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

Intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli.

Biochimica et biophysica acta - 17 Aug 1999

Kasche V, Lummer K, Nurk A, Piotraschke E, Rieks A, Stoeva S, Voelter W

Abstract excerpt

The penicillin amidase (PA) from Escherichia coli belongs to a group of proteolytically processed bacterial enzymes. The mechanism of the maturation of the single polypeptide proenzyme has been studied for the PA from E. coli using a slowly processing mutant proenzyme. The mutant proenzyme was constructed by replacing Thr with Gly in the Thr(263)-Ser(264) bond that must be hydrolysed in active PA. The mutant...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Chromatography, Affinity

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

Share to Endopeptidases

Share to Enzyme Precursors

Share to Escherichia coli

Share to Kinetics

Share to Mass Spectrometry

Share to Molecular Structure

Source

Identifiers

PMID: 10446361
DOI: 10.1016/s0167-4838(99)00155-7

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

Intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli.PMID 10446361Read ↗

Primary structure requirements for the maturation in vivo of penicillin acylase from Escherichia coli ATCC 11105.Semantic proximity Read ↗

Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft.Semantic proximity Read ↗

Propeptide processing and proteolytic activity of proenzymes of the staphylococcal and enterococcal GluV8-family protease.Semantic proximity Read ↗

Degradation of secreted proteins in Escherichia coli.Semantic proximity Read ↗

Activation of Pseudomonas aeruginosa elastase in Pseudomonas putida by triggering dissociation of the propeptide-enzyme complex.Semantic proximity Read ↗

Processive degradation of unstructured protein by Escherichia coli Lon occurs via the slow, sequential delivery of multiple scissile sites followed by rapid and synchronized peptide bond cleavage events.Semantic proximity Read ↗

Inhibitor-assisted refolding of protease: a protease inhibitor as an intramolecular chaperone.Semantic proximity Read ↗

Folding and assembly of bacterial alkaline phosphatase in vitro and in vivo.Semantic proximity Read ↗

Intein-Promoted Cyclization of Aspartic Acid Flanking the Intein Leads to Atypical N-Terminal Cleavage.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 ↗

The propeptide is required for in vivo formation of stable active yeast proteinase A and can function even when not covalently linked to the mature region.Semantic proximity Read ↗

Autoprocessing: an essential step for the activation of HIV-1 protease.Semantic proximity Read ↗

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