Enancjoselektywna enzymatyczna desymetryzacja katalizowana oksydoreduktazami. Reakcje utleniania. Część 1
Journal Title: Wiadomości Chemiczne - Year 2015, Vol 69, Issue 1
Abstract
The main advantage of biotransformation involving enzymes, compared to chemical processes, is a highly selective formation of products with precise configuration. Herein we describe enzymes participating in the oxidation processes, especially dehydrogenases and monooxygenases. Dehydrogenases are not only able to catalyze the enantioselective reduction of prochiral ketones, but they can also desymmetrize meso and prochiral diols through the enantioselective oxidation. As a result of this processes, optically active hydroxyketones, hydroxycarboxylic acids, and their derivatives are obtained. Cytochrome P450 monooxygenases (CYPs) constitute a family of heme-containing enzymes which exhibits a variety of catalytic activities. They catalyze different reactions, such as hydroxylation, epoxidation, oxidative deamination, or N- and (S)-oxidation. In the oxidation reaction with monooxygenases, the whole cells are commonly used as catalysts. The use of monooxygenases in the oxidation reaction of prochiral alkanes provides the optically active alcohols. It is very significant that these transformations are still difficult to carry out by chemical methods. Baeyer-Villiger monooxygenases (BVMO EC 1.14.13.X) effectively catalyze the nucleophilic and electrophilic oxidation reactions of various functional groups. BVMO are highly regio- and stereoselective enzymes, and their catalytic potential is used in the synthesis of optically pure lactones and esters.
Authors and Affiliations
Aleksandra Karczmarska-Wódzka, Renata Kołodziejska, Agnieszka Tafelska-Kaczmarek, Marcin Wróblewski, Beata Augustyńska
Keywords
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