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Information on EC 2.3.1.22 - 2-acylglycerol O-acyltransferase and Organism(s) Mus musculus and UniProt Accession Q80W94
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EC Tree
2.3.1.22 2-acylglycerol O-acyltransferaseIUBMB Comments
Various 2-acylglycerols can act as acceptor; palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. The sn-1 position and the sn-3 position are both acylated, at about the same rate.
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Word Map
- 2.3.1.22
- n-glycans
-
mgats
- diacylglycerols
- triacylglycerol
-
n-acetylglucosaminyltransferase
-
bisect
- glcnac
- gnt-iii
-
nipecotic
-
glycome
-
tiagabine
-
acyl-coa:diacylglycerol
- medicine
- st6gal1
- drug development
- pharmacology
- analysis
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
mgat1, mgat2, mgat3, mogat1, lpgat1, mogat2, mogat3, acyl-coa:monoacylglycerol acyltransferase, monoacylglycerol o-acyltransferase, monoacylglycerol o-acyltransferase 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl coenzyme A-monoglyceride acyltransferase
-
-
-
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acyl-CoA:monoacylglycerol transferase
-
-
-
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acylglycerol palmitoyltransferase
-
-
-
-
MGAT
monoacylglycerol acyltransferase
-
-
-
-
monoglyceride acyltransferase
-
-
-
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palmitoyltransferase, acylglycerol
-
-
-
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MGAT
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:2-acylglycerol O-acyltransferase
Various 2-acylglycerols can act as acceptor; palmitoyl-CoA and other long-chain acyl-CoAs can act as donors. The sn-1 position and the sn-3 position are both acylated, at about the same rate.
CAS REGISTRY NUMBER
COMMENTARY
9055-17-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-acyl-sn-glycerol + palmitoyl-CoA
diacylglycerol + CoA
-
in vitro assay in lysate of transfected CHO cells or of microsome preparation of mouse liver, 2-monoacylglycerol is preferred over 1-monoacylglycerol, 25°C, pH 6.4
-
-
?
2-monooleoylglycerol + palmitoyl-CoA
2-oleoyl-3-palmitoylglycerol + CoA
-
-
-
-
?
arachidonoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-arachidonoyl-2-oleoylglycerol
-
-
-
?
arachidoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-arachidoyl-2-oleoylglycerol
-
-
-
?
lauroyl-CoA + sn-2-monooleoylglycerol
CoA + 1-lauroyl-2-oleoylglycerol
-
-
-
?
linoleoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-linoleoyl-2-oleoylglycerol
-
-
-
?
n-octanoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-octanoyl-2-oleoylglycerol
-
-
-
?
oleoyl-CoA + sn-1-monooleoylglycerol
CoA + sn-1,3-dioleoylglycerol
-
-
?
oleoyl-CoA + sn-3-monostearoylglycerol
CoA + 1-oleoyl-3-stearoylglycerol
-
-
?
palmitoyl-CoA + sn-2-monooleoylglycerol
CoA + 1(3)-palmitoyl-2-oleoylglycerol
-
-
-
?
rac-1-monoacylglycerol + palmitoyl-CoA
diacylglycerol + CoA
-
in vitro assay in lysate of transfected CHO cells, 25°C, pH 6.4
-
-
?
stearoyl-CoA + sn-2-monooleoylglycerol
CoA + 1-stearoyl-2-oleolyglycerol
-
-
-
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
the enzyme plays a predominant role in dietary fat absorption in the small intestine, where it catalyzes the first step of triacylglycerol resynthesis in enterocytes for chylomicron formation and secretion
-
-
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
in the intestine the enzyme plays a major role in the absorption of dietary fat because resynthesis of triacylglycerol is required for the assembly of lipoproteins that transport absorbed fat to other tissues
-
-
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
MGAT2 may play an important role in dietary fat absorption
-
-
?
monoacylglycerol + acyl-CoA
diacylglycerol + CoA
-
radioactive monoacylglycerol administration to the lumen of the small intestine
-
-
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + sn-1,2(2,3)-dioleoylglycerol
-
-
-
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + sn-1,2(2,3)-dioleoylglycerol
-
-
-
-
?
oleoyl-CoA + sn-2-monooleoylglycerol
CoA + sn-1,2(2,3)-dioleoylglycerol
-
-
?
additional information
?
-
-
the enzyme catalyzes the acylation of rac-1-monoacylglycerol, sn-2-monoacylglycerol, and sn-3-monoacylglycerols, the enzyme prefers monoacylglycerols containing unsaturated fatty acyls
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-
?
additional information
?
-
-
predominant role of enzyme in dietary fat absorption
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-
?
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
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-
?
additional information
?
-
-
no significant production of phosphatidic acid (substrate lysophosphatidic acid), triacylglycerol (diacylglycerol), or cholesterol ester (substrate cholesterol), 25°C, pH 6.4
-
-
?
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
2-monooleoylglycerol + palmitoyl-CoA
2-oleoyl-3-palmitoylglycerol + CoA
-
-
-
-
?
additional information
?
-
-
predominant role of enzyme in dietary fat absorption
-
-
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
the enzyme plays a predominant role in dietary fat absorption in the small intestine, where it catalyzes the first step of triacylglycerol resynthesis in enterocytes for chylomicron formation and secretion
-
-
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
in the intestine the enzyme plays a major role in the absorption of dietary fat because resynthesis of triacylglycerol is required for the assembly of lipoproteins that transport absorbed fat to other tissues
-
-
?
acyl-CoA + sn-2-monoacylglycerol
CoA + diacylglycerol
-
MGAT2 may play an important role in dietary fat absorption
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1r,4r)-4-([[(3,3,4,4,4-pentafluoro-2-methylbutan-2-yl)oxy]carbonyl]amino)cyclohexyl 5-[(4-chloro-2,6-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
compound inhibits elevation of plasma triglyceride in mice challenged with an oil-supplemented liquid meal. Oil challenge stimulates the secretion of hormones peptide tyrosine-tyrosine and glucagon-like peptide-1 into the bloodstream, and these responses are augmented in mice pretreated with the inhibitor. Administration of the compound to high-fat diet-fed ob/ob mice for 5 weeks suppresses food intake and body weight gain and inhibits elevation of glycated hemoglobin
(3R)-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
1-(2,2,3,3,3-pentafluoropropyl)piperidin-4-yl 5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxoimidazolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
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1-([1,1'-biphenyl]-4-yl)-N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
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2-[2-(4-tert-butylphenyl)ethyl]-N-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-[2-(4-tert-butylphenyl)ethyl]-N-[4-(3-cyclopentylpropyl)-2-fluorophenyl]-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]-N-(2,2,3,3,3-pentafluoropropyl)pyrimidine-5-carboxamide
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3-ethyl-3-methyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
MGAT2 inhibitor for the treatment of metabolic diseases and nonalcoholic steatohepatitis
benzyl 2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(5-oxopyrazolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]pyrimidine-5-carboxylate
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N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-1-phenyl-2,3-dihydro-1H-indole-5-sulfonamide
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shRNA-adenovirus
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short hairpin RNA adenovirus construct to knockdown mouse lysophosphatidylglycerol acyltransferase 1, injected via tail vein
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000085
(1r,4r)-4-([[(3,3,4,4,4-pentafluoro-2-methylbutan-2-yl)oxy]carbonyl]amino)cyclohexyl 5-[(4-chloro-2,6-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.00005
(3R)-N-(2,4-difluorophenyl)-3-ethyl-3-methyl-2,5-dioxo-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.0000038
1-(2,2,3,3,3-pentafluoropropyl)piperidin-4-yl 5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxoimidazolidin-1-yl)-2,3-dihydro-1H-indole-1-carboxylate
Mus musculus
pH 7.4, 23°C
0.0000016
1-([1,1'-biphenyl]-4-yl)-N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Mus musculus
pH 7.4, 23°C
0.00117
2-[2-(4-tert-butylphenyl)ethyl]-N-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.000004
2-[2-(4-tert-butylphenyl)ethyl]-N-[4-(3-cyclopentylpropyl)-2-fluorophenyl]-1,2,3,4-tetrahydroisoquinoline-6-sulfonamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.0000019
2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(2-oxopyrrolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]-N-(2,2,3,3,3-pentafluoropropyl)pyrimidine-5-carboxamide
Mus musculus
pH 7.4, 23°C
0.002511
3-ethyl-3-methyl-2,5-dioxo-N-phenyl-2,3,4,5-tetrahydro-1H-1,4-benzodiazepine-7-sulfonamide
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.0000011
benzyl 2-[5-[(2,4-difluorophenyl)sulfamoyl]-7-(5-oxopyrazolidin-1-yl)-2,3-dihydro-1H-indol-1-yl]pyrimidine-5-carboxylate
Mus musculus
pH 7.4, 23°C
0.0000006
N-(2,4-difluorophenyl)-7-(2-oxopyrrolidin-1-yl)-1-phenyl-2,3-dihydro-1H-indole-5-sulfonamide
Mus musculus
pH 7.4, 23°C
additional information
shRNA-adenovirus
Mus musculus
-
infection with 60000000000 particles per animal (dose limit of no effect of control particles) leads to 83% decreased mRNA levels on day 5, 92% decrease on day 16 post-injection, associated with reduces hepatic MGAT and LPGAT activities (pH 6.4, 25°C), slight body weight reduction despite normal food consumption throughout most of the experimental treatment period (only 15% reduction on day 2), reduced serum triacylglycerols and cholesterol but increased total cholesterol accumulation in the liver
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MGAT1 localizes to the endoplasmic reticulum under normal conditions, and colocalizes to lipid droplets under conditions of enriching fatty acids, contributing to TAG synthesis and LD expansion
MGAT1 localizes to the endoplasmic reticulum under normal conditions, and colocalizes to lipid droplets under conditions of enriching fatty acids, contributing to TAG synthesis and LD expansion
for the enzyme activity, both the N-terminal transmembrane domain and catalytic HPHG motif are required. The transmembrane domain consists of two hydrophobic regions in the N-terminus, the consensus sequence FLXLXXXn, a putative neutral lipid-binding domain, exists in the first transmembrane domain
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
mice lacking the gene Mogat2 , which codes for an MGAT highly expressed in the small intestine, are resistant to obesity and other metabolic disorders induced by high-fat feeding. The Mogat2-deficient mice absorb normal amounts of dietary fat but exhibit a reduced rate of fat absorption, increased energy expenditure, decreased respiratory exchange ratio, and impaired metabolic efficiency. Recombinant expression of the human gene MOGAT2, encoding the enzyme, in the intestine increases intestinal MGAT activity, restores fat absorption rate, partially corrects energy expenditure, and promotes weight gain upon high-fat feeding. The changes in respiratory exchange ratio are not reverted, and the recoveries in metabolic efficiency and weight gain are incomplete
physiological function
acyl CoA:monoacylglycerol acyltransferase (MGAT) catalyzes the resynthesis of triacylglycerol, a crucial step in the absorption of dietary fat. MGAT2 in the intestine plays an indispensable role in enhancing metabolic efficiency, in other tissues it may contribute to the regulation of energy metabolism
malfunction
-
Mogat2 (-/-) mice lack MGAT2 protein and have a greater than 50% decrease in intestinal MGAT activity compared to wild-type mice, they display a normal weight gain and body composition on low-fat diet, with 60% calories from fat knockout mice gain 40% less weight than wild-type mice after 16 weeks, Mogat2 (+/-) mice show an intermediate phenotype, female mice with 60% fat containing diet and males with a 45% fat containing diet also show reduced weight gain, knockout mice show lower fasting insulin concentrations, better glucose tolerance, lower concentrations of total and non-high-density lipoprotein cholesterol in plasma, similar plasma triacylglycerol concentrations as wild-type mice, and less than 5% of wild-type hepatic triacylglycerol content, 7% higher oxygen consumption during active (dark) phase and a higher body temperature (while the mechanism of the increased thermogenisis remains unclear) but similar locomotive activity, similar fat absorption in knockout and wild-type mice, similar fecal fat amounts, fecal mass and energy content, 70% triacylglycerol synthesis in enterocytes compared to wild-type, residual diacylglycerol formation from monoacylglycerol or alternative pathway via breakdown of monoacylglycerol to glycerol and fatty acids and entering into the glycerol-phosphate pathway which is more energy demanding, knockout mice show a reduced rate of fat entering the circulation upon a fat boost, more fat enters the distal intestine, therefore fat entry into the circulation is delayed
metabolism
physiological function
metabolism
-
significant role in hepatic triacylglycerol synthesis and secretion in diabetic mice (db/db)
physiological function
-
heterologous expression of a mouse MGAT acyltransferase in Nicotiana benthamiana significantly increases TAG accumulation in vegetative tissues despite the low levels of endogenous MAG substrate available. In addition, diacylglycerol produced by this acyltransferase can serve as a substrate for both native and coexpressed diacylglycerol acyltransferases
physiological function
hepatic expression of Mogat1 is significantly increased in the liver of fasted mice compared with mice given ad libitum access to food. Basal and fasting-induced expression of Mogat1 is markedly diminished in the liver of mice lacking the transcription factor PPARalpha. Suppressing Mogat1 expression in liver and adipose tissue with antisense oligonucleotides reduces hepatic MGAT activity and triglyceride content compared with fasted controls. The expression of many other PPARalpha target genes and PPARalpha activity is also decreased in mice given Mogat1 antisense oligonucleotides
physiological function
MGAT1 expression is reduced in physiologic contexts where lipolysis is high. Knockdown or knockout of MGAT1 in adipocytes leads to higher rates of basal adipocyte lipolysis
physiological function
MGAT1 interacts with DGAT2, which serves to synergistically increase the TAG biosynthesis and lipid droplet expansion, leading to enhancement of lipid accumulation in the liver and fat
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). MOGT2_MOUSE
334
1
38591
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
expression of human MGAT2 in the intestine of Mogat2-/- mice promotes the uptake and esterification of monoaclglycerol, and partially restores metabolic efficiency in diet-induced weight gain
additional information
-
knockdown of hepatic lysophosphatidylglycerol acyltransferase 1 gene expression in transfected CHO cells by an adenovirus construct of short hairpin RNA (shRNA)
additional information
-
Mogat2-targeted 129/SvJae embryonic stem cells are generated with a targeting vector designed to replace exon 1 of Mogat2 including the translation-initiating methionine, Mogat2 (-/-) and wild-type are generated from breeding heterozygotes (first backcrossed with C57BL/6J mice)
additional information
mutant FL-DELTA1-160, with both transmembrane regions deleted, displays relocation in the cytosol. Mutant FL-DELTA161-335, which contains the N-terminus and the two transmembrane domains, exists in the membrane fraction
additional information
-
mutant FL-DELTA1-160, with both transmembrane regions deleted, displays relocation in the cytosol. Mutant FL-DELTA161-335, which contains the N-terminus and the two transmembrane domains, exists in the membrane fraction
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Mogat2, expression analysis, comparison of the relative expression levels of human MGAT2 in the transgenic mice to those of endogenous mouse MGAT2 in the wild-type mice
PCR-amplification, transfection and expression of CHO cells with FLAG-tagged enzyme cDNA plasmid
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
basal and fasting-induced expression of Mogat1 is markedly diminished in the liver of mice lacking the transcription factor PPARalpha
expression of MGAT1 is robustly induced during adipocyte differentiation and its expression is suppressed in fat of genetically-obese mice
hepatic expression of Mogat1 is significantly increased in the liver of fasted mice compared with mice given ad libitum access to food
hepatic LPGAT1 expression in diabetic (db/db) mice is 2fold higher than in control (db/m), consistent with 1.5fold higher hepatic monoacylglycerol acyltransferase activity
-
the infection with a short hairpin RNA-adenovirus construct lowers the lysophosphatidylglycerol acyltransferase 1 expression in diabetic (db/db) mice compared to a control virus infection in a dose-dependent manner, causing a marked reduction in serum triacylglycerol and cholesterol levels, and a significant increase in hepatic cholesterol levels
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
enzyme expression is not affected during diabetes, while total intestinal activity is significantly increased. Up-regulation of both enzyme expression and activity in animals fed with high fat diet
medicine
-
enzyme deficiency protects mice from metabolic disorders (obesity, glucose intolerance, hypercholesterolemia, and fatty liver) despite high-fat diet, caloric intake is normal and dietary fat is absorbed fully but entry into the circulation is reduced, enzyme may be useful target to treat obesity and other metabolic diseases associated with excessive fat intake
medicine
expression of MGAT1 is robustly induced during adipocyte differentiation and its expression is suppressed in fat of genetically-obese mice
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cao, J.; Lockwood, J.; Burn, P.; Shi, Y.
Cloning and functional characterization of a mouse intestinal acyl-CoA: monoacylglycerol acyltransferase, MGAT2
J. Biol. Chem.
278
13860-13866
2003
Mus musculus
Yen, C.L.E.; Stone, S.J.; Cases, S.; Zhou, P.; Farese, R.V., Jr.
Identification of a gene encoding MGAT1, a monoacylglycerol acyltransferase
Proc. Natl. Acad. Sci. USA
99
8512-8517
2002
Mus musculus (Q91ZV4)
Yen, C.L.; Farese, R.V., Jr.
MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine
J. Biol. Chem.
5
1-24
2003
Homo sapiens, Mus musculus
-
Cao, J.; Hawkins, E.; Brozinick, J.; Liu, X.; Zhang, H.; Burn, P.; Shi, Y.
A predominant role of acyl-CoA:monoacylglycerol acyltransferase-2 in dietary fat absorption implicated by tissue distribution, subcellular localization, and up-regulation by high fat diet
J. Biol. Chem.
279
18878-18886
2004
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
Hiramine, Y.; Emoto, H.; Takasuga, S.; Hiramatsu, R.
Novel acyl-coenzyme A:monoacylglycerol acyltransferase (MGAT) plays an important role in hepatic triacylglycerol secretion
J. Lipid Res.
51
1424-1431
2010
Mus musculus
Yen, C.L.; Cheong, M.L.; Grueter, C.; Zhou, P.; Moriwaki, J.; Wong, J.S.; Hubbard, B.; Marmor, S.; Farese, R.V.
Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding
Nat. Med.
15
442-446
2009
Mus musculus
Yue, Y.G.; Chen, Y.Q.; Zhang, Y.; Wang, H.; Qian, Y.W.; Arnold, J.S.; Calley, J.N.; Li, S.D.; Perry, W.L.; Zhang, H.Y.; Konrad, R.J.; Cao, G.
The acyl coenzymeA:monoacylglycerol acyltransferase 3 (MGAT3) gene is a pseudogene in mice but encodes a functional enzyme in rats
Lipids
46
513-520
2011
Mus musculus, Rattus norvegicus
Petrie, J.R.; Vanhercke, T.; Shrestha, P.; El Tahchy, A.; White, A.; Zhou, X.R.; Liu, Q.; Mansour, M.P.; Nichols, P.D.; Singh, S.P.
Recruiting a new substrate for triacylglycerol synthesis in plants: the monoacylglycerol acyltransferase pathway
PLoS ONE
7
e35214
2012
Arabidopsis thaliana, Mus musculus
Gao, Y.; Nelson, D.W.; Banh, T.; Yen, M.I.; Yen, C.L.
Intestine-specific expression of MOGAT2 partially restores metabolic efficiency in Mogat2-deficient mice
J. Lipid Res.
54
1644-1652
2013
Homo sapiens (Q3SYC2), Homo sapiens, Mus musculus (Q80W94), Mus musculus C57/BL6J (Q80W94)
Lee, Y.J.; Kim, J.W.
Monoacylglycerol O-acyltransferase 1 (MGAT1) localizes to the ER and lipid droplets promoting triacylglycerol synthesis
BMB Rep.
50
367-372
2017
Mus musculus (Q91ZV4), Mus musculus
Adachi, R.; Ishii, T.; Ogawa, K.; Matsumoto, S.; Satou, T.; Sakamoto, J.; Sato, K.; Kawamoto, T.
Pharmacological characterization of a series of aryl-sulfonamide derivatives that potently and selectively inhibit monoacylglycerol acyltransferase 2
Eur. J. Pharmacol.
791
569-577
2016
Homo sapiens (Q3SYC2), Homo sapiens, Mus musculus (Q80W94), Mus musculus
Mochida, T.; Take, K.; Maki, T.; Nakakariya, M.; Adachi, R.; Sato, K.; Kitazaki, T.; Takekawa, S.
Inhibition of MGAT2 modulates fat-induced gut peptide release and fat intake in normal mice and ameliorates obesity and diabetes in ob/ob mice fed on a high-fat diet
FEBS Open Bio
10
316-326
2020
Homo sapiens (Q3SYC2), Mus musculus (Q80W94)
Liss, K.H.H.; Lutkewitte, A.J.; Pietka, T.; Finck, B.N.; Franczyk, M.; Yoshino, J.; Klein, S.; Hall, A.M.
Metabolic importance of adipose tissue monoacylglycerol acyltransferase 1 in mice and humans
J. Lipid Res.
59
1630-1639
2018
Homo sapiens (Q96PD6), Homo sapiens, Mus musculus (Q91ZV4)
Lutkewitte, A.J.; McCommis, K.S.; Schweitzer, G.G.; Chambers, K.T.; Graham, M.J.; Wang, L.; Patti, G.J.; Hall, A.M.; Finck, B.N.
Hepatic monoacylglycerol acyltransferase 1 is induced by prolonged food deprivation to modulate the hepatic fasting response
J. Lipid Res.
60
528-538
2019
Mus musculus (Q91ZV4)
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