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.
Keywords:
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