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

Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis.

Nucleic acids research - 15 Sept 1999

Ibba M, Sever S, Praetorius-Ibba M, Söll D

Abstract excerpt

Sequence-specific interactions between aminoacyl-tRNA synthetases and their cognate tRNAs ensure both accurate RNA recognition and the efficient catalysis of aminoacylation. The effects of tRNA(Trp)variants on the aminoacylation reaction catalyzed by wild-type Escherichia coli tryptophanyl-tRNA synthe-tase (TrpRS) have now been investigated by stopped-flow fluorimetry, which allowed a pre-steady-state analysis to...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Monophosphate
Share to Catalysis
Share to Fluorescence

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

Share to Nucleic Acid Conformation

Share to RNA, Transfer, Amino Acyl

Share to RNA, Transfer, Gln

Share to Thermodynamics

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 10471730
DOI: 10.1093/nar/27.18.3631
PMCID: PMC148616

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

Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis.PMID 10471730Read ↗

Species-specific differences in the operational RNA code for aminoacylation of tRNA(Trp).Semantic proximity Read ↗

Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase.Semantic proximity Read ↗

Role of tRNA amino acid-accepting end in aminoacylation and its quality control.Semantic proximity Read ↗

Tertiary structure base pairs between D- and TpsiC-loops of Escherichia coli tRNA(Leu) play important roles in both aminoacylation and editing.Semantic proximity Read ↗

An active role for tRNA in decoding beyond codon:anticodon pairing.Semantic proximity Read ↗

Association between Archaeal prolyl- and leucyl-tRNA synthetases enhances tRNA(Pro) aminoacylation.Semantic proximity Read ↗

The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation.Semantic proximity Read ↗

Three G.C base pairs required for the efficient aminoacylation of tRNATrp by tryptophanyl-tRNA synthetase from Bacillus subtilis.Semantic proximity Read ↗

Substrate selection by aminoacyl-tRNA synthetases.Semantic proximity Read ↗

The Roots of Genetic Coding in Aminoacyl-tRNA Synthetase Duality.Semantic proximity Read ↗

Human tryptophanyl-tRNA synthetase is switched to a tRNA-dependent mode for tryptophan activation by mutations at V85 and I311.Semantic proximity Read ↗

Transfer RNA determinants for translational editing by Escherichia coli valyl-tRNA synthetase.Semantic proximity Read ↗

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