ArticleFEBS open bio2020
Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self-cleavage exhibits enhanced enzymatic activity.
Article in FEBS open bio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Sequence-free landscape inference for directed evolution.PLoS computational biology · 2026Article
- Improvements in large-scale production of tobacco etch virus protease.Protein expression and purification · 2025Article
- Article
- Structural determination and kinetic analysis of the transketolase from Vibrio vulnificus reveal unexpected cooperative behavior.Protein science : a publication of the Protein Society · 2024Article
- Mechanism of Mutation-Induced Effects on the Catalytic Function of TEV Protease: A Molecular Dynamics Study.Molecules (Basel, Switzerland) · 2024Article
- Advancing large-scale production of TEV protease through an innovative NT* tag-based fusion construct.Current research in structural biology · 2023Article
- Fluorescence dequenching assay for the activity of TEV protease.Analytical biochemistry · 2022Article
- Between Protein Fold and Nucleophile Identity: Multiscale Modeling of the TEV Protease Enzyme-Substrate Complex.ACS omega · 2022Article
- Construction, Investigation and Application of TEV Protease Variants with Improved Oxidative Stability.Journal of microbiology and biotechnology · 2021Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tobacco etch virus (TEV) protease is a 27-kDa catalytic domain of the polyprotein nuclear inclusion a (NIa) in TEV, which recognizes the specific amino acid sequence ENLYFQG/S and cleaves between Q and G/S. Despite its substrate specificity, its use is limited by its autoinactivation through self-cleavage and poor solubility during purification. It was previously reported that T17S/N68D/I77V mutations improve the solubility and yield of TEV protease and S219 mutations provide protection against self-cleavage. In this study, we isolated TEV proteases with S219N and S219V mutations in the background of T17S, N68D, and I77V without the inclusion body, and measured their enzyme kinetics. The k
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