Monooxygenase-catalyzed Baeyer-Villiger oxidations: CHMO versus CPMO

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DOIResolve DOI: http://doi.org/10.1016/S1381-1177(03)00036-5
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TypeArticle
Journal titleJournal of Catalysis
Volume22
Issue3-4
Pages211218; # of pages: 8
Subjectenv; Enzymes
AbstractCyclopentanone monooxygenase (CPMO) from Comamonas sp. NCIMB 9872 expressed in E. coli was evaluated as a potential new bioreagent for Baeyer-Villiger oxidations of 4-alkoxy- and halo-substituted cyclohexanones (10 examples). The results were compared with those obtained in oxidations catalyzed by an engineered E. coli strain expressing cyclohexanone monooxygenase (CHMO) from Acinetobacter sp. CPMO was found to have modest to good stereoselectivity and broader substrate acceptability than CHMO. The stereoselectivities of the two enzymes were generally opposite. It appears, therefore, that the two engineered strains can be useful and complementary reagents for enantioselective Baeyer-Villiger oxidations of certain prochiral ketones.
Publication date
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number45906
NPARC number3540119
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Record identifier4a7c146e-3819-4977-88db-8dceea2a332e
Record created2009-03-01
Record modified2016-05-09
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