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[[Image:Image_1.PNG|400 px|left|thumb|Figure 1. This image shows the location of the DGAT protein within the Endoplasmic Reticulum Membrane]]
[[Image:Image_1.PNG|400 px|left|thumb|Figure 1. This image shows the location of the DGAT protein within the Endoplasmic Reticulum Membrane]]
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DGAT, or Diacylglycerol Transferase, makes [https://en.wikipedia.org/wiki/Triglyceride triglycerides] from a [https://en.wikipedia.org/wiki/Diglyceride diglyceride] in plasma. DGAT is a polytopic endoplasmic reticulum membrane protein embedded within the membrane of the ER. DGAT is highly expressed in epithelial cells of the small intenstine. It can also be found in the liver, where it helps synthesize fats for storage, and the female mammary glands, where it produces fat in the milk.
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DGAT, or Diacylglycerol Acyltransferase is a polytopic endoplasmic reticulum membrane protein embedded within the membrane of the [https://en.wikipedia.org/wiki/Endoplasmic_reticulum ER]. DGAT is highly expressed in epithelial cells of the small intenstine of homo sapiens. It can also be found in the liver, where it helps synthesize fats for storage, and the female mammary glands, where it produces fat in the milk.
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DGAT was originally discovered by its homology to [https://en.wikipedia.org/wiki/Sterol_O-acyltransferase Acyl-CoA cholesterol acyltransferases (ACAT) 1 and 2]. The structure, catalytic mechanism of diacylglycerol acyltransferase, and how DGAT interacts with CoA was discovered using a [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy Cryo-EM]. The Cryo-EM map revealed that DGAT forms a dimer, with each subunit containing nine transmembrane helices. The N and C terminals of each helice are located on the cytosolic and luminal sides of the endoplasmic reticulum membrane respectively.
==Function==
==Function==
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DGAT makes [https://en.wikipedia.org/wiki/Triglyceride triglycerides] from a [https://en.wikipedia.org/wiki/Diglyceride diglyceride] in plasma. In order to do this, DGAT uses two substrates: a fatty acyl-CoA and a diacylglycerol substrate. The basic mechanism consists of a lone pair on a hydroxyl group of glycerol attacking the carbon of the thioester bond of CoA. This results in the breakage of the thioester bond, and the attached acyl group attaches to the glycerol, creating a triglyceride.
==Structure==
==Structure==

Revision as of 22:19, 17 March 2021

DGAT Human

Caption for this structure

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References

[3]

[4]

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. Wang L, Qian H, Nian Y, Han Y, Ren Z, Zhang H, Hu L, Prasad BVV, Laganowsky A, Yan N, Zhou M. Structure and mechanism of human diacylglycerol O-acyltransferase 1. Nature. 2020 May;581(7808):329-332. doi: 10.1038/s41586-020-2280-2. Epub 2020 May, 13. PMID:32433610 doi:http://dx.doi.org/10.1038/s41586-020-2280-2
  4. Sui X, Wang K, Gluchowski NL, Elliott SD, Liao M, Walther TC, Farese RV Jr. Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme. Nature. 2020 May;581(7808):323-328. doi: 10.1038/s41586-020-2289-6. Epub 2020 May, 13. PMID:32433611 doi:http://dx.doi.org/10.1038/s41586-020-2289-6

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