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

Allosteric control of the oligomerization of carbamoyl phosphate synthetase from Escherichia coli.

Biochemistry - 18 Sept 2001

Kim J, Raushel F M

Abstract excerpt

Carbamoyl phosphate synthetase (CPS) from Escherichia coli is allosterically regulated by the metabolites ornithine, IMP, and UMP. Ornithine and IMP function as activators, whereas UMP is an inhibitor. CPS undergoes changes in the state of oligomerization that are dependent on the protein concentration and the binding of allosteric effectors. Ornithine and IMP promote the formation of an (alphabeta)4 tetramer...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Allosteric Regulation
Share to Gene Expression Regulation, Enzymologic

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

Share to Glutamine

Share to Ligands

Share to Models, Chemical

Share to Ornithine

Share to Uridine Monophosphate

Source

Identifiers

PMID: 11551199
DOI: 10.1021/bi011121u

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

Allosteric control of the oligomerization of carbamoyl phosphate synthetase from Escherichia coli.PMID 11551199Read ↗

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

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 ↗

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 ↗

Allosteric regulation in Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase revisited: association of concerted homotropic cooperative interactions and local heterotropic effects.Semantic proximity Read ↗

Evolution of oligomeric state through allosteric pathways that mimic ligand binding.Semantic proximity Read ↗

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

Positions 94-98 of the lactose repressor N-subdomain monomer-monomer interface are critical for allosteric communication.Semantic proximity Read ↗

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

Yeast epiarginase regulation, an enzyme-enzyme activity control: identification of residues of ornithine carbamoyltransferase and arginase responsible for enzyme catalytic and regulatory activities.Semantic proximity Read ↗

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