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  Protein Engineering of Stereoselective Baeyer–Villiger Monooxygenases

Zhang, Z.-G., Parra, L. P., & Reetz, M. T. (2012). Protein Engineering of Stereoselective Baeyer–Villiger Monooxygenases. Chemistry-a European Journal, 18, 10160-10172. doi:10.1002/chem.201202163.

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 Urheber:
Zhang, Zhi-Gang1, 2, Autor           
Parra, Loreto P.1, 2, Autor           
Reetz, Manfred T.1, 2, Autor           
Affiliations:
1Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, DE, ou_1445588              
2Fachbereich Chemie, Philipps-Universität Marburgstitut für Kohlenforschung, Max Planck Society, Hans-Meerwein-Str., 35032 Marburg, DE, ou_1445588              

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Schlagwörter: Baeyer–Villiger monooxygenses chirality directed evolution enzyme catalysis; protein engineering stereoselectivity
 Zusammenfassung: 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.

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Sprache(n): eng - English
 Datum: 2012-07-16
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1002/chem.201202163
 Art des Abschluß: -

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Titel: Chemistry-a European Journal
  Andere : Chem.-Eur. J.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 18 Artikelnummer: - Start- / Endseite: 10160 - 10172 Identifikator: ISSN: 0947-6539
CoNE: https://pure.mpg.de/cone/journals/resource/954926979058