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

A new kinetic mechanism for the concomitant hydrolysis and transfer reactions catalyzed by bacterial DD-peptidases.

Biochemistry - 20 Jul 1993

Jamin M, Wilkin J M, Frère J M

Abstract excerpt

In the presence of an adequate nucleophilic acceptor substrate (A) and ester and thiolester donor substrates (S), the Streptomyces R61 soluble DD-peptidase catalyzes both hydrolysis and acyl group transfer reactions. Simple bisubstrate models do not explain the variation of the transfer to hydrolysis ratios with the donor and acceptor concentrations. A new kinetic mechanism for the concomitant hydrolysis and...

Read the complete abstract on PubMed

Topics

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

Share to Asparagine
Share to Catalysis
Share to Hydrolysis

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

Share to Kinetics

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Serine

Share to Streptomyces

Source

Identifiers

PMID: 8343517
DOI: 10.1021/bi00079a026

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

A new kinetic mechanism for the concomitant hydrolysis and transfer reactions catalyzed by bacterial DD-peptidases.PMID 8343517Read ↗

Importance of the His-298 residue in the catalytic mechanism of the Streptomyces R61 extracellular DD-peptidase.Semantic proximity Read ↗

The catalytic mechanism of DD-peptidases: unexpected importance of tyrosine 280 in the transpeptidation reaction catalysed by the Streptomyces R61 DD-peptidase.Semantic proximity Read ↗

A simple method for the determination of individual rate constants for substrate hydrolysis by serine proteases.Semantic proximity Read ↗

Biophysical characterization of in vitro bound Streptomyces peucetius daunorubicin-serine protease complex.Semantic proximity Read ↗

Glucose transport by a mutant of Streptococcus mutans unable to accumulate sugars via the phosphoenolpyruvate phosphotransferase system.Semantic proximity Read ↗

Deacylation kinetics analysis of Streptococcus pneumoniae penicillin-binding protein 2x mutants resistant to beta-lactam antibiotics using electrospray ionization- mass spectrometry.Semantic proximity Read ↗

The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis.Semantic proximity Read ↗

Point mutations of two arginine residues in the Streptomyces R61 DD-peptidase.Semantic proximity Read ↗

Catalytic site interactions in yeast OMP synthase.Semantic proximity Read ↗

Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.Semantic proximity Read ↗

Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase.Semantic proximity Read ↗

Transient kinetic analysis of L-serine interaction with Escherichia coli D-3-phosphoglycerate dehydrogenase containing amino acid mutations in the hinge regions.Semantic proximity Read ↗

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