ArticleScientific reports2017
Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- 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
- Citric Acid Changes the Fingerprint of Flavonoids and Promotes Their Accumulation inLife (Basel, Switzerland) · 2022Article
- Towards a general approach for tailoring the hydrophobic binding site of phenylalanine ammonia-lyases.Scientific reports · 2022Article
- In-depth Sequence-Function Characterization Reveals Multiple Pathways to Enhance Enzymatic Activity.ACS catalysis · 2022Article
- Robust, site-specifically immobilized phenylalanine ammonia-lyases for the enantioselective ammonia addition of cinnamic acids.Catalysis science & technology · 2021Article
- Article
- Identification and Characterization of an Efficient Phenylalanine Ammonia-Lyase from Photorhabdus luminescens.Applied biochemistry and biotechnology · 2021Article
- Fluorescent enzyme-coupled activity assay for phenylalanine ammonia-lyases.Scientific reports · 2020Article
- Purification and Characterization ofJournal of microbiology and biotechnology · 2020Article
- The production of L- and D-phenylalanines using engineered phenylalanine ammonia lyases from Petroselinum crispum.Scientific reports · 2019Article
- Tailored Mutants of Phenylalanine Ammonia-Lyase fromChemCatChem · 2018Article
- Phenylpropionic acid produced by gut microbiota alleviates acetaminophen-induced hepatotoxicity.Gut microbesArticle
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Authors and funding
8 authors.
Funding
Abstract
The suite of biological catalysts found in Nature has the potential to contribute immensely to scientific advancements, ranging from industrial biotechnology to innovations in bioenergy and medical intervention. The endeavour to obtain a catalyst of choice is, however, wrought with challenges. Herein we report the design of a structure-based annotation system for the identification of functionally similar enzymes from diverse sequence backgrounds. Focusing on an enzymatic activity with demonstrated synthetic and therapeutic relevance, five new phenylalanine ammonia lyase (PAL) enzymes were discovered and characterised with respect to their potential applications. The variation and novelty of various desirable traits seen in these previously uncharacterised enzymes demonstrates the importance of effective sequence annotation in unlocking the potential diversity that Nature provides in the search for tailored biological tools. This new method has commercial relevance as a strategy for assaying the 'evolvability' of certain enzyme features, thus streamlining and informing protein engineering efforts.
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