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

A covalently trapped folding intermediate of subtilisin E: spontaneous dimerization of a prosubtilisin E Ser49Cys mutant in vivo and its autoprocessing in vitro.

Biochemistry - 18 Jan 1994

Hu Z, Zhu X, Jordan F, Inouye M

Abstract excerpt

The propeptide of subtilisin E (the N-terminal 77 amino acid extension) is required for the proper folding of the nascent mature protein and is also a potent and specific inhibitor of the active enzyme. Previous studies have demonstrated that the propeptide can renature denatured mature sequence either in cis or in trans and can be considered an intramolecular chaperone, since it is not required for activity of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence
Share to Cloning, Molecular

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

Share to Escherichia coli

Share to Macromolecular Substances

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Mutation

Source

Identifiers

PMID: 8286386
DOI: 10.1021/bi00168a022

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

A covalently trapped folding intermediate of subtilisin E: spontaneous dimerization of a prosubtilisin E Ser49Cys mutant in vivo and its autoprocessing in vitro.PMID 8286386Read ↗

Substrate-induced activation of a trapped IMC-mediated protein folding intermediate.Semantic proximity Read ↗

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

The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli.Semantic proximity Read ↗

Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants.Semantic proximity Read ↗

Identification of furin pro-region determinants involved in folding and activation.Semantic proximity Read ↗

Accelerated refolding of subtilisin BPN' by tertiary-structure-forming mutants of its propeptide.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 ↗

Engineering the independent folding of the subtilisin BPN' prodomain: analysis of two-state folding versus protein stability.Semantic proximity Read ↗

Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilisin nattokinase.Semantic proximity Read ↗

Crystal structures of subtilisin BPN' variants containing disulfide bonds and cavities: concerted structural rearrangements induced by mutagenesis.Semantic proximity Read ↗

Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity.Semantic proximity Read ↗

Cystathionine beta-synthase mutants exhibit changes in protein unfolding: conformational analysis of misfolded variants in crude cell extracts.Semantic proximity Read ↗

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