Matches in SemOpenAlex for { <https://semopenalex.org/work/W2138628181> ?p ?o ?g. }
- W2138628181 endingPage "10172" @default.
- W2138628181 startingPage "10160" @default.
- W2138628181 abstract "Baeyer–Villiger monooxygenases (BVMOs) have been used for decades as catalysts in stereoselective Baeyer–Villiger reactions, including oxidative kinetic resolution of racemic ketones and desymmetrization of prochiral substrates with high enantioselectivity. These complement catalytic BV processes based on chiral synthetic catalysts. However, as in any enzyme-catalyzed process, limitations exist due to the often observed narrow substrate scope and/or insufficient stereoselectivity. Recent protein engineering of BVMOs in the form of directed evolution and rational design have eliminated these traditional limitations, which is the subject of this Minireview. The main focus is on phenylacetone monooxygenase (PAMO); an unusually thermostable and robust BVMO, which has a very narrow substrate scope. Protein engineering of PAMO has provided a number of mutants that display relatively wide substrate scope, high stereoselectivity, and maintained thermostability." @default.
- W2138628181 created "2016-06-24" @default.
- W2138628181 creator A5019901372 @default.
- W2138628181 creator A5034787589 @default.
- W2138628181 creator A5050231254 @default.
- W2138628181 date "2012-07-16" @default.
- W2138628181 modified "2023-10-16" @default.
- W2138628181 title "Protein Engineering of Stereoselective Baeyer-Villiger Monooxygenases" @default.
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