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 oligomerization of Escherichia coli carbamoyl phosphate synthetase and modulation by the allosteric effectors. A site-directed mutagenesis study.

FEBS letters - 30 Jan 2002

Mora Paz, Rubio Vicente, Cervera Javier

Abstract excerpt

We use site-directed mutagenesis to clarify the role of effector-mediated oligomerization changes on the modulation of the activity of Escherichia coli carbamoyl phosphate synthetase (CPS) by its allosteric activator ornithine and its inhibitor UMP. The regulatory domain mutations H975L, L990A and N992A abolished, and N987V decreased CPS oligomerization. The oligomerization domain mutation L421E prevented...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Chromatography, Gel

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

Share to Dimerization

Share to Molecular Weight

Share to Mutagenesis, Site-Directed

Share to Ornithine

Share to Protein Structure, Quaternary

Share to Uridine Monophosphate

Source

Identifiers

PMID: 11821039
DOI: 10.1016/s0014-5793(01)03246-x

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mechanism of oligomerization of Escherichia coli carbamoyl phosphate synthetase and modulation by the allosteric effectors. A site-directed mutagenesis study.PMID 11821039Read ↗

Allosteric control of the oligomerization of carbamoyl phosphate synthetase from Escherichia coli.Semantic proximity Read ↗

Site-directed mutagenesis of the regulatory domain of Escherichia coli carbamoyl phosphate synthetase identifies crucial residues for allosteric regulation and for transduction of the regulatory signals.Semantic proximity Read ↗

Dissection of the conduit for allosteric control of carbamoyl phosphate synthetase by ornithine.Semantic proximity Read ↗

A functional analysis of the allosteric nucleotide monophosphate binding site of carbamoyl phosphate synthetase.Semantic proximity Read ↗

Regulation of an Escherichia coli/mammalian chimeric carbamoyl-phosphate synthetase.Semantic proximity Read ↗

Serine 948 and threonine 1042 are crucial residues for allosteric regulation of Escherichia coli carbamoylphosphate synthetase and illustrate coupling effects of activation and inhibition pathways.Semantic proximity Read ↗

Steady-state kinetics and analysis of pH dependence on wild-type and a modified allosteric Pseudomonas aeruginosa ornithine carbamoyltransferase containing the replacement of glutamate 105 by alanine.Semantic proximity Read ↗

The site for the allosteric activator GTP of Escherichia coli UMP kinase.Semantic proximity Read ↗

Molecular mechanisms underlying allosteric behavior of Escherichia coli DgoR, a GntR/FadR family transcriptional regulator.Semantic proximity Read ↗

Altered oligomerization properties of N316 mutants of Escherichia coli TyrR.Semantic proximity Read ↗

Active site mutants of the "non-hydrolyzing" UDP-N-acetylglucosamine 2-epimerase from Escherichia coli.Semantic proximity Read ↗

Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.Semantic proximity Read ↗

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