The Enzymes in Synthesis of Chiral Bioactive Compounds

The administration of chiral compounds in an enantiomerically pure form, instead of racemic mixtures, become an important issue especially in the pharmaceutical and agrochemical industries due to the well established correlation between the biological activity and stereochemistry. Pure enantiomers could be formed by the asymmetric synthesis and /or the resolution of racemates. This could be achieved by the use of enzymes as chiral catalysts. The advantages of enzymes are their high stereo- (chiral), regio- (positional) and chemo- (functional group specific) selectivity. This selectivity offers several benefits like high catalytic efficiency, preservation of asymmetric centres, single step transformations, easier separation, mild operating conditions and fewer environmental problems. The organic reactions that are catalyzed by enzymes to give chiral bioactive organic compounds include, for example, reduction (e.g. by dehydrogenases, ketoreductases), oxidation (e.g. by monooxygenases, dioxygenases), hydrolytic (e.g. by lipases, esterases) reactions.

Autorentext

Prof. Dr. Nesrin Mahmoud Morsy is an associate professor at an Organometallic and Organometalloid Chemistry Department. Dr. Eman Hamed Imam Ismael and Prof.Dr. Hisham Abdallah A. Yosef are respectively a researcher and professor at an Organometallic and Organometalloid Chemistry Department, Industrial Chemistry Division, National Research Centre.