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

Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies.

Biochimie - 1 Sept 2011

Mikleušević Goran, Stefanić Zoran, Narczyk Marta, Wielgus-Kutrowska Beata, Bzowska Agnieszka, Luić Marija

Abstract excerpt

The catalytic mechanism of Escherichia coli purine nucleoside phosphorylase (PNP) is revised using site-directed mutagenesis, kinetic studies and structure determinations. The experimental evidence on the role of the particular catalytic amino acid during catalysis has not been available. Therefore, the active site mutants Arg24Ala, Asp204Ala, Asp204Asn, Arg217Ala and Asp204Ala/Arg217Ala were prepared and their...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Crystallography, X-Ray

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

Share to Guanosine

Share to Kinetics

Share to Mutagenesis, Site-Directed

Share to Purine-Nucleoside Phosphorylase

Share to Structure-Activity Relationship

Share to Substrate Specificity

Source

Identifiers

PMID: 21672603
DOI: 10.1016/j.biochi.2011.05.030

Genes

PNP

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

Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies.PMID 21672603Read ↗

Structural analysis of the bacterial HPr kinase/phosphorylase V267F mutant gives insights into the allosteric regulation mechanism of this bifunctional enzyme.Semantic proximity Read ↗

Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach.Semantic proximity Read ↗

Structure-function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria.Semantic proximity Read ↗

Mutational analysis of polynucleotide phosphorylase from Escherichia coli.Semantic proximity Read ↗

A conserved loop in polynucleotide phosphorylase (PNPase) essential for both RNA and ADP/phosphate binding.Semantic proximity Read ↗

On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase.Semantic proximity Read ↗

Determinants of ligand binding and catalytic activity in the myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase.Semantic proximity Read ↗

Thermodynamics of the Purine Nucleoside Phosphorylase Reaction Revealed by Computer Simulations.Semantic proximity Read ↗

Enhancement of nucleoside phosphorylation activity in an acid phosphatase.Semantic proximity Read ↗

Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase.Semantic proximity Read ↗

Aromatic stacking between nucleobase and enzyme promotes phosphate ester hydrolysis in dUTPase.Semantic proximity Read ↗

Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase.Semantic proximity Read ↗

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