Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Many pathways in laboratory evolution can lead to improved enzymes: how to escape from local minima.

Chembiochem : a European journal of chemical biology - 7 May 2012

Gumulya Yosephine, Sanchis Joaquin, Reetz Manfred T

Abstract excerpt

Directed evolution is a method to tune the properties of enzymes for use in organic chemistry and biotechnology, to study enzyme mechanisms, and to shed light on darwinian evolution in nature. In order to enhance its efficacy, iterative saturation mutagenesis (ISM) was implemented. This involves: 1) randomized mutation of appropriate sites of one or more residues; 2) screening of the initial mutant libraries for...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Directed Molecular Evolution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzymes

Share to Gene Library

Share to Models, Molecular

Share to Mutagenesis

Share to Protein Engineering

Share to Stereoisomerism

Source

Identifiers

PMID: 22522601
DOI: 10.1002/cbic.201100784

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Many pathways in laboratory evolution can lead to improved enzymes: how to escape from local minima.PMID 22522601Read ↗

Constructing and analyzing the fitness landscape of an experimental evolutionary process.Semantic proximity Read ↗

Directed evolution of an enantioselective epoxide hydrolase: uncovering the source of enantioselectivity at each evolutionary stage.Semantic proximity Read ↗

Manipulating the expression rate and enantioselectivity of an epoxide hydrolase by using directed evolution.Semantic proximity Read ↗

Directed enzyme evolution: beyond the low-hanging fruit.Semantic proximity Read ↗

Dynamics and constraints of enzyme evolution.Semantic proximity Read ↗

Enhancing the efficiency of directed evolution in focused enzyme libraries by the adaptive substituent reordering algorithm.Semantic proximity Read ↗

Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes.Semantic proximity Read ↗

Methods for enzyme library creation: Which one will you choose?: A guide for novices and experts to introduce genetic diversity.Semantic proximity Read ↗

Manipulating the stereoselectivity of limonene epoxide hydrolase by directed evolution based on iterative saturation mutagenesis.Semantic proximity Read ↗

The evolving art of creating genetic diversity: From directed evolution to synthetic biology.Semantic proximity Read ↗

Controlling the selectivity and stability of proteins by new strategies in directed evolution: the case of organocatalytic enzymes.Semantic proximity Read ↗

Strategy and success for the directed evolution of enzymes.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.