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Monooxygenase‐Mediated Baeyer−Villiger Oxidations
Author(s) -
Mihovilovic Marko D.,
Müller Bernhard,
Stanetty Peter
Publication year - 2002
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/1099-0690(200211)2002:22<3711::aid-ejoc3711>3.0.co;2-5
Subject(s) - chemistry , monooxygenase , flavin group , biocatalysis , natural product , cofactor , substrate (aquarium) , enzyme , stereochemistry , synthetic biology , organic chemistry , combinatorial chemistry , reaction mechanism , catalysis , cytochrome p450 , computational biology , oceanography , biology , geology
Enzyme‐mediated Baeyer−Villiger oxidations offer a “green chemistry” approach for the production of chiral lactones. Several organisms have been found to catalyze this reaction in the course of their metabolic pathways. A number of flavin‐dependent monooxygenases have been characterized, and acceptance of a multitude of non‐natural substrates has been found. Such biocatalysts are used in synthetic chemistry either as isolated enzymes in combination with appropriate cofactor recycling systems or as living whole cells, in native or recombinant form, for the production of valuable intermediates. This review gives an overview of the most widely utilized enzymes and the corresponding substrate profiles, together with applications in natural product and bioactive compound synthesis. (© Wiley‐VCH Verlag GmbH, 69451 Weinheim, Germany, 2002)