activity in intact cells
additional information
DGAT2 overexpression also increases wax monoester synthase activity in intact cells
additional information
short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
-
short-term overexpression of DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production, overview
additional information
an isoform DGAT2 mutant lacking both its transmembrane domains still associates with membranes, but is absent from the endoplasmic reticulum and instead localizes to mitochondria. The mutant is still active and capable of interacting with lipid droplets to promote triacylglycerol storage. Mutants, in which regions of the C-terminus are either truncated or specific regions are deleted, fail to co-localize with lipid droplets when cells are loaded with oleate to stimulate triacylglycerol synthesis
additional information
-
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
construction of chimeric enzyme BioId/DGAT2, DGAT2 is fused in-frame to the C-terminus of a promiscuous biotin ligase, BirA. Like DGAT2, BioId/DGAT2 stimulates the formation of large lipid droplets. Fusing DGAT2 to the C-terminus does not appear to change its localization or function in cells. When biotin is added to the culture medium, with or without oleate, there is a strong biotinylation signal that co-localizes with BioId/DGAT2 both in the endoplasmic reticulum and around lipid droplets. Protein interaction analysis of biotinylated BioId/DGAT2 in recombinant HEK-293T cells, overview
additional information
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant biotinylated FLAG- or myc-tagged DGAT-2 fused to biotin ligase from HEK-293T cells, biotinylated proteins are captured with magnetic streptavidin beads
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DGAT1, functional expression of the FLAG-tagged enzyme in membranes of Spodoptera frugiperda Sf9 cells and in COS-7 cells, expression analysis
DNA and amino acid sequence determination and analysis, phylogenetic tree, expression in insect cells
short-term hepatic overexpression of DGAT1 in mice using adenoviral vectors results in 2.0fold increases in the triglyceride content of liver, the increase in hepatic triglyceride content has no effect on the production rate of VLDL triglyceride or apoB
DGAT2, functional expression of the FLAG-tagged enzyme in Spodoptera frugiperda Sf9 cells, expression analysis
gene DGAT2, expression of FLAG-tagged wild-type and mutant enzyme in COS-7 cells
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recombinant expression of FLAG- or myc-tagged DGAT-2 fused to biotin ligase in HEK-293T cells and in COS-7 cells
short-term hepatic overexpression of DGAT2 in mice using adenoviral vectors results in 2.4fold increases in the triglyceride content of liver, the increase in hepatic triglyceride content has no effect on the production rate of VLDL triglyceride or apoB
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cases, S.; Smith, S.J.; Zheng, Y.W.; Myers, H.M.; Lear, S.R.; Sande, E.; Novak, S.; Collins, C.; Welch, C.B.; Lusis, A.J.; Erickson, S.K.; Farese, R.V., Jr.
Identification of a gene encoding an acyl CoA:diacylglycerol acyltransferase, a key enzyme in triacylglycerol synthesis
Proc. Natl. Acad. Sci. USA
95
13018-13023
1998
Homo sapiens, Mus musculus (Q9Z2A7), Mus musculus
Cases, S.; Stone, S.J.; Zhou, P.; Yen, E.; Tow, B.; Lardizabal, K.D.; Voelker, T.; Farese, R.V., Jr.
Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members
J. Biol. Chem.
276
38870-38876
2001
Homo sapiens (Q96PD7), Homo sapiens, Mus musculus (Q9DCV3), Mus musculus
Meegalla, R.L.; Billheimer, J.T.; Cheng, D.
Concerted elevation of acyl-coenzyme A:diacylglycerol acyltransferase (DGAT) activity through independent stimulation of mRNA expression of DGAT1 and DGAT2 by carbohydrate and insulin
Biochem. Biophys. Res. Commun.
298
317-323
2002
Mus musculus
Wakimoto, K.; Chiba, H.; Michibata, H.; Seishima, M.; Kawasaki, S.; Okubo, K.; Mitsui, H.; Torii, H.; Imai, Y.
A novel diacylglycerol acyltransferase (DGAT2) is decreased in human psoriatic skin and increased in diabetic mice
Biochem. Biophys. Res. Commun.
310
296-302
2003
Homo sapiens, Mus musculus
Stone, S.J.; Levin, M.C.; Farese, R.V.
Membrane topology and identification of key functional amino acid residues of murine acyl-CoA:diacylglycerol acyltransferase-2
J. Biol. Chem.
281
40273-40282
2006
Mus musculus
Yen, C.L.; Monetti, M.; Burri, B.J.; Farese, R.V.
The triacylglycerol synthesis enzyme DGAT1 also catalyzes the synthesis of diacylglycerols, waxes, and retinyl esters
J. Lipid Res.
46
1502-1511
2005
Mus musculus (Q9DCV3), Mus musculus (Q9Z2A7)
Millar, J.S.; Stone, S.J.; Tietge, U.J.; Tow, B.; Billheimer, J.T.; Wong, J.S.; Hamilton, R.L.; Farese, R.V.; Rader, D.J.
Short-term overexpression of DGAT1 or DGAT2 increases hepatic triglyceride but not VLDL triglyceride or apoB production
J. Lipid Res.
47
2297-2305
2006
Mus musculus (Q9DCV3), Mus musculus (Q9Z2A7), Mus musculus
Lung, S.C.; Weselake, R.J.
Diacylglycerol acyltransferase: a key mediator of plant triacylglycerol synthesis
Lipids
41
1073-1088
2006
Acinetobacter calcoaceticus, Arabidopsis thaliana, Arabidopsis thaliana (Q9SLD2), Arachis hypogaea, Brassica napus, Brassica napus (Q9XGR5), Brassica napus (Q9XGV4), Carthamus tinctorius, Ricinus communis, Ricinus communis (Q67C39), Glycine max, Umbelopsis ramanniana, Mus musculus, Mus musculus (Q9Z2A7), Olea europaea, Rattus norvegicus, Spinacia oleracea, Zea mays, Cuphea sp., Nicotiana tabacum (Q9SEG9)
Villanueva, C.J.; Monetti, M.; Shih, M.; Zhou, P.; Watkins, S.M.; Bhanot, S.; Farese, R.V.
Specific role for acyl CoA:diacylglycerol acyltransferase 1 (Dgat1) in hepatic steatosis due to exogenous fatty acids
Hepatology
50
434-442
2009
Mus musculus
Cheng, D.; Iqbal, J.; Devenny, J.; Chu, C.H.; Chen, L.; Dong, J.; Seethala, R.; Keim, W.J.; Azzara, A.V.; Lawrence, R.M.; Pelleymounter, M.A.; Hussain, M.M.
Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal fat absorption
J. Biol. Chem.
283
29802-29811
2008
Homo sapiens, Mus musculus, Rattus norvegicus
McFie, P.J.; Banman, S.L.; Kary, S.; Stone, S.J.
Murine diacylglycerol acyltransferase-2 (DGAT2) can catalyze triacylglycerol synthesis and promote lipid droplet formation independent of its localization to the endoplasmic reticulum
J. Biol. Chem.
286
28235-28246
2011
Mus musculus (Q9DCV3), Mus musculus
Li, C.; Li, L.; Lian, J.; Watts, R.; Nelson, R.; Goodwin, B.; Lehner, R.
Roles of acyl-CoA:diacylglycerol acyltransferases 1 and 2 in triacylglycerol synthesis and secretion in primary hepatocytes
Arterioscler. Thromb. Vasc. Biol.
35
1080-1091
2015
Mus musculus
McFie, P.J.; Jin, Y.; Banman, S.L.; Beauchamp, E.; Berthiaume, L.G.; Stone, S.J.
Characterization of the interaction of diacylglycerol acyltransferase-2 with the endoplasmic reticulum and lipid droplets
Biochim. Biophys. Acta
1841
1318-1328
2014
Mus musculus
Kaylor, J.J.; Radu, R.A.; Bischoff, N.; Makshanoff, J.; Hu, J.; Lloyd, M.; Eddington, S.; Bianconi, T.; Bok, D.; Travis, G.H.
Diacylglycerol O-acyltransferase type-1 synthesizes retinyl esters in the retina and retinal pigment epithelium
PLoS ONE
10
e0125921
2015
Mus musculus
Hong, D.J.; Jung, S.H.; Kim, J.; Jung, D.; Ahn, Y.G.; Suh, K.H.; Min, K.H.
Synthesis and biological evaluation of novel thienopyrimidine derivatives as diacylglycerol acyltransferase 1 (DGAT-1) inhibitors
J. Enzyme Inhib. Med. Chem.
35
227-234
2020
Canis lupus familiaris (E2RDN4), Canis lupus familiaris, Homo sapiens (O75907), Rattus norvegicus (Q9ERM3), Mus musculus (Q9Z2A7), Mus musculus
Xu, Y.; Caldo, K.M.P.; Pal-Nath, D.; Ozga, J.; Lemieux, M.J.; Weselake, R.J.; Chen, G.
Properties and biotechnological applications of acyl-CoA diacylglycerol acyltransferase and phospholipid diacylglycerol acyltransferase from terrestrial plants and microalgae
Lipids
53
663-688
2018
Arabidopsis thaliana, Arabidopsis thaliana (Q9ASU1), Arabidopsis thaliana (Q9C5W0), Arabidopsis thaliana (Q9SLD2), Arachis hypogaea, Arachis hypogaea (A0A0M3SGK9), Arachis hypogaea (Q2KP14), Chlamydomonas reinhardtii, Linum usitatissimum, Linum usitatissimum (V5LV83), Linum usitatissimum (V5LV86), Nicotiana tabacum, Nicotiana tabacum (Q9SEG9), Phaeodactylum tricornutum, Tropaeolum majus, Tropaeolum majus (Q8RX96), Triadica sebifera, Boechera stricta, Cuphea avigera var. pulcherrima (A0A193DVK9), Cuphea avigera (A0A193DVK9), Ricinus communis (A1A442), Ricinus communis (Q67C39), Zea mays (B0LF77), Echium pitardii (D9U3F8), Glycine max (I1MSF2), Glycine max (Q5GKZ7), Brassica napus (K9LL63), Brassica napus (Q9XGR5), Brassica napus (Q9XGV4), Sesamum indicum (M1E7W9), Vernicia fordii (Q0QJH9), Vernicia fordii (Q0QJI1), Euonymus alatus (Q5UEM2), Olea europaea (Q6ED63), Umbelopsis ramanniana (Q96UY1), Umbelopsis ramanniana (Q96UY2), Caenorhabditis elegans (Q9XUW0), Mus musculus (Q9Z2A7), Thraustochytrium aureum (R9QY77)
Brandt, C.; McFie, P.J.; Vu, H.; Chumala, P.; Katselis, G.S.; Stone, S.J.
Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein
PLoS ONE
14
e0210396
2019
Mus musculus (Q9DCV3), Mus musculus
EXTERNAL LINKS (specific for EC-Number 2.3.1.20)
Transporter Classification Database (TCDB): 2.A.50.4.1, 2.A.50.4.10
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