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

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

The Journal of biological chemistry - 20 Nov 1998

Sahay N, Guy H I, Liu X, Evans D R

Abstract excerpt

Carbamoyl-phosphate synthetase (CPSase) consists of a 120-kDa synthetase domain (CPS) that makes carbamoyl phosphate from ATP, bicarbonate, and ammonia usually produced by a separate glutaminase domain. CPS is composed of two subdomains, CPS.A and CPS.B. Although CPS.A and CPS.B have specialized functions in intact CPSase, the separately cloned subdomains can catalyze carbamoyl phosphate synthesis. This report...

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 Escherichia coli
Share to Ligands

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

Share to Mammals

Share to Models, Molecular

Share to Mutation

Share to Recombinant Fusion Proteins

Share to Sequence Deletion

Source

Identifiers

PMID: 9813025
DOI: 10.1074/jbc.273.47.31195

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

Regulation of an Escherichia coli/mammalian chimeric carbamoyl-phosphate synthetase.PMID 9813025Read ↗

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 ↗

Access to the carbamate tunnel of carbamoyl phosphate synthetase.Semantic proximity Read ↗

Cloning, expression, and functional interactions of the amidotransferase domain of mammalian CAD carbamyl phosphate synthetase.Semantic proximity Read ↗

Deconstruction of the catalytic array within the amidotransferase subunit of carbamoyl phosphate synthetase.Semantic proximity Read ↗

The function of Glu338 in the catalytic triad of the carbamoyl phosphate synthetase amidotransferase domain.Semantic proximity Read ↗

Understanding carbamoyl phosphate synthetase deficiency: impact of clinical mutations on enzyme functionality.Semantic proximity Read ↗

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 ↗

Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia.Semantic proximity Read ↗

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

Interdomain signaling in glutamine phosphoribosylpyrophosphate amidotransferase.Semantic proximity Read ↗

Dissection of the functional domains of Escherichia coli carbamoyl phosphate synthetase by site-directed mutagenesis.Semantic proximity Read ↗

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