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

Efficient production of enantiomerically pure D-phenyllactate from phenylpyruvate by structure-guided design of an engineered D-lactate dehydrogenase.

Applied microbiology and biotechnology - 1 Sept 2016

Wang Min, Zhu Lingfeng, Xu Xiaoling, Wang Limin, Yin Ruochun, Yu Bo

Abstract excerpt

3-Phenyllactic acid (PLA) is an antimicrobial compound with broad-spectrum activity against bacteria and fungi that could be widely used in the food industry and livestock feeds. Notably, D-PLA exhibits higher antibacterial activity, which gains more attention than L-PLA. In this report, the D-lactate dehydrogenase DLDH744 from Sporolactobacillus inulinus CASD was engineered to increase the enzymatic activities...

Read the complete abstract on PubMed

Topics

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

Share to Anti-Bacterial Agents
Share to Biotransformation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Escherichia coli

Share to Lactates

Share to Mutation

Share to Stereoisomerism

Source

Identifiers

PMID: 27020295
DOI: 10.1007/s00253-016-7456-1

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Efficient production of enantiomerically pure D-phenyllactate from phenylpyruvate by structure-guided design of an engineered D-lactate dehydrogenase.PMID 27020295Read ↗

Highly stereoselective biosynthesis of (R)-α-hydroxy carboxylic acids through rationally re-designed mutation of D-lactate dehydrogenase.Semantic proximity Read ↗

Directed modification of l-LcLDH1, an l-lactate dehydrogenase from Lactobacillus casei, to improve its specific activity and catalytic efficiency towards phenylpyruvic acid.Semantic proximity Read ↗

Substrate specificity engineering of leucine dehydrogenase for efficient synthesis of aromatic L-homophenylalanine.Semantic proximity Read ↗

Semi-rational design of L-amino acid deaminase for production of pyruvate and D-alanine by Escherichia coli whole-cell biocatalyst.Semantic proximity Read ↗

Metabolomic and proteomic analysis of D-lactate-producing Lactobacillus delbrueckii under various fermentation conditions.Semantic proximity Read ↗

Structure-based modification of D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589 for depsipeptide synthesis.Semantic proximity Read ↗

Genetic engineering of Escherichia coli to improve L-phenylalanine production.Semantic proximity Read ↗

Characterization of the Pro101Gln mutation that enhances the catalytic performance of T. indicus NADH-dependent d-lactate dehydrogenase.Semantic proximity Read ↗

Evolution of D-lactate dehydrogenase activity from glycerol dehydrogenase and its utility for D-lactate production from lignocellulose.Semantic proximity Read ↗

Characterization and site-directed mutation of a novel aldo-keto reductase from Lodderomyces elongisporus NRRL YB-4239 with high production rate of ethyl (R)-4-chloro-3-hydroxybutanoate.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 ↗

Streptomyces virginiae PPDC Is a New Type of Phenylpyruvate Decarboxylase Composed of Two Subunits.Semantic proximity Read ↗

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