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

Active site mutants of Escherichia coli citrate synthase. Effects of mutations on catalytic and allosteric properties.

The Journal of biological chemistry - 7 Jan 1994

Pereira D S, Donald L J, Hosfield D J, Duckworth H W

Abstract excerpt

We report properties of five active site mutants of Escherichia coli citrate synthase, in which histidine 264, aspartate 362, and phenylalanine 383 were replaced by alanines, and arginines 387 and 407 by leucines. All mutants have much lower turnover numbers than wild type enzyme; the strongest effect was with the arginine 387 mutant, perhaps because the substrate, oxaloacetate, binds in a different orientation....

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 Base Sequence

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

Share to Binding Sites

Share to Catalysis

Share to DNA, Bacterial

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Mutation

Source

Identifiers

PMID: 8276829

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

Active site mutants of Escherichia coli citrate synthase. Effects of mutations on catalytic and allosteric properties.PMID 8276829Read ↗

A mutant of Escherichia coli citrate synthase that affects the allosteric equilibrium.Semantic proximity Read ↗

Mutation of amino acids thought to polarize the oxaloacetate carbonyl in citrate synthase severely reduces but does not abolish activity of the enzyme.Semantic proximity Read ↗

Mutation of essential catalytic residues in pig citrate synthase.Semantic proximity Read ↗

Ability of single-site mutants of citrate synthase to catalyze proton transfer from the methyl group of dethiaacetyl-coenzyme A, a non-thioester substrate analog.Semantic proximity Read ↗

Insights into the evolution of allosteric properties. The NADH binding site of hexameric type II citrate synthases.Semantic proximity Read ↗

Conversion of citrate synthase into citryl-CoA lyase as a result of mutation of the active-site aspartic acid residue to glutamic acid.Semantic proximity Read ↗

The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants.Semantic proximity Read ↗

On the catalytic mechanism of human ATP citrate lyase.Semantic proximity Read ↗

A single amino acid mutation enhances the thermal stability of Escherichia coli malate dehydrogenase.Semantic proximity Read ↗

Evolution of allosteric citrate binding sites on 6-phosphofructo-1-kinase.Semantic proximity Read ↗

Probing the roles of key residues in the unique regulatory NADH binding site of type II citrate synthase of Escherichia coli.Semantic proximity Read ↗

Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity.Semantic proximity Read ↗

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