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

Separation of inhibition and activation of the allosteric yeast chorismate mutase.

Proceedings of the National Academy of Sciences of the United States of America - 17 Mar 1998

Schnappauf G, Lipscomb W N, Braus G H

Abstract excerpt

Yeast chorismate mutase (EC 5.4.99.5) shows homotropic activation by the substrate, allosteric activation by tryptophan, and allosteric inhibition by tyrosine. In this study mutants of chorismate mutase have been found that remain sensitive to one allosteric effector (tryptophan) but insensitive to the other (tyrosine). These mutations are located in the catalytic domain: loop 220s (212-226) and helix 12...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Activation
Share to Models, Biological
Share to Models, Molecular

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

Share to Mutation

Share to Protein Structure, Secondary

Share to Saccharomyces cerevisiae

Share to Tryptophan

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 9501182
DOI: 10.1073/pnas.95.6.2868
PMCID: PMC19661

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

Separation of inhibition and activation of the allosteric yeast chorismate mutase.PMID 9501182Read ↗

Yeast allosteric chorismate mutase is locked in the activated state by a single amino acid substitution.Semantic proximity Read ↗

Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures.Semantic proximity Read ↗

Structural evolution of differential amino acid effector regulation in plant chorismate mutases.Semantic proximity Read ↗

Coevolution of transcriptional and allosteric regulation at the chorismate metabolic branch point of Saccharomyces cerevisiae.Semantic proximity Read ↗

Feedback inhibition of chorismate mutase/prephenate dehydrogenase (TyrA) of Escherichia coli: generation and characterization of tyrosine-insensitive mutants.Semantic proximity Read ↗

Regulation of chorismate mutase in Saccharomyces cerevisiae.Semantic proximity Read ↗

Mutations in the regulatory subunit of yeast acetohydroxyacid synthase affect its activation by MgATP.Semantic proximity Read ↗

Allosteric communication between the pyridoxal 5'-phosphate (PLP) and heme sites in the H2S generator human cystathionine β-synthase.Semantic proximity Read ↗

Transcriptional activator LEU3 of yeast. Mapping of the transcriptional activation function and significance of activation domain tryptophans.Semantic proximity Read ↗

The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors.Semantic proximity Read ↗

Residue N84 of yeast cystathionine beta-synthase is a determinant of reaction specificity.Semantic proximity Read ↗

Evolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation.Semantic proximity Read ↗

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