ArticlePloS one2014
Expression and properties of the highly alkalophilic phenylalanine ammonia-lyase of thermophilic Rubrobacter xylanophilus.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 35 citations in OpenAlex.
- Genome-wide analysis and expression profiling of the phenylalanine ammonia-lyase gene family in Chrysanthemum morifolium.BMC plant biology · 2026Article
- How to Enhance the Applicability of Metal Ion Affinity-bound Biocatalysts? Comprehensive Overview and Case Study With a Phenylalanine Ammonia Lyase and an Amine Transaminase.Chembiochem : a European journal of chemical biology · 2026Article
- Evolution of phenylalanine ammonia-lyase protein family from algae to angiosperm.Functional & integrative genomics · 2025Article
- Detrimental Effects of Elevated Temperatures on the Structure and Activity of Phenylalanine Ammonia Lyase-Bovine Serum Albumin Mixtures and the Stabilizing Potential of Surfactant and Sugars.AAPS PharmSciTech · 2022Article
- Biochemical Characterization of Novel Phenylalanine Ammonia-Lyase from Spirulina CPCC-695.The protein journal · 2022Article
- The First Insight into Polyhydroxyalkanoates Accumulation in Multi-ExtremophilicMicroorganisms · 2021Article
- Fluorescent enzyme-coupled activity assay for phenylalanine ammonia-lyases.Scientific reports · 2020Article
- Purification and Characterization ofJournal of microbiology and biotechnology · 2020Article
- Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes.Scientific reports · 2017Article
- Highly Active and Specific Tyrosine Ammonia-Lyases from Diverse Origins Enable Enhanced Production of Aromatic Compounds in Bacteria and Saccharomyces cerevisiae.Applied and environmental microbiology · 2015Article
- Immobilization of Phenylalanine Ammonia-Lyase on Single-Walled Carbon Nanotubes for Stereoselective Biotransformations in Batch and Continuous-Flow Modes.ChemCatChem · 2015Article
- Phenylpropionic acid produced by gut microbiota alleviates acetaminophen-induced hepatotoxicity.Gut microbesArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sequence of a phenylalanine ammonia-lyase (PAL; EC: 4.3.1.24) of the thermophilic and radiotolerant bacterium Rubrobacter xylanophilus (RxPAL) was identified by screening the genomes of bacteria for members of the phenylalanine ammonia-lyase family. A synthetic gene encoding the RxPAL protein was cloned and overexpressed in Escherichia coli TOP 10 in a soluble form with an N-terminal His6-tag and the recombinant RxPAL protein was purified by Ni-NTA affinity chromatography. The activity assay of RxPAL with l-phenylalanine at various pH values exhibited a local maximum at pH 8.5 and a global maximum at pH 11.5. Circular dichroism (CD) studies showed that RxPAL is associated with an extensive α-helical character (far UV CD) and two distinctive near-UV CD peaks. These structural characteristics were well preserved up to pH 11.0. The extremely high pH optimum of RxPAL can be rationalized by a three-dimensional homology model indicating possible disulfide bridges, extensive salt-bridge formation and an excess of negative electrostatic potential on the surface. Due to these properties, RxPAL may be a candidate as biocatalyst in synthetic biotransformations leading to unnatural l- or d-amino acids or as therapeutic enzyme in treatment of phenylketonuria or leukemia.
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.