Abstract
Monellin, a protein found in the berries of the West African plant Dioscoreophyllum cumminsii, is one of the most potently sweet compounds known. The native three-dimensional structure of monellin is required for sweetness, and this protein has been the subject of intense research in an attempt at understanding the structural basis for its taste activity. We have used structure-based site-directed mutagenesis to delineate the taste-active site(s) of monellin, and we present these results, along with similar work from M. Kohmura, Y. Ariyoshi and coworkers, in the light of the three-dimensional structure of this protein. The mutagenesis work suggests that at least four residues, located N-terminal to the alpha-helix, form part of a taste-active region of monellin. In addition, there is evidence that a second region, formed by residues in the fourth and fifth beta-strands, may also be contributing to monellin's activity.
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