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evolution
the enzyme belongs to the evolutionarily conserved acyltransferase gene family. All DGAT2 family members, including monoacylglycerol acyltransferases (MGAT)1-3 and wax synthases 1 and 2, contain a highly conserved four amino acid sequence - histidine-proline-histidine-glycine
evolution
three subtypes of monoacylglycerol O-acyltransferase, MGAT, enzymes, MGAT1, MGAT2, and MGAT3: in a phylogenetic tree with inferred evolutionary relationships, MGAT3 shares higher sequence homology with the diacylglycerol O-acyltransferase 2 enzyme than with MGAT1 or MGAT2, phylogenetic analysis
malfunction
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mice with targeted inactivation of the MGAT2 gene exhibit a delay in dietary fat absorption, however, in contrast to knockout mice that absorb normal quantities of fat
malfunction
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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
malfunction
knockout of MOGAT3 attenuates MGAT activity in a liver-derived cell line
malfunction
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overexpression of the OLE3 gene in Saccharomyces cerevisiae results in an increased accumulation of diacylglycerols and triacylglycerols and decreased phospholipids
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
malfunction
the enzyme is involved in hepatic steatosis, characterized by an increase in intrahepatic triacylglycerol, is an important marker of metabolic dysfunction and is associated closely with insulin resistance and dyslipidemia. Inhibition of MGAT1 ameliorates hepatic steatosis in human liver Hep-G2 cell line, inhibition of MGAT1 by siRNA treatment efficiently ameliorates the lipid accumulation
malfunction
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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
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metabolism
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crucial role in assimilation of dietary fat
metabolism
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diacylglyceride synthesis, involved in triglyceride and phospholipid synthesis
metabolism
diacylglyceride synthesis, involved in triglyceride and phospholipid synthesis
metabolism
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monoacylglycerol pathway followed by diacylglycerol acyltransferase activity to produce triacylglycerol
metabolism
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monoacylglycerol pathway is followed by diacylglycerol acyltransferase activity to produce triacylglycerol
metabolism
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significant role in hepatic triacylglycerol synthesis and secretion in diabetic mice (db/db)
metabolism
overexpression of the MGAT gene in yeast (Saccharomyces cerevisiae) causes an increase in triacylglycerol accumulation
metabolism
the enzyme interacts with the acyl CoA:1,2-diacylglycerol acyltransferase (DGAT)-2, an endoplasmic reticulum integral membrane protein that catalyzes triacylglycerol synthesis using diacylglycerol and fatty acyl CoA as substrates. Deletion mutagenesis shows that the interaction with MGAT2 is dependent on the two transmembrane domains of DGAT2. The interaction of the enzyme and DGAT2 serves to channel lipid substrates efficiently for triacylglycerol biosynthesis
metabolism
the enzyme is involved in triglyceride synthesis by catalyzing the formation of diacylglycerol from monoacylglycerol and fatty acyl CoAs
physiological function
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besides being the substrates for monoacylglycerol acyltransferase, monoacylglycerols, especially 2-acylglycerol, function as endogenous ligand for endocannaboid receptors, thus stimulating appetite
physiological function
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involved in energy storage (fat digestion and absorption), lipoprotein and membrane formation, intracellular signaling for protein kinase activation
physiological function
involved in energy storage (fat digestion and absorption), lipoprotein and membrane formation, intracellular signaling for protein kinase activation
physiological function
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involved in functions such as intestinal fat absorption, lipoprotein assembly, adipose tissue formation, signal transduction, satiety, lactation, for example by the modulation of intracellular levels of monoacylglycerols and diacylglycerols
physiological function
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involved in functions such as intestinal fat absorption, lipoprotein assembly, adipose tissue formation, signal transduction, satiety, lactation, for example by the modulation of intracellular levels of monoacylglycerols and diacylglycerols, 2-acylglycerol functions as endogenous ligand for endocannaboid receptors, stimulating appetite
physiological function
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involved in functions such as intestinal fat absorption, lipoprotein assembly, adipose tissue formation, signal transduction, satiety, lactation, for example by the modulation of intracellular levels of monoacylglycerols and diacylglycerols, 2-acylglycerol functions as endogenous ligand for endocannaboid receptors, stimulating apppetite
physiological function
involvid in energy storage (fat digestion and absorption), lipoprotein and membrane formation, intracellular signaling for protein kinase activation
physiological function
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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
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heterologous expression of Arabidopsis thaliana GPAT4 acyltransferase in Saccharomyces cerevisiae GPAT mutant can produce monoacylglycerol using oleoyl-CoA as the acyl-donor
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
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
physiological function
in the intestine, the majority of diacylglycerol is produced by the MGAT pathway via monoacylglycerol acyltransferase-2, MGAT2, which catalyzes the synthesis of diacylglycerol in an acyl CoA-dependent manner using 2-monoacylglycerol as an acyl acceptor. Co-expression of acyl CoA:1,2-diacylglycerol acyltransferase, DGAT2, and monoacylglycerol acyltransferase MGAT2 stimulates triacylglycerol storage
physiological function
monoacylglycerol O-acyltransferase 1 is regulated by peroxisome proliferator-activated receptor gamma in human hepatocytes and increases lipid accumulation
physiological function
the enzyme is involved in diabetes, obesity and other diseases which together constitute the metabolic syndrome
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
physiological function
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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
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