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

The role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences - 29 Aug 2006

Wang Lin, Goodey Nina M, Benkovic Stephen J, Kohen Amnon

Abstract excerpt

Residues M42 and G121 of Escherichia coli dihydrofolate reductase (ecDHFR) are on opposite sides of the catalytic centre (15 and 19 A away from it, respectively). Theoretical studies have suggested that these distal residues might be part of a dynamics network coupled to the reaction catalysed at the active site. The ecDHFR mutant G121V has been extensively studied and appeared to have a significant effect on...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Escherichia coli

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

Share to Hydrogen

Share to Kinetics

Share to Models, Chemical

Share to Structure-Activity Relationship

Share to Temperature

Share to Tetrahydrofolate Dehydrogenase

Source

Open in PubMed Open full text

Identifiers

PMID: 16873118
DOI: 10.1098/rstb.2006.1871
PMCID: PMC1647312

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

The role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.PMID 16873118Read ↗

Effects of a distal mutation on active site chemistry.Semantic proximity Read ↗

Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.Semantic proximity Read ↗

Effects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reaction.Semantic proximity Read ↗

Connecting protein conformational dynamics with catalytic function as illustrated in dihydrofolate reductase.Semantic proximity Read ↗

Effect of Asp122 Mutation on the Hydride Transfer in E. coli DHFR Demonstrates the Goldilocks of Enzyme Flexibility.Semantic proximity Read ↗

Hydride transfer catalysed by Escherichia coli and Bacillus subtilis dihydrofolate reductase: coupled motions and distal mutations.Semantic proximity Read ↗

A remote mutation affects the hydride transfer by disrupting concerted protein motions in thymidylate synthase.Semantic proximity Read ↗

Protein motions during catalysis by dihydrofolate reductases.Semantic proximity Read ↗

Correlated motion and the effect of distal mutations in dihydrofolate reductase.Semantic proximity Read ↗

Preservation of protein dynamics in dihydrofolate reductase evolution.Semantic proximity Read ↗

The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase.Semantic proximity Read ↗

The role of the Met20 loop in the hydride transfer in Escherichia coli dihydrofolate reductase.Semantic proximity Read ↗

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