Expanding the substrate scope of enzymes: combining mutations obtained by CASTing.
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Summary
A simple method is presented for further optimization of initial hits by combining the mutational changes obtained from two different libraries in the combinatorial active-site saturation test.
- Type
- article
- Published
- 2006-08-07
- Cited by
- 136
- References
- 105
- OpenAlex
- https://openalex.org/W16789057
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24019613
Keywords
Computer science
References
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- Mejora y evaluación de lipasas microbianas para la síntesis de biodiésel = Improvement and evaluation of microbial lipases for biodiesel synthesis
- Hydroxynitril-Lyasen für die Biotechnologie
- Semi-rational Directed Evolution of Monoamine Oxidase for Kinetic Resolution of rac-Mexiletine
- The role of aromatic residue W20 in the activity and enantioselectivity control of esterase BioH toward aryl substrate
- The development of novel biocatalysts for the asymmetric hydroamination of alkenes
- Expression of a lipase in prokaryote and eukaryote host systems allowing engineering
- Neue Zugänge zu enantioselektiven lipolytischen Enzymen durch fluoreszenzbasierte Durchmusterung kombinatorischer Bibliotheken
- New oxidoreductases for the synthesis of chiral building blocks
- Murine erythroid 5-aminolevulinate synthase: Adenosyl-binding site Lys221 modulates substrate binding and catalysis
- Recent advances in production and biotechnological applications of thermostable and alkaline bacterial lipases
- Extreme synergistic mutational effects in the directed evolution of a baeyer-villiger monooxygenase as catalyst for asymmetric sulfoxidation.
- Application of designed enzymes in organic synthesis.
- Directed evolution drives the next generation of biocatalysts.
- Laboratory evolution of stereoselective enzymes as a means to expand the toolbox of organic chemists
- Using site‐saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate‐dependent enzymes
- Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
- Steering directed protein evolution: strategies to manage combinatorial complexity of mutant libraries.
- Improved PCR method for the creation of saturation mutagenesis libraries in directed evolution: application to difficult-to-amplify templates
- Enzyme engineering for enantioselectivity: from trial-and-error to rational design?
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