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

Engineering of phenylacetaldehyde reductase for efficient substrate conversion in concentrated 2-propanol.

Applied and environmental microbiology - 1 Aug 2005

Makino Yoshihide, Inoue Kousuke, Dairi Tohru, Itoh Nobuya

Abstract excerpt

Phenylacetaldehyde reductase (PAR) is suitable for the conversion of various aryl ketones and 2-alkanones to corresponding chiral alcohols. 2-Propanol acts as a substrate solvent and hydrogen donor of coupled cofactor regeneration during the conversion of substrates catalyzed by PAR. To improve the conversion efficiency in high concentrations of substrate and 2-propanol, selection of a PAR mutant library and the...

Read the complete abstract on PubMed

Topics

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

Share to Alcohol Oxidoreductases
Share to Corynebacterium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Library

Share to Genetic Engineering

Share to Industrial Microbiology

Share to Molecular Sequence Data

Share to Sequence Analysis, DNA

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 16085867
DOI: 10.1128/AEM.71.8.4713-4720.2005
PMCID: PMC1183298

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

Engineering of phenylacetaldehyde reductase for efficient substrate conversion in concentrated 2-propanol.PMID 16085867Read ↗

Substrate expansion of Geotrichum candidum alcohol dehydrogenase towards diaryl ketones by mutation.Semantic proximity Read ↗

Directed evolution of Aspergillus oryzae lipase for the efficient resolution of (R,S)-ethyl-2-(4-hydroxyphenoxy) propanoate.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 ↗

Significant improvement of the enantioselectivity of a halohydrin dehalogenase for asymmetric epoxide ring opening reactions by protein engineering.Semantic proximity Read ↗

An efficient route to selective bio-oxidation catalysts: an iterative approach comprising modeling, diversification, and screening, based on CYP102A1.Semantic proximity Read ↗

Laboratory evolution of robust and enantioselective Baeyer-Villiger monooxygenases for asymmetric catalysis.Semantic proximity Read ↗

Efficient production of (R)-2-hydroxy-4-phenylbutyric acid by using a coupled reconstructed D-lactate dehydrogenase and formate dehydrogenase system.Semantic proximity Read ↗

Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer.Semantic proximity Read ↗

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

Rational design of a minimal and highly enriched CYP102A1 mutant library with improved regio-, stereo- and chemoselectivity.Semantic proximity Read ↗

Evolving P450pyr Monooxygenase for Regio- and Stereoselective Hydroxylations.Semantic proximity Read ↗

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

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