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

Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.

EMBO reports - 1 Sept 2000

Fülöp V, Szeltner Z, Polgár L

Abstract excerpt

Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta-propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Crystallography, X-Ray
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Disulfides

Share to Enzyme Stability

Share to Hydrogen-Ion Concentration

Share to Oxidation-Reduction

Share to Serine Endopeptidases

Source

Open in PubMed Open full text

Identifiers

PMID: 11256612
DOI: 10.1093/embo-reports/kvd048
PMCID: PMC1083722

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

Catalysis of serine oligopeptidases is controlled by a gating filter mechanism.PMID 11256612Read ↗

Protease propeptide structures, mechanisms of activation, and functions.Semantic proximity Read ↗

Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems.Semantic proximity Read ↗

Activity modulation of the oligopeptidase B from Serratia proteamaculans by site-directed mutagenesis of amino acid residues surrounding catalytic triad histidine.Semantic proximity Read ↗

Substrate Recognition Properties of Oligopeptidase B fromSalmonella entericaSerovar TyphimuriumSemantic proximity Read ↗

Ala657 and conserved active site residues promote fibroblast activation protein endopeptidase activity via distinct mechanisms of transition state stabilization.Semantic proximity Read ↗

Mapping specificity, entropy, allosteric changes and substrates in blood proteases by a high-throughput protease screenSemantic proximity Read ↗

Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate.Semantic proximity Read ↗

Allosteric regulation of the proteasome’s catalytic sites by the proteasome activator PA28γ /REGγSemantic proximity Read ↗

Rhomboids: 7 years of a new protease familySemantic proximity Read ↗

The serpins: nature's molecular mousetraps.Semantic proximity Read ↗

Propeptide engineering of Aspergillus niger-derived aspartic protease PepA for enhanced catalytic activity.Semantic proximity Read ↗

Massively parallel, computationally-guided design of a pro-enzymeSemantic proximity Read ↗

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