Phenylalanine ammonia lyase from Arabidopsis thaliana ( At PAL2): A potent MIO-enzyme for the synthesis of non-canonical aromatic alpha-amino acids.-Reference-Cited by-同舟云学术

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Phenylalanine ammonia lyase from Arabidopsis thaliana ( At PAL2): A potent MIO-enzyme for the synthesis of non-canonical aromatic alpha-amino acids.

Published:2017-09 Issue: Volume:258 Page:158-166
ISSN:0168-1656
Container-title:Journal of Biotechnology
language:en
Short-container-title:Journal of Biotechnology

Author:

Dreßen Alana,Hilberath Thomas,Mackfeld Ursula,Rudat Jens,Pohl Martina

Funder

Federal Ministry for Education and Research (BMBF) project: Molecular Interaction Engineering

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology,Bioengineering

Reference41 articles.

1. Non-canonical amino acids as a useful synthetic biological tool for lipase-catalysed reactions in hostile environments;Acevedo-Rocha;Catal. Sci. Technol.,2013

2. Chemoenzymatic synthesis of optically pure L - and D - biarylalanines through biocatalytic asymmetric amination and palladium-catalyzed arylation;Ahmed;ACS Catal.,2015

3. Structure and function of amino acid ammonia-lyases;Asano;Biocatal. Biotransform.,2004

4. Immobilization of phenylalanine ammonia-lyase on single-walled carbon nanotubes for stereoselective biotransformations in batch and continuous-flow modes;Bartha-Vári;ChemCatChem,2015

5. Mutational analysis of phenylalanine ammonia lyase to improve reactions rates for various substrates;Bartsch;Protein Eng. Des. Sel.,2010

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3. Yeast-Based Whole-Cell Factory for the Ecofriendly Synthesis of Vanillylamine as a Critical Step toward Capsaicin Production;ACS Sustainable Chemistry & Engineering;2023-05-11

4. Sustainable synthesis of L-phenylalanine derivatives in continuous flow by immobilized phenylalanine ammonia lyase;Frontiers in Catalysis;2023-05-04

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