Cloning of DGAT2, a Second Mammalian Diacylglycerol Acyltransferase, and Related Family Members*

By S. Cases, S. Stone, P. Zhou, E. Yen, B. Tow, K. Lardizabal, T. Voelker, Robert V Farese. Journal of Biological Chemistry, 2001

789 citations recorded by the source corpus.

Studies involving the cloning and disruption of the gene for acyl-CoA:diacylglycerol acyltransferase (DGAT) have shown that alternative mechanisms exist for triglyceride synthesis. In this study, we cloned and characterized a second mammalian DGAT, DGAT2, which was identified by its homology to a DGAT in the fungus Mortierella rammaniana. DGAT2 is a member of a gene family that has no homology with DGAT1 and includes several mouse and human homologues that are candidates for additional DGAT genes. The expression of DGAT2 in insect cells stimulated triglyceride synthesis 6-fold in assays with cellular membranes, and DGAT2 activity was dependent on the presence of fatty acyl-CoA and diacylglycerol, indicating that this protein is a DGAT. Activity was not observed for acyl acceptors other than diacylglycerol. DGAT2 activity was inhibited by a high concentration (100 mm) of MgCl2 in anin vitro assay, a characteristic that distinguishes DGAT2 from DGAT1. DGAT2 is expressed in many tissues with high expression levels in the liver and white adipose tissue, suggesting that it may play a significant role in mammalian triglyceride metabolism.

Subfields: Biochemistry, Genetics, Plant Science

View Paper: https://www.semanticscholar.org/paper/360890ee0e0d0db7940b01e68d775e00c45f9c45

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In Biochemistry

1. Ruth Welti
2. Douglas P Lee
3. R. Coleman
4. M. Alves‐Bezerra
5. David E Cohen

In Plant Science

1. Y. Li-Beisson
2. Ruth Welti
3. I. Graham
4. T. Vogt

Citations in the corpus

• Triglyceride metabolism in the liver (2017, neutral): “DGAT2 exhibits in vitro specificity for the use of DG molecules as substrates (42).”
• Plant triacylglycerols as feedstocks for the production of biofuels. (2008, background): “Two classes of DGAT enzymes have been isolated (Cases et al., 1998, 2001; Lardizabal et al., 2001), and orthologs have been identified in numerous plant species.”
• Enzymes of triacylglycerol synthesis and their regulation. (2004, methodology): “The proteins from mouse and human are predicted to be 388 and 387 aa, respectively, and to have two predicted transmembrane domains [134].”
• Acyl-Lipid Metabolism (2013, background): “Pioneering work has identified two different classes of DGAT enzymes (Cases et al., 1998, 2001; Lardizabal et al., 2001), orthologs of which have been isolated in various plants.”