Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self-cleavage exhibits enhanced enzymatic activity.

FEBS open bio - 1 Apr 2020

Nam Heejin, Hwang Beom J, Choi Deog-Young, Shin Sooim, Choi Moonsung

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalytic Domain
Share to Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Activation

Share to Inclusion Bodies

Share to Potyvirus

Share to Solubility

Share to Substrate Specificity

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 32129006
DOI: 10.1002/2211-5463.12828
PMCID: PMC7137792

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tobacco etch virus (TEV) protease with multiple mutations to improve solubility and reduce self-cleavage exhibits enhanced enzymatic activity.PMID 32129006Read ↗

In vivo and in vitro characterization of TEV protease mutants.Semantic proximity Read ↗

Combination of the mutations for improving activity of TEV protease in inclusion bodies.Semantic proximity Read ↗

P1' specificity of the S219V/R203G mutant tobacco etch virus protease.Semantic proximity Read ↗

Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency.Semantic proximity Read ↗

An improved variant of tobacco etch virus (TEV) protease that does not need reducing agents.Semantic proximity Read ↗

Construction, Investigation and Application of TEV Protease Variants with Improved Oxidative Stability.Semantic proximity Read ↗

Insight into the structural stability of wild type and mutants of the tobacco etch virus protease with molecular dynamics simulations.Semantic proximity Read ↗

Engineering soluble tobacco etch virus protease accompanies the loss of stability.Semantic proximity Read ↗

Engineered tobacco etch virus (TEV) protease active in the secretory pathway of mammalian cells.Semantic proximity Read ↗

Enhancing the stability and solubility of TEV protease using in silico design.Semantic proximity Read ↗

A tobacco etch virus protease with increased substrate tolerance at the P1' position.Semantic proximity Read ↗

[Tobacco etch virus proteinase: crystal structure of the active enzyme and its inactive mutant].Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.