Directed evolution of enantioselective enzymes: iterative cycles of CASTing for probing protein-sequence space
about
To get what we aim for--progress in diversity generation methodsA 5000-Fold Increase in the Specificity of a Bacterial Phosphotriesterase for Malathion through Combinatorial Active Site MutagenesisThe Generation and Exploitation of Protein Mutability Landscapes for Enzyme EngineeringFumarate Production by Torulopsis glabrata: Engineering Heterologous Fumarase Expression and Improving Acid ToleranceBiocatalyst development by directed evolutionOmniChange: the sequence independent method for simultaneous site-saturation of five codonsHotSpot Wizard 2.0: automated design of site-specific mutations and smart libraries in protein engineering.Enhancement of the stability of a prolipase from Rhizopus oryzae toward aldehydes by saturation mutagenesis.Steering directed protein evolution: strategies to manage combinatorial complexity of mutant libraries.Induced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase.Revisiting the lipase from Pseudomonas aeruginosa: directed evolution of substrate acceptance and enantioselectivity using iterative saturation mutagenesis.An efficient route to selective bio-oxidation catalysts: an iterative approach comprising modeling, diversification, and screening, based on CYP102A1.Enhancing the thermal robustness of an enzyme by directed evolution: least favorable starting points and inferior mutants can map superior evolutionary pathways.Engineering of biocatalysts - from evolution to creation.Enhancing the efficiency of directed evolution in focused enzyme libraries by the adaptive substituent reordering algorithm.Many pathways in laboratory evolution can lead to improved enzymes: how to escape from local minima.Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB.Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis.Expanding the library and substrate diversity of the pyrrolysyl-tRNA synthetase to incorporate unnatural amino acids containing conjugated rings.Directed evolution by using iterative saturation mutagenesis based on multiresidue sites.Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution.Computational tools for rational protein engineering of aldolases.A smart library of epoxide hydrolase variants and the top hits for synthesis of (S)-β-blocker precursors.Exploring the enantioselective mechanism of halohydrin dehalogenase from Agrobacterium radiobacter AD1 by iterative saturation mutagenesisSpeedyGenes: an improved gene synthesis method for the efficient production of error-corrected, synthetic protein libraries for directed evolution.Amino ester hydrolase from Xanthomonas campestris pv. campestris, ATCC 33913 for enzymatic synthesis of ampicillinMutations Closer to the Active Site Improve the Promiscuous Aldolase Activity of 4-Oxalocrotonate Tautomerase More Effectively than Distant Mutations.Enzyme Tunnels and Gates As Relevant Targets in Drug Design.A Simple Combinatorial Codon Mutagenesis Method for Targeted Protein EngineeringIterative combinatorial mutagenesis as an effective strategy for generation of deacetoxycephalosporin C synthase with improved activity toward penicillin G.Altering coenzyme specificity of Pichia stipitis xylose reductase by the semi-rational approach CASTing.Directed enzyme evolution: climbing fitness peaks one amino acid at a time.Stepwise acquisition of pyrimethamine resistance in the malaria parasiteEnzyme (re)design: lessons from natural evolution and computation.Bioinspired catalyst design and artificial metalloenzymes.Protein engineering of α/β-hydrolase fold enzymes.The importance of green chemistry in process research and development.Artificial metalloenzymes as catalysts in stereoselective Diels-Alder reactions.Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes.Recent advances in rational approaches for enzyme engineering.
P2860
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P2860
Directed evolution of enantioselective enzymes: iterative cycles of CASTing for probing protein-sequence space
description
wetenschappelijk artikel
@nl
наукова стаття, опублікована в лютому 2006
@uk
name
Directed evolution of enantios ...... probing protein-sequence space
@en
Directed evolution of enantios ...... probing protein-sequence space
@nl
type
label
Directed evolution of enantios ...... probing protein-sequence space
@en
Directed evolution of enantios ...... probing protein-sequence space
@nl
prefLabel
Directed evolution of enantios ...... probing protein-sequence space
@en
Directed evolution of enantios ...... probing protein-sequence space
@nl
P2093
P356
P1476
Directed evolution of enantios ...... probing protein-sequence space
@en
P2093
Li-Wen Wang
Manfred T Reetz
Marco Bocola
P304
P356
10.1002/ANIE.200502746
P407
P577
2006-02-13T00:00:00Z