| Δ3-Δ2-Enoyl-CoA isomerase from the yeast Saccharomyces cerevisiae: Molecular and structural characterization | ||
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Future studies on the yeast Δ3-Δ2-enoyl-CoA isomerase will focus on crystallographic binding studies with substrates, both with cis- and trans-3 double bonds, and substrate analogues of variable chain length and with better resolution, in order to more accurately determine the catalytic mechanism of the yeast enoyl-CoA isomerase and to elucidate the role of the empty apolar cavity in the binding of longer fatty acyl chains. Also, the substrate chain length specificity will be studied by enzyme assays. In addition, structural studies on the human mitochondrial Δ3-Δ2-enoyl-CoA isomerase and the rat MFE-1 are ongoing in our laboratory. These enzymes also belong to the hydratase/isomerase superfamily but have different catalytic residues for the enoyl-CoA isomerase reaction compared to the yeast enoyl-CoA isomerase and also occur in different oligomeric forms, the mitochondrial isomerase being a trimer and the MFE-1 a monomer. The crystal structures of these enzymes are expected to give invaluable information about the importance of different catalytic residues at the active site architecture.