Enzymes are effective targets for therapy, research, and synthesis, as well as magnificent tools for natural product modification. In the development of cancer therapies, rebeccamycin and granulatimides serve as starting point for therapeutic inhibitor design due to their ability to inhibit the enzymes, respectively topoisomerase I and checkpoint kinase I, which contribute to the control of the cell cycle. The design and synthetic progress of hybrid products is reported herein.
In the study of cell-surface oligosaccharide function, glycosidase inhibitors have assisted in the understanding of glycan processing and recognition. Inactivators of glycosidases have also been utilized in the treatment of diabetes, flu and HIV. The design and synthesis of a novel glycosidase inhibitor is discussed.
Glycosyl transferases have proven to be useful instruments in the chemoenzymatic synthesis of glycopeptides and glycoproteins, contributing to the study of their structure and functional relationships. Efforts to use PNGase for glycopeptide synthesis and progress toward the determination of peptide sequence specificity of PglL are detailed.
Finally, the enzyme transglutaminase which has been employed for improved quality of meats and other foods is investigated for its potential use in the enhancement of the properties of soy protein toward the production of valuable end products.