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

Improvement of the activity of arylmalonate decarboxylase by random mutagenesis.

Applied microbiology and biotechnology - 1 Dec 2006

Terao Y, Miyamoto K, Ohta H

Abstract excerpt

Arylmalonate decarboxylase (EC 4.1.1.76) catalyzes enantioselective decarboxylation of alpha-aryl-alpha-methylmalonates to give optically pure alpha-arylpropionates. Recently, we have succeeded in creating a double mutant enzyme that gave opposite enantionmer as the product. Unfortunately, howeve...

Read the complete abstract on PubMed

Topics

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

Share to Alcaligenes
Share to Carboxy-Lyases
Share to Directed Molecular Evolution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis

Share to Protein Engineering

Share to Stereoisomerism

Share to Substrate Specificity

Share to Transformation, Bacterial

Source

Identifiers

PMID: 16865343
DOI: 10.1007/s00253-006-0518-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16865343-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Improvement of the activity of arylmalonate decarboxylase by random mutagenesis.PMID 16865343Read ↗

Dramatically improved catalytic activity of an artificial (S)-selective arylmalonate decarboxylase by structure-guided directed evolution.Semantic proximity Read ↗

Engineered hydrophobic pocket of (S)-selective arylmalonate decarboxylase variant by simultaneous saturation mutagenesis to improve catalytic performance.Semantic proximity Read ↗

[Increasing activity of a monoamine oxidase by random mutation].Semantic proximity Read ↗

Increasing the synthetic performance of penicillin acylase PAS2 by structure-inspired semi-random mutagenesis.Semantic proximity Read ↗

Directed evolution: selecting today's biocatalysts.Semantic proximity Read ↗

Creation of (R)-Amine Transaminase Activity within an α-Amino Acid Transaminase Scaffold.Semantic proximity Read ↗

Construction of a high-efficiency GjCCD4a mutant and its application for de novo biosynthesis of five crocins in Escherichia coli.Semantic proximity Read ↗

Rapid evolution of novel traits in microorganisms.Semantic proximity Read ↗

Enzyme modification using mutation site prediction method for enhancing the regioselectivity of substrate reaction sites.Semantic proximity Read ↗

Inverting the enantioselectivity of P450pyr monooxygenase by directed evolution.Semantic proximity Read ↗

A new type of class I bacterial 5-enopyruvylshikimate-3-phosphate synthase mutants with enhanced tolerance to glyphosate.Semantic proximity Read ↗

Enhancement of the catalytic activity of ferulic acid decarboxylase from Enterobacter sp. Px6-4 through random and site-directed mutagenesis.Semantic proximity Read ↗

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