| Δ3-Δ2-Enoyl-CoA isomerase from the yeast Saccharomyces cerevisiae: Molecular and structural characterization | ||
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The complete sequencing of the genome of baker’s yeast, S. cerevisiae, revealed that it has three genes encoding possible members of the hydratase/isomerase superfamily. The initial goal of the study was to start identifying the functions of these gene products and, especially, to search for the Δ3-Δ2-enoyl-CoA isomerase or the Δ3,5–Δ2,4-dienoyl-CoA isomerase of S. cerevisiae. To start the search, the first aim was:
To subclone the yeast gene YLR284c into a bacterial expression vector, to overexpress it and to determine the enzymatic activity of the gene product.
Once the gene YLR284c had been found to encode for a Δ3-Δ2-enoyl-CoA isomerase, more specific aims for the study were set:
To purify and characterize the recombinant yeast Δ3-Δ2-enoyl-CoA isomerase.
To determine the crystal structure of the Δ3-Δ2-enoyl-CoA isomerase in the absence and presence of an active site ligand.
To compare the Δ3-Δ2-enoyl-CoA isomerase structures with each other and with the other known structures belonging to the hydratase/isomerase superfamily.