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Deconstructing the DGAT1 enzyme: Binding sites and substrate interactions
Authors:José LS Lopes  Thatyane M Nobre  Eduardo M Cilli  Leila M Beltramini  Ana PU Araújo  BA Wallace
Institution:1. Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, Brazil;2. Institute of Structural and Molecular Biology, Birkbeck College, University of London, UK;3. Instituto de Química, Universidade Estadual Paulista, Araraquara, Brazil
Abstract:Diacylglycerol acyltransferase 1 (DGAT1) is a microsomal membrane enzyme responsible for the final step in the synthesis of triacylglycerides. Although DGATs from a wide range of organisms have nearly identical sequences, there is little structural information available for these enzymes. The substrate binding sites of DGAT1 are predicted to be in its large luminal extramembranous loop and to include common motifs with acyl-CoA cholesterol acyltransferase enzymes and the diacylglycerol binding domain found in protein kinases.
Keywords:Diacylglycerol acyltransferase  Enzyme catalysis  Peptide&ndash  lipid interaction  Langmuir monolayer  Synchrotron radiation circular dichroism (SRCD) spectroscopy  Triglyceride synthesis
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