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

Directed evolution of Anabaena variabilis phenylalanine ammonia-lyase (PAL) identifies mutants with enhanced activities.

Chemical communications (Cambridge, England) - 14 May 2020

Mays Zachary Js, Mohan Karishma, Trivedi Vikas D, Chappell Todd C, Nair Nikhil U

Abstract excerpt

There is broad interest in engineering phenylalanine ammonia-lyase (PAL) for its biocatalytic applications in industry and medicine. While site-specific mutagenesis has been employed to improve PAL stability or substrate specificity, combinatorial techniques are poorly explored. Here, we report development of a directed evolution technique to engineer PAL enzymes. Central to this approach is a high-throughput...

Read the complete abstract on PubMed

Topics

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

Share to Mutation
Share to Protein Engineering

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Open in PubMed Open full text

Identifiers

PMID: 32270162
DOI: 10.1039/d0cc00783h
PMCID: PMC7274816

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Directed evolution of Anabaena variabilis phenylalanine ammonia-lyase (PAL) identifies mutants with enhanced activities.PMID 32270162Read ↗

Directed evolution of <i>Anabaena variabilis</i> phenylalanine ammonia-lyase (PAL) identifies mutants with enhanced activitiesSemantic proximity Read ↗

Saturation Mutagenesis for Phenylalanine Ammonia Lyases of Enhanced Catalytic Properties.Semantic proximity Read ↗

Phenylalanine ammonia-lyases: combining protein engineering and natural diversity.Semantic proximity Read ↗

A silk-based platform to stabilize phenylalanine ammonia-lyase (PAL) for orally administered enzyme replacement therapySemantic proximity Read ↗

Engineering and kinetic stabilization of the therapeutic enzyme Anabeana variabilis phenylalanine ammonia lyase.Semantic proximity Read ↗

Improved bacterial recombineering by parallelized protein discoverySemantic proximity Read ↗

Improved bacterial recombineering by parallelized protein discovery.Semantic proximity Read ↗

Metabolic engineering of a genetic selection system with tunable stringency.Semantic proximity Read ↗

Enzyme engineering by targeted libraries.Semantic proximity Read ↗

Active site diversification of a non-canonical amino acid decarboxylase by merging substrate multiplexed screening with computationally guided recombination.Semantic proximity Read ↗

Mutational analysis of phenylalanine ammonia lyase to improve reactions rates for various substrates.Semantic proximity Read ↗

A high-throughput screen for the engineered production of β-lactam antibiotics.Semantic proximity Read ↗

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