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

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

Indian journal of biochemistry & biophysics - 1 Aug 2007

Lo Huei-Fen, Lin Long-Liu, Chen Pei-Jing, Chou Wei-Mou

Abstract excerpt

Sequence comparison showed that residues Thr407, Asp433, and Met464 in the small subunit of Escherichia coli gamma-glutamyltranspeptidase (EcGGT) were conserved in the aligned enzymes. In this study, we further investigated the functional significance of these conserved residues by site-directed mutagenesis. The wild-type and mutant enzymes were overexpressed in the recombinant E. coli M15 cells and purified to...

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 Amino Acids

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

Share to Conserved Sequence

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to gamma-Glutamyltransferase

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Source

Identifiers

PMID: 17970276

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

Site-directed mutagenesis of conserved Thr407, Asp433 and Met464 residues in small subunit of Escherichia coli gamma-glutamyltranspeptidase.PMID 17970276Read ↗

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

Effect of site-directed mutations on processing and activity of gamma-glutamyltranspeptidase of Escherichia coli K-12.Semantic proximity Read ↗

Expression optimization and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Escherichia coli novablue.Semantic proximity Read ↗

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

Increased activity of β-glucuronidase variants produced by site-directed mutagenesis.Semantic proximity Read ↗

Escherichia coli gamma-glutamyltranspeptidase mutants deficient in processing to subunits.Semantic proximity Read ↗

Identification of two glutamic acid residues essential for catalysis in the beta-glycosidase from the thermoacidophilic archaeon Sulfolobus solfataricus.Semantic proximity Read ↗

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

Enhancement of Streptomyces transglutaminase activity and pro-peptide cleavage efficiency by introducing linker peptide in the C-terminus of the pro-peptide.Semantic proximity Read ↗

Modification of substrate-binding site of glutamyl endopeptidase from Bacillus intermedius.Semantic proximity Read ↗

Approaching transglutaminase from Streptomyces bacteria over three decadesSemantic proximity Read ↗

Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli.Semantic proximity Read ↗

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