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

Kinetic and structural characterization of dihydrofolate reductase from Streptococcus pneumoniae.

Biochemistry - 12 Jan 2010

Lee Jeeyeon, Yennawar Neela H, Gam Jongsik, Benkovic Stephen J

Abstract excerpt

Drug resistance associated with dihydrofolate reductase (DHFR) has emerged as a critical issue in the treatment of bacterial infections. In our efforts to understand the mechanism of a drug-resistant dihydrofolate reductase (DHFR) from a pathogenic bacterial source, we report the first kinetic characterization of Streptococcus pneumoniae DHFR (spDHFR) along with its X-ray structure. This study revealed that the...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to G-Quadruplexes
Share to Histidine

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

Share to Protein Folding

Share to Streptococcus pneumoniae

Share to Tetrahydrofolate Dehydrogenase

Share to Thermodynamics

Share to Trimethoprim

Source

Open in PubMed Open full text

Identifiers

PMID: 19950924
DOI: 10.1021/bi901614m
PMCID: PMC3773979

Genes

DHFR

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

Kinetic and structural characterization of dihydrofolate reductase from Streptococcus pneumoniae.PMID 19950924Read ↗

First Three-Dimensional Structure of <i>Toxoplasma gondii</i> Thymidylate Synthase–Dihydrofolate Reductase: Insights for Catalysis, Interdomain Interactions, and Substrate ChannelingSemantic proximity Read ↗

Mutational 'hot-spots' in mammalian, bacterial and protozoal dihydrofolate reductases associated with antifolate resistance: sequence and structural comparison.Semantic proximity Read ↗

Predicting antifolate resistance in the unculturable fungal pathogen Pneumocystis jirovecii.Semantic proximity Read ↗

Deep mutational scanning of Pneumocystis jirovecii dihydrofolate reductase reveals allosteric mechanism of resistance to an antifolate.Semantic proximity Read ↗

Deep mutational scanning of <i>Pneumocystis jirovecii</i> dihydrofolate reductase reveals allosteric mechanism of resistance to an antifolateSemantic proximity Read ↗

Exploration of fluoroquinolone resistance in Streptococcus pyogenes: comparative structure analysis of wild-type and mutant DNA gyrase.Semantic proximity Read ↗

The Structural and Functional Basis for Recurring Sulfa Drug Resistance Mutations in Staphylococcus aureus Dihydropteroate SynthaseSemantic proximity Read ↗

Structure, dynamics, and catalytic function of dihydrofolate reductase.Semantic proximity Read ↗

Structural comparison of chromosomal and exogenous dihydrofolate reductase from Staphylococcus aureus in complex with the potent inhibitor trimethoprim.Semantic proximity Read ↗

A conservative amino acid mutation in the chromosome-encoded dihydrofolate reductase confers trimethoprim resistance in Streptococcus pneumoniae.Semantic proximity Read ↗

DHFR Mutants Modulate Their Synchronized Dynamics with the Substrate by Shifting Hydrogen Bond Occupancies.Semantic proximity Read ↗

Trimethoprim Resistance of Dihydrofolate Reductase Variants from Clinical Isolates of Pneumocystis jiroveciiSemantic proximity Read ↗

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