Enhancement of tryptophan 2-monooxygenase thermostability by semi-rational enzyme engineering: a strategic design to minimize experimental investigation-Reference-Cited by-同舟云学术

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Enhancement of tryptophan 2-monooxygenase thermostability by semi-rational enzyme engineering: a strategic design to minimize experimental investigation

Published:2024 Issue: Volume: Page:
ISSN:2633-0679
Container-title:RSC Chemical Biology
language:en
Short-container-title:RSC Chem. Biol.

Author:

Kongjaroon Sirus¹^ORCID,Lawan Narin²^ORCID,Trisrivirat Duangthip¹^ORCID,Chaiyen Pimchai¹^ORCID

Affiliation:

1. School of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology (VISTEC), Wangchan Valley, Rayong, 21210, Thailand

2. Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand

Abstract

A semi-rational and strategic-design approach using in silico tools and site-saturation mutagenesis with minimal experimental effort was used to engineer tryptophan 2-monooxygenase to obtain thermostable variants with the same enzyme activity.

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CB/D4CB00102H

Reference44 articles.

1. Indole-3-acetic acid in microbial and microorganism-plant signaling

2. Versatile and Facile One-Pot Biosynthesis for Amides and Carboxylic Acids in E. coli by Engineering Auxin Pathways of Plant Microbiomes

3. De novo biosynthesis of 2-phenylacetamide in engineered Escherichia coli

4. Dynamic modulation of enzyme activity by synthetic CRISPR–Cas6 endonucleases

5. A tryptophan-2-monooxygenase based amperometric biosensor for L-tryptophan determination: use of a competitive inhibitor as a tool for selectivity increase

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