Laboratory evolution of stereoselective enzymes: a prolific source of catalysts for asymmetric reactions.
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Structure-function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymesMachine-Assisted Organic SynthesisComputer aided enzyme design and catalytic conceptsShedding light on protein folding, structural and functional dynamics by single molecule studiesHydroxynitrile Lyases with α/β-Hydrolase Fold: Two Enzymes with Almost Identical 3D Structures but Opposite Enantioselectivities and Different Reaction MechanismsAzurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding PocketEvolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atomKey Mutations Alter the Cytochrome P450 BM3 Conformational Landscape and Remove Inherent Substrate BiasAn artificial oxygenase built from scratch: substrate binding site identified using a docking approachResidues Controlling Facial Selectivity in an Alkene Reductase and Semirational Alterations to Create Stereocomplementary VariantsReshaping an enzyme binding pocket for enhanced and inverted stereoselectivity: use of smallest amino acid alphabets in directed evolutionTuning and Switching Enantioselectivity of Asymmetric Carboligation in an Enzyme through Mutational Analysis of a Single Hot SpotThe Generation and Exploitation of Protein Mutability Landscapes for Enzyme EngineeringDirected evolution of a pyruvate aldolase to recognize a long chain acyl substrateHighly regio- and enantioselective multiple oxy- and amino-functionalizations of alkenes by modular cascade biocatalysisCombining a Clostridial enzyme exhibiting unusual active site plasticity with a remarkably facile sigmatropic rearrangement: rapid, stereocontrolled entry into densely functionalized fluorinated phosphonates for chemical biologyComputational protein engineering: bridging the gap between rational design and laboratory evolution.Protein engineering: navigating between chance and reason.Directed evolution strategies for enantiocomplementary haloalkane dehalogenases: from chemical waste to enantiopure building blocks.One-bead-one-catalyst approach to aspartic acid-based oxidation catalyst discoveryRevisiting the lipase from Pseudomonas aeruginosa: directed evolution of substrate acceptance and enantioselectivity using iterative saturation mutagenesis.Recombinant silicateins as model biocatalysts in organosiloxane chemistry.Manipulating the expression rate and enantioselectivity of an epoxide hydrolase by using directed evolution.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.Combinatorial reshaping of the Candida antarctica lipase A substrate pocket for enantioselectivity using an extremely condensed library.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.Use of 'small but smart' libraries to enhance the enantioselectivity of an esterase from Bacillus stearothermophilus towards tetrahydrofuran-3-yl acetate.Substrate control in stereoselective lanthionine biosynthesis.Directed evolution by using iterative saturation mutagenesis based on multiresidue sites.Patch cloning method for multiple site-directed and saturation mutagenesis.Assessing directed evolution methods for the generation of biosynthetic enzymes with potential in drug biosynthesis.The "gate keeper" role of Trp222 determines the enantiopreference of diketoreductase toward 2-chloro-1-phenylethanone.SpeedyGenes: an improved gene synthesis method for the efficient production of error-corrected, synthetic protein libraries for directed evolution.Marine extremophiles: a source of hydrolases for biotechnological applications.Combinatorial library based engineering of Candida antarctica lipase A for enantioselective transacylation of sec-alcohols in organic solvent.Economical analysis of saturation mutagenesis experiments.Directed Evolution of Enzymes for Industrial Biocatalysis.Single mutations of ketoreductase ChKRED20 enhance the bioreductive production of (1S)-2-chloro-1-(3, 4-difluorophenyl) ethanol.
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Laboratory evolution of stereoselective enzymes: a prolific source of catalysts for asymmetric reactions.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 2011
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Laboratory evolution of stereo ...... ysts for asymmetric reactions.
@en
Laboratory evolution of stereo ...... ysts for asymmetric reactions.
@nl
type
label
Laboratory evolution of stereo ...... ysts for asymmetric reactions.
@en
Laboratory evolution of stereo ...... ysts for asymmetric reactions.
@nl
prefLabel
Laboratory evolution of stereo ...... ysts for asymmetric reactions.
@en
Laboratory evolution of stereo ...... ysts for asymmetric reactions.
@nl
P356
P1476
Laboratory evolution of stereo ...... ysts for asymmetric reactions.
@en
P2093
Manfred T Reetz
P2860
P304
P356
10.1002/ANIE.201000826
P407
P577
2011-01-01T00:00:00Z