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Papers In Press, published online ahead of print December 14, 2006
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Cellular and Molecular Physiology, Penn State School of Medicine, Hershey, PA 17033
Corresponding Author: yus11{at}psu.edu
MGAT3 is a member of monoacylglycerol acyltransferase (MGAT) family of enzymes that catalyze the synthesis of diacylglycerol (DAG) from monoacylglycerol (MAG), a committed step in dietary fat absorption. Although named after initial identification of its MGAT activity, MGAT3 shares higher sequence homology to DGAT2 than other MGAT enzymes, suggesting that MGAT3 may also possess significant DGAT activity. The present study compared the catalytic properties of MGAT3 with those of MGAT1 and MGAT2 enzymes using both MAG and DAG as substrates. Our results showed that in addition to the expected MGAT activity, the recombinant MGAT3 enzyme expressed in Sf-9 insect cells displayed a strong DGAT activity relative to that of MGAT1 and MGAT2 enzymes in the order of MGAT3 > MGAT1 >MGAT2. In contrast, none of the three MGAT enzymes recognized biotinylated acyl-CoA or MAG as a substrate. Although MGAT3 possesses full DGAT activity, it differs from DGAT1 in catalytic properties and subcellular localization. The MGAT3 activity was sensitive to inhibition by the presence of 1% CHAPS, whereas DGAT1 activity was stimulated by the detergent. Consistent with high sequence homology to DGAT2, the MGAT3 enzyme demonstrated a similar subcellular distribution pattern to that of DGAT2, but not DGAT1 when expressed in COS-7 cells. Our data suggest that MGAT3 functions as a novel TAG synthase that catalyzes efficiently the two consecutive acylation steps in TAG synthesis.
Revised on December 8, 2006
Accepted on December 13, 2006
Catalytic properties of MGAT3, a putative triacylgycerol synthase
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