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

[Mechanism of functioning of aminoacyl-tRNA-synthetases].

Molekuliarnaia biologiia - 1 Jan 2000

Malygin E G, Kiselev L L

Abstract excerpt

The article reviews the data available concerning the kinetics of reactions catalysed by eukaryotic and procaryotic aminoacyl-tRNA synthetases (E.C.6.1.1). It is shown that most of these enzymes operate in accordance with the flip-flop mechanism although individual variations do exist. It is stressed that a simplified kinetic approach of Cleland is inappropriate if applied to the aminoacyl-tRNA synthetases where...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acyl-tRNA Synthetases
Share to Kinetics
Share to Models, Biological

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

Share to Mutation

Share to Protein Biosynthesis

Share to RNA, Transfer

Share to RNA, Transfer, Amino Acyl

Share to Substrate Specificity

Source

Identifiers

PMID: 6390174

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

[Mechanism of functioning of aminoacyl-tRNA-synthetases].PMID 6390174Read ↗

Mechanistic perspectives on anti-aminoacyl-tRNA synthetase syndromeSemantic proximity Read ↗

Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots.Semantic proximity Read ↗

A dynamical model of programmed -1 ribosomal frameshifting.Semantic proximity Read ↗

[Exploring the "motion" = "function" of the ribosomal A-site molecular switch].Semantic proximity Read ↗

Seryl-tRNA synthetase from Escherichia coli: functional evidence for cross-dimer tRNA binding during aminoacylation.Semantic proximity Read ↗

[Molecular mechanisms of spontaneous transversions and transitions].Semantic proximity Read ↗

[Biogenesis and secretion of alkaline phosphatase and its mutants in Escherichia coli. III. Substitution of N-terminal amino acids of alkaline phosphatase affect its biogenesis].Semantic proximity Read ↗

[Enzymatic mechanisms of compensation of deleterious mutations].Semantic proximity Read ↗

Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases.Semantic proximity Read ↗

[Structural and functional characteristics of ATP-dependent Lon-proteinase from Escherichia coli].Semantic proximity Read ↗

Impaired in vitro kinetics of EF-Tu mutant Aa.Semantic proximity Read ↗

Modelling efficiency, error propagation and the effect of error-enhancing drugs in protein synthesis.Semantic proximity Read ↗

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