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

Modification of substrate-binding site of glutamyl endopeptidase from Bacillus intermedius.

Protein engineering, design & selection : PEDS - 1 May 2004

Demidyuk I V, Romanova D V, Nosovskaya E A, Chestukhina G G, Kuranova I P, Kostrov S V

Abstract excerpt

Glutamyl endopeptidases (GEPs) are serine proteases belonging to the chymotrypsin structural family. Although the family as a whole has been described in detail, the molecular mechanism underlying strict substrate specificity of GEPs remains unclear. The most popular hypothesis attributes the key role in recognition of the charged substrates by GEPs to the conserved amino acid His213 (chymotrypsin numbering...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus
Share to Binding Sites
Share to Histidine

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

Share to Insulin

Share to Mutation

Share to Serine Endopeptidases

Share to Substrate Specificity

Source

Identifiers

PMID: 15187226
DOI: 10.1093/protein/gzh050

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

Modification of substrate-binding site of glutamyl endopeptidase from Bacillus intermedius.PMID 15187226Read ↗

Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase.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 ↗

Deciphering the molecular basis of the broad substrate specificity of alpha-glucosidase from Bacillus sp. SAM1606.Semantic proximity Read ↗

Roles of asp126 and asp156 in the enzyme function of sphingomyelinase from Bacillus cereus.Semantic proximity Read ↗

Approaching transglutaminase from Streptomyces bacteria over three decadesSemantic proximity Read ↗

Crystal structures of protein glutaminase and its pro forms converted into enzyme-substrate complex.Semantic proximity Read ↗

Site-directed mutagenesis of conserved Thr407, Asp433 and Met464 residues in small subunit of Escherichia coli gamma-glutamyltranspeptidase.Semantic proximity Read ↗

Analysis of essential amino acid residues for catalytic activity of glutaminase from Micrococcus luteus K-3.Semantic proximity Read ↗

Change in substrate preference of Streptomyces aminopeptidase through modification of the environment around the substrate binding site.Semantic proximity Read ↗

Evolving transpeptidase and hydrolytic variants of γ-glutamyl transpeptidase from Bacillus licheniformis by targeted mutations of conserved residue Arg109 and their biotechnological relevance.Semantic proximity Read ↗

Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis.Semantic proximity Read ↗

Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by site-directed mutagenesis.Semantic proximity Read ↗

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