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4 results on '"Manfred T. Reetz"'

1. A genetic selection system for evolving enantioselectivity of enzymes.

Author

Manfred T. Reetz, Horst Höbenreich, Pankaj Soni, and Layla Fernández

Subjects
*ENZYMES, *ORGANIC compounds, *ENANTIOSELECTIVE catalysis, *LIPASES, *HYDROLYSIS, *CHEMICAL kinetics
Abstract

As an alternative to screening in the directed evolution of enantioselective enzymes, a selection system has been implemented for a lipase-catalyzed hydrolytic kinetic resolution of a chiral ester. [ABSTRACT FROM AUTHOR]

Published
2008
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2. Greatly reduced amino acid alphabets in directed evolution: making the right choice for saturation mutagenesis at homologous enzyme positions.

Author

Manfred T. Reetz and Sheng Wu

Subjects
*AMINO acids, *MUTAGENESIS, *RADIOGENETICS, *ENANTIOSELECTIVE catalysis, *MONOOXYGENASES, *CHEMICAL reactions
Abstract

Enantioselective mutants of the thermally robust phenyl acetone monooxygenase (PAMO) as catalysts in Baeyer–Villiger reactions have been evolved by utilizing saturation mutagenesis in which drastically reduced amino acid alphabets are employed at homologous enzyme positions. [ABSTRACT FROM AUTHOR]

Published
2008
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3. Deazaflavins as mediators in light-driven cytochrome P450 catalyzed hydroxylationsElectronic supplementary information (ESI) available: Experimental details and additional control experiments. See DOI: 10.1039/b913863c.

Author

Felipe E. ZillyThese authors contributed equally to this paper., Andreas Taglieber, Frank Schulz, Frank Hollmann, and Manfred T. Reetz

Subjects
*FLAVINS, *CYTOCHROME P-450, *ADENINE nucleotides, *HYDROXYLATION, *ENZYME activation
Abstract

A light-driven deazaflavin-dependent direct enzyme regeneration system has been developed for a P450-BM3 catalyzed CH-activating hydroxylation, thereby avoiding the need for the expensive NADPH cofactor. [ABSTRACT FROM AUTHOR]

Published
2009
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4. Directed evolution and axial chirality: optimization of the enantioselectivity of Pseudomonas aeruginosa lipase towards the kinetic resolution of a racemic allene.

Author

José Daniel Carballeira, Patrik Krumlinde, Marco Bocola, Andreas Vogel, Manfred T. Reetz, and Jan-E. Bäckvall

Subjects
*CHIRALITY, *PSEUDOMONAS aeruginosa, *LIPASES, *ALLENE
Abstract

Directed evolution of Pseudomonas aeruginosa lipase by the use of combinatorial active site saturation test (CAST) criteria provided a highly enantioselective mutant (Leu162Phe) for kinetic resolution of an axially chiral allene, p-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate (E = 111); the high enantioselectivity of the Leu162Phe mutant was rationalized by π–π stacking. [ABSTRACT FROM AUTHOR]

Published
2007
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