ArticleScientific reports2019
The production of L- and D-phenylalanines using engineered phenylalanine ammonia lyases from Petroselinum crispum.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- Estimation of Phenylalanine Ammonia-Lyase Activity for Assessing Resistance of Muskmelon Against Fusarium oxysporum f. sp. melonis Infection.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Switching Enantioselectivity in Phenylalanine Ammonia Lyase for the Synthesis of Electron-Deficient Aromatic d-Amino Acids.Angewandte Chemie (International ed. in English) · 2025Article
- Engineered Biocatalysts for the Asymmetric Synthesis of d-Phenylalanines.ACS catalysis · 2025Review
- Direct asymmetric synthesis of β-branched aromatic α-amino acids using engineered phenylalanine ammonia lyases.Nature communications · 2024Article
- Towards a general approach for tailoring the hydrophobic binding site of phenylalanine ammonia-lyases.Scientific reports · 2022Article
- Discovery of Novel Tyrosine Ammonia Lyases for the Enzymatic Synthesis of p-Coumaric Acid.Chembiochem : a European journal of chemical biology · 2022Article
- Population distributions of single-cell adhesion parameters during the cell cycle from high-throughput robotic fluidic force microscopy.Scientific reports · 2022Article
- Robust, site-specifically immobilized phenylalanine ammonia-lyases for the enantioselective ammonia addition of cinnamic acids.Catalysis science & technology · 2021Article
- Identification and Characterization of an Efficient Phenylalanine Ammonia-Lyase from Photorhabdus luminescens.Applied biochemistry and biotechnology · 2021Article
- Study of the l-Phenylalanine Ammonia-Lyase Penetration Kinetics and the Efficacy of Phenylalanine Catabolism Correction Using In Vitro Model Systems.Pharmaceutics · 2021Article
- Fluorescent enzyme-coupled activity assay for phenylalanine ammonia-lyases.Scientific reports · 2020Article
- Saturation Mutagenesis for Phenylalanine Ammonia Lyases of Enhanced Catalytic Properties.Biomolecules · 2020Article
- Advances in Enzymatic Synthesis of D-Amino Acids.International journal of molecular sciences · 2020Review
- Overview on Multienzymatic Cascades for the Production of Non-canonical α-Amino Acids.Frontiers in bioengineering and biotechnology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biocatalytic synthesis of L- and D-phenylalanine analogues of high synthetic value have been developed using as biocatalysts mutant variants of phenylalanine ammonia lyase from Petroselinum crispum (PcPAL), specifically tailored towards mono-substituted phenylalanine and cinnamic acid substrates. The catalytic performance of the engineered PcPAL variants was optimized within the ammonia elimination and ammonia addition reactions, focusing on the effect of substrate concentration, biocatalyst:substrate ratio, reaction buffer and reaction time, on the conversion and enantiomeric excess values. The optimal conditions provided an efficient preparative scale biocatalytic procedure of valuable phenylalanines, such as (S)-m-methoxyphenylalanine (Y = 40%, ee > 99%), (S)-p-bromophenylalanine (Y = 82%, ee > 99%), (S)-m-(trifluoromethyl)phenylalanine (Y = 26%, ee > 99%), (R)-p-methylphenylalanine, (Y = 49%, ee = 95%) and (R)-m-(trifluoromethyl)phenylalanine (Y = 34%, ee = 93%).
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.