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

Thermal stable and oxidation-resistant variant of subtilisin E.

Journal of biotechnology - 25 Aug 2000

Yang Y, Jiang L, Zhu L, Wu Y, Yang S

Abstract excerpt

A remarkable thermal stable and oxidation-resistant mutant was obtained using the random mutagenesis PCR technique on the mutant M222A gene of subtilisin E. Sequencing analysis revealed an A was replaced by G at nucleotide 671 of the subtilisin E gene, converting the asparagine codon (AAT) to serine codon (AGT) at position 118. The half-life of M222A/N118S enzyme activity, when heated at 65 degrees C, was...

Read the complete abstract on PubMed

Topics

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

Share to Amidohydrolases
Share to Amino Acid Substitution
Share to Bacillus subtilis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Hot Temperature

Share to Mutagenesis

Share to Oxidation-Reduction

Share to Subtilisins

Source

Identifiers

PMID: 10989170
DOI: 10.1016/s0168-1656(00)00272-8

Genes

AGT

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Thermal stable and oxidation-resistant variant of subtilisin E.PMID 10989170Read ↗

Exploring mutable conserved sites and fatal non-conserved sites by random mutation of esterase from Sulfolobus tokodaii and subtilisin from Thermococcus kodakarensis.Semantic proximity Read ↗

Enhanced thermostability of the single-Cys mutant subtilisin E under oxidizing conditions.Semantic proximity Read ↗

Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease.Semantic proximity Read ↗

Improvement in the alkaline stability of subtilisin using an efficient random mutagenesis and screening procedure.Semantic proximity Read ↗

The role of tryptophan residues in the autoprocessing of prosubtilisin E.Semantic proximity Read ↗

Need for aromatic residue at position 115 for proteolytic activity found by site-directed mutagenesis of tryptophan 115 in thermolysin.Semantic proximity Read ↗

An alternative mature form of subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis identified in the presence of Ca2+.Semantic proximity Read ↗

Mutational effects on thermostable superoxide dismutase from Aquifex pyrophilus: understanding the molecular basis of protein thermostability.Semantic proximity Read ↗

Identification of the amino acid residues essential for proteolytic activity in an archaeal signal peptide peptidase.Semantic proximity Read ↗

Enhancement of keratinolytic activity of a thermophilic subtilase by improving its autolysis resistance and thermostability under reducing conditions.Semantic proximity Read ↗

The effect of changing the hydrophobic S1' subsite of thermolysin-like proteases on substrate specificity.Semantic proximity Read ↗

Improved autoprocessing efficiency of mutant subtilisins E with altered specificity by engineering of the pro-region.Semantic proximity Read ↗

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