Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution-Reference-Cited by-同舟云学术

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Enhancing PLP-Binding Capacity of Class-III ω-Transaminase by Single Residue Substitution

Published:2019-10-18 Issue: Volume:7 Page:
ISSN:2296-4185
Container-title:Frontiers in Bioengineering and Biotechnology
language:
Short-container-title:Front. Bioeng. Biotechnol.

Author:

Roura Padrosa David,Alaux Raphael,Smith Phillip,Dreveny Ingrid,López-Gallego Fernando,Paradisi Francesca

Funder

Biotechnology and Biological Sciences Research Council

Ministerio de Economía, Industria y Competitividad, Gobierno de España

Ministerio de Ciencia y Tecnología

Publisher

Frontiers Media SA

Subject

Biomedical Engineering,Histology,Bioengineering,Biotechnology

Reference44 articles.

1. Self-sufficient flow-biocatalysis by coimmobilization of pyridoxal 5′-phosphate and ω-transaminases onto porous carriers;Benítez-Mateos;ACS Sustain. Chem. Eng.,2018

2. Generic HPLC platform for automated enzyme reaction monitoring: advancing the assay toolbox for transaminases and other PLP-dependent enzymes;Börner;Biotech. J.,2016

3. Three in one: temperature, solvent and catalytic stability by engineering the cofactor-binding element of amine transaminase;Börner;ChemBioChem

4. Explaining operational instability of amine transaminases: substrate-induced inactivation mechanism and influence of quaternary structure on enzyme-cofactor intermediate stability;Börner;ACS Catal.

5. The ω-transaminase engineering database (OTAED): a navigation tool in protein sequence and structure space;Buß;Proteins,2018

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