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Monoacyglycerol acyltransferases (MGATs) and diacylglycerol acyltransferases (DGATs) catalyze two consecutive steps of enzyme reactions in the synthesis of triacylglycerols (TAGs).
MGAT catalyzes the first step in TAG synthesis involved in dietary absorption by enterocytes.
DGAT catalyzes the final step in mammalian TAG synthesis that merges the MGAT and G-3-P pathways (Fig.
In addition to the synthesis of TAG, the MGAT and DGAT enzymes also modulate intracellular levels of MAG and DAG, two important signaling molecules. Digestion is needed to breakdown large insoluble molecules found in the bolus into smaller soluble molecules.  These molecules can then absorbed through the walls of the small intestine and onto the blood stream by diffusion. The muscle before the bolus of food contract and the muscles after the bolus relax resulting in a wave of muscular contractions which pushes the bolus through the oesophagus.
In the duodenum, the bile produced by the liver as well as the enzymes produced by the pancreas are released in the alimentary canal and they will mix with the food. In the digestive system, ingested food is converted into a form that can be absorbed into the circulatory system for distribution to and utilization by the various tissues of the body. To begin with this topic it is important to know what a mammal is.The following link gives you a good introduction to what a mammal is. The metabolic complexity of TAG synthesis is reflected by the presence of multiple isoforms of MGAT and DGAT enzymes that differ in catalytic properties, subcellular localization, tissue distribution, and physiological functions.
Three isoforms of MGAT enzymes, known as MGAT1, MGAT2, and MGAT3, have been identified so far. DAG is an activator for protein kinase C (PKC), which regulates insulin sensitivity in the liver and skeletal muscles (43).
The acid lowers the pH of the gastric juices to a value close to the pH optimum for pepsin. This is accomplished both physically, by mastication in the mouth and churning of the stomach, and chemically, by secretions and enzymes of the gastrointestinal tract. MGAT and DGAT enzymes play fundamental roles in the metabolism of monoacylglycerol (MAG), diacylglycerol (DAG), and triacylglycerol (TAG) that are involved in many aspects of physiological functions, such as intestinal fat absorption, lipoprotein assembly, adipose tissue formation, signal transduction, satiety, and lactation.
All three MGAT isoforms possess strong MGAT enzyme activity and are localized in the endoplasmic reticulum (ER) (11, 14, 22, 78, 79).
2-Arachidonoylglycerol (2-AG) in the brain is a natural ligand for endocannabinoid receptors, which regulate various physiological events, including appetite (27, 48, 65). The recent progress in the phenotypic characterization of mice deficient in MGAT and DGAT enzymes and the development of chemical inhibitors have revealed important roles of these enzymes in the regulation of energy homeostasis and insulin sensitivity. The monoacylglycerol (MAG) pathway begins with the acylation of MAG with a fatty acyl-CoA by monoacylglycerol acyltransferase (MGAT).


DGAT1 is a member of the mammalian ACAT gene family (13, 53), whereas DGAT2 belongs to a new family of acyltransferases that includes the three MGAT enzymes. Consequently, the MGAT and DGAT families of enzymes are implicated in the regulation of various physiological functions, such as dietary fat absorption, lipid metabolism, fat storage, insulin sensitivity, satiety, and energy homeostasis (Fig.
Respiration later down the page will go into more detail but the basic respiration idea is that cells need food, oxygen and waste removed. Consequently, selective inhibition of MGAT or DGAT enzymes by synthetic compounds may provide novel treatment for obesity and its related metabolic complications. This pathway plays a predominant role in the enterocytes after feeding, where large amounts of 2-MAG and fatty acids (FA) are released from the digestion of dietary lipids (57). The MGAT1 mRNA has been detected mainly in stomach, kidney, and adipose tissue, whereas MGAT2 and MGAT3 exhibit highest expression in the small intestine (11, 22, 78, 79). In addition to DAG, both DGAT1 and DGAT2 also recognize MAG as a substrate in the synthesis of TAG (21, 75).
The MAG pathway is also active in adipose tissue (58), likely playing a role in storing excess energy in the form of TAG. Although both DGAT1 and DGAT2 enzymes catalyze the same reactions in TAG synthesis with DAG or MAG and acyl-CoA as substrates, they are functionally distinguished by their differences in catalytic properties (9, 21), subcellular localization (64), physiological regulation (50), and phenotypic consequences when rendered deficient in mice (61, 63). A second pathway to TAG synthesis is the glycerol 3-phosphate (G-3-P) pathway, a de novo pathway in most tissues, including the small intestine. The G-3-P pathway begins with the acylation of G-3-P with a fatty acyl-CoA, producing lysophosphatidic acid, followed by further acylation and dephosphorylation to yield diacylglycerol (DAG) (5, 26). Although named after its enzyme activity, MGAT3 shares higher sequence homology with DGAT2 than with the other MGAT isoforms. However, the DGAT activity of DGAT1 is dramatically inhibited when high concentration of MAG is used as a substrate, resulting in an increased production of DAG (21). When low concentrations of 2-MAG are used as a substrate, the major enzyme product of MGAT3 is TAG (21). Overexpression of DGAT1 results in the accumulation of small lipid droplets around the cell periphery, whereas overexpression of DGAT2 leads to increases in large cytosolic lipid droplets (63). The monoacylglycerol (MAG) pathway, also known as the remodeling pathway, begins with the acylation of MAG with fatty acyl-CoA catalyzed by monoacylglycerol acyltransferase (MGAT). In contrast, DAG is the major enzymatic product when high concentrations of 2-MAG are used as a substrate (21). This difference may be related to the previous reports on two proposed types of DGAT activities in liver microsomes, an overt activity that regulates the cytosolic TAG pools and another that is latent and plays a role in TAG secretion (55, 71). This pathway dominates in the small intestine, a tissue primarily responsible for dietary fat absorption. It can be envisaged that MGATs and DGAT2 enzymes may be evolved from a common ancestral gene.


This is supported by studies in which inactivation of the yeast Dgat1 gene resulted in the reduction of DGAT activity on lipid particles, but without significant effect on DGAT activity in the ER (62). The glycerol 3-phosphate (G-3-P) pathway is a de novo pathway involved in TAG synthesis in most tissues. This notion is supported by their similar subcellullar localization pattern (9) and the colocalization of DGAT2 gene with MGAT2 gene on the same region of human chromosome 11. Upon the treatment of oleate, DGAT2, but not DGAT1 and MGAT2, can also be detected in mitochondria-associated membranes and lipid droplets in addition to ER (64). The G-3-P pathway begins with the acylation of G-3-P by glycerol-3-phosphate acyltransferase (GPAT) with fatty acyl-CoA, producing lysophosphatidic acid (LPA), followed sequentially by further acylation by LPA acyltransferase (LPAAT) and dephosphorylation by phosphatidic acid (PA) phosphorylase (PAP) to yield diacylgycerol (DAG). Although MGAT3 enzyme exhibits strong DGAT activity, its catalytic properties are quite different from those of DGAT1. Furthermore, when DGAT1 is overexpressed in mouse liver via an adenoviral vector, the mice showed increased VLDL secretion and gonadal fat mass, whereas hepatic-specific DGAT2 overexpression increased liver TAG content but not VLDL secretion (74).
The 2 pathways share the final step in converting DAG into TAG, which is catalyzed by diacylglycerol acyltransferase (DGAT). Whereas MGAT3 is very sensitive to treatment with 1% 3[(3-cholamidopropyl)dimethylammonio]-propanesulfonate, DGAT1 activity is stimulated by its application, indicating that they possess different catalytic mechanisms.
DAG is also used as a substrate for the synthesis of phosphatidic choline (PC) and phosphatidic ethanolamine (PE).In the past few years, great strides have been made in the identification and characterization of the enzymes of these two pathways. Interestingly, MGAT3 activity is equally sensitive to detergent inactivation when either MAG or DAG is used as a substrate, suggesting that the DGAT and MGAT activities of the MGAT enzymes are inseparable (9). As a result of rapid progress in genomics, bioinformatics, and transgenic mouse models, much has been learned about the underlying mechanisms that regulate TAG synthesis.
Herbivores need to break down the tough cellulose cell wall of the plant to access the available energy. The use of bioinformatics bypasses the difficulties in the purification of these enzymes from primary tissues because most of the enzymes are intrinsic membrane proteins. Whereas excess TAG accumulation in adipose leads to obesity, ectopic storage of TAG in nonadipose tissues such as liver and skeletal muscle is associated with insulin resistance (45). Recent progress in the identification and characterization of the MGAT and DGAT enzymes along with the phenotypic characterizations of mice with altered expression of these genes have provided important insights into their dynamic roles in the regulation of energy homeostasis and other physiological functions.



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