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

A fluorescent probe-labeled Escherichia coli aspartate transcarbamoylase that monitors the allosteric conformational state.

The Journal of biological chemistry - 9 Jan 2004

West Jay M, Tsuruta Hiro, Kantrowitz Evan R

Abstract excerpt

A new system has been developed capable of monitoring conformational changes of the 240s loop of aspartate transcarbamoylase, which are tightly correlated with the quaternary structural transition, with high sensitivity in solution. Pyrene, a fluorescent probe, was conjugated to residue 241 in the 240s loop of aspartate transcarbamoylase to monitor changes in conformation by fluorescence spectroscopy. Pyrene...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Site
Share to Aspartate Carbamoyltransferase

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

Share to Catalysis

Share to Fluorescent Dyes

Share to Pyrenes

Share to Scattering, Radiation

Share to Spectrometry, Fluorescence

Share to X-Rays

Source

Identifiers

PMID: 14581486
DOI: 10.1074/jbc.M304018200

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

A fluorescent probe-labeled Escherichia coli aspartate transcarbamoylase that monitors the allosteric conformational state.PMID 14581486Read ↗

Monitoring the transition from the T to the R state in E.coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant enzyme in four distinct allosteric states.Semantic proximity Read ↗

Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation.Semantic proximity Read ↗

Comparison of two T-state structures of regulatory-chain mutants of Escherichia coli aspartate transcarbamoylase suggests that His20 and Asp19 modulate the response to heterotropic effectors.Semantic proximity Read ↗

Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle.Semantic proximity Read ↗

Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.Semantic proximity Read ↗

L-aspartate association contributes to rate limitation and induction of the T-->R transition in Escherichia coli aspartate transcarbamoylase. Equilibrium exchanges and kinetic isotope effects with a Vmax-enhanced mutant, Asp-236-->Ala.Semantic proximity Read ↗

Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.Semantic proximity Read ↗

Importance of domain closure for the catalysis and regulation of Escherichia coli aspartate transcarbamoylase.Semantic proximity Read ↗

Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase.Semantic proximity Read ↗

Integrated allosteric regulation in the S. cerevisiae carbamylphosphate synthetase - aspartate transcarbamylase multifunctional protein.Semantic proximity Read ↗

Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine.Semantic proximity Read ↗

The central loop of Escherichia coli glutamine synthetase is flexible and functionally passive.Semantic proximity Read ↗

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