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

Kinetics and Optimization of the Lysine-Isopeptide Bond Forming Sortase Enzyme from Corynebacterium diphtheriae.

Bioconjugate chemistry - 17 Jun 2020

Sue Christopher K, McConnell Scott A, Ellis-Guardiola Ken, Muroski John M, McAllister Rachel A, Yu Justin, Alvarez Ana I, Chang Chungyu, Ogorzalek Loo Rachel R, Loo Joseph A, Ton-That Hung, Clubb Robert T

Abstract excerpt

Site-specifically modified protein bioconjugates have important applications in biology, chemistry, and medicine. Functionalizing specific protein side chains with enzymes using mild reaction conditions is of significant interest, but remains challenging. Recently, the lysine-isopeptide bond forming activity of the sortase enzyme that builds surface pili in Corynebacterium diphtheriae (CdSrtA) has been...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Corynebacterium diphtheriae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine Endopeptidases

Share to Kinetics

Share to Lysine

Share to Mutation

Share to Peptides

Share to Protein Domains

Source

Open in PubMed Open full text

Identifiers

PMID: 32396336
DOI: 10.1021/acs.bioconjchem.0c00163
PMCID: PMC8153732

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kinetics and Optimization of the Lysine-Isopeptide Bond Forming Sortase Enzyme from Corynebacterium diphtheriae.PMID 32396336Read ↗

The Basal and Major Pilins in the <i>Corynebacterium diphtheriae</i> SpaA Pilus Adopt Similar Structures that Competitively React with the Pilin PolymeraseSemantic proximity Read ↗

A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence.Semantic proximity Read ↗

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

Conformational analysis and chemical reactivity of the multidomain sulfurtransferase, Staphylococcus aureus CstA.Semantic proximity Read ↗

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

Acyl enzyme intermediates in sortase-catalyzed pilus morphogenesis in gram-positive bacteria.Semantic proximity Read ↗

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

Engineering protein farnesyltransferase for enzymatic protein labeling applications.Semantic proximity Read ↗

Synthetic mycolates derivatives to decipher protein mycoloylation, a unique post-translational modification in bacteriaSemantic proximity Read ↗

In Silico Screening Using Freely Available Computational Tools to Generate Novel Peptide/Protein Pairs for Protein-Protein Ligation.Semantic proximity Read ↗

Structure-based rational design of streptavidin mutants with pseudo-catalytic activity.Semantic proximity Read ↗

Diaminopimelic Acid Amidation in Corynebacteriales: NEW INSIGHTS INTO THE ROLE OF LtsA IN PEPTIDOGLYCAN MODIFICATION.Semantic proximity Read ↗

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