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Changing the enantioselectivity of enzymes by directed evolution
article published in 2004
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scholarly article
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title
Changing the enantioselectivity of enzymes by directed evolution
(English)
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main subject
enantioselectivity
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inferred from title
author
Manfred T. Reetz
series ordinal
1
object named as
Manfred T Reetz
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language of work or name
English
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publication date
2004
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published in
Methods in Enzymology
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volume
388
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page(s)
238-56
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cites work
Lipases as practical biocatalysts
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Directed Evolution and Biocatalysis
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Combinatorial and computational challenges for biocatalyst design
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Enantioselective enzymes for organic synthesis created by directed evolution
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New methods for the high-throughput screening of enantioselective catalysts and biocatalysts
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Directed evolution of an enantioselective lipase
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Improved method for PCR-mediated site-directed mutagenesis
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Directed Evolution of an Enantioselective Enzyme through Combinatorial Multiple-Cassette Mutagenesis
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Crystal structure of pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases
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Network of coupled promoting motions in enzyme catalysis
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Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenylbutyrate
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Improved enantioselectivity of a lipase by rational protein engineering.
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Learning from directed evolution: theoretical investigations into cooperative mutations in lipase enantioselectivity
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A High-Throughput-Screening Method for the Identification of Active and Enantioselective Hydrolases
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High-throughput screening of enantioselective catalysts by immunoassay
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Measurement of Enantiomeric Excess by Kinetic Resolution and Mass Spectrometry
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Creation of a productive, highly enantioselective nitrilase through gene site saturation mutagenesis (GSSM).
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Reaction microarrays: a method for rapidly determining the enantiomeric excess of thousands of samples.
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Identifiers
DOI
10.1016/S0076-6879(04)88021-2
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PubMed publication ID
15289076
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