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

Ca2+ -independent sortase-A exhibits high selective protein ligation activity in the cytoplasm of Escherichia coli.

Biotechnology journal - 1 Sept 2015

Hirakawa Hidehiko, Ishikawa Suguru, Nagamune Teruyuki

Abstract excerpt

A Staphylococcus aureus transpeptidase, sortase A (SrtA), which catalyzes a peptide ligation with high substrate specificity, is a useful tool to site-specifically attach proteinaceous/peptidic functional molecules to target proteins. However, its strong Ca(2+) dependency makes SrtA difficult for use under low Ca(2+) concentrations and in the presence of Ca(2+)-binding substances. To overcome this problem, we...

Read the complete abstract on PubMed

Topics

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

Share to Aminoacyltransferases
Share to Calcium
Share to Cysteine Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoplasm

Share to Escherichia coli

Share to Kinetics

Share to Proteins

Share to Staphylococcus aureus

Source

Identifiers

PMID: 25864513
DOI: 10.1002/biot.201500012

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

Ca2+ -independent sortase-A exhibits high selective protein ligation activity in the cytoplasm of Escherichia coli.PMID 25864513Read ↗

Generation of Ca2+-independent sortase A mutants with enhanced activity for protein and cell surface labeling.Semantic proximity Read ↗

Design of Ca2+-independent Staphylococcus aureus sortase A mutants.Semantic proximity Read ↗

Semisynthesis and initial characterization of sortase A mutants containing selenocysteine and homocysteine.Semantic proximity Read ↗

Sortase mutants with improved protein thermostability and enzymatic activity obtained by consensus design.Semantic proximity Read ↗

Mutagenesis studies of substrate recognition and catalysis in the sortase A transpeptidase from Staphylococcus aureus.Semantic proximity Read ↗

Site-specific protein modification using immobilized sortase in batch and continuous-flow systems.Semantic proximity Read ↗

A FRET Ligation Assay using Fluorescent Proteins for Bacterial Sortase EnzymesSemantic proximity Read ↗

Sequence variation in the β7-β8 loop of bacterial class A sortase enzymes alters substrate selectivity.Semantic proximity Read ↗

Synthetic protein degradation circuits using programmable cleavage and ligation by Sortase ASemantic proximity Read ↗

Amino acid variants at the P94 position in <i>Staphylococcus aureus</i> class A sortase modulate substrate binding and enzyme activitySemantic proximity Read ↗

Functional analysis of Clostridium difficile sortase B reveals key residues for catalytic activity and substrate specificity.Semantic proximity Read ↗

Streptococcus suis sortase A is Ca2+ independent and is inhibited by acteoside, isoquercitrin and baicalin.Semantic proximity Read ↗

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