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Results 1 - 10 of 31 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22evolution 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 736458
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22evolution 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 735610
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22malfunction knockout of MOGAT3 attenuates MGAT activity in a liver-derived cell line 720180
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22malfunction 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 -, 736602
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22malfunction 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 701625
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22malfunction 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 705856
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22malfunction overexpression of the OLE3 gene in Saccharomyces cerevisiae results in an increased accumulation of diacylglycerols and triacylglycerols and decreased phospholipids 720021
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22malfunction 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 735610
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22metabolism crucial role in assimilation of dietary fat 705856
Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.22metabolism diacylglyceride synthesis, involved in triglyceride and phospholipid synthesis 703312
Results 1 - 10 of 31 > >>