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

Selection and analysis of non-interactive mutants in the Escherichia coli tryptophan synthase alpha subunit.

Molecular & general genetics : MGG - 1 May 1992

Swift S, Kuhn J, Stewart G S

Abstract excerpt

The inherent infidelity of Taq DNA polymerase in the polymerase chain reaction was exploited to produce random mutations in the trp A gene. Screening of the resulting clones allowed selection of non-interactive mutant alpha subunits retaining their intrinsic catalytic activity. Two single changes responsible for this phenotype were identified by DNA sequencing as: alpha 126 valine (GTG)----glutamic acid (GAG) and...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to DNA Mutational Analysis
Share to Escherichia coli

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

Share to Molecular Sequence Data

Share to Mutation

Share to Plasmids

Share to Polymerase Chain Reaction

Share to Protein Conformation

Source

Identifiers

PMID: 1603055
DOI: 10.1007/BF00587570

Genes

AGA

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

Selection and analysis of non-interactive mutants in the Escherichia coli tryptophan synthase alpha subunit.PMID 1603055Read ↗

Enzymatic properties of mutant Escherichia coli tryptophan synthase alpha-subunits.Semantic proximity Read ↗

Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.Semantic proximity Read ↗

The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis.Semantic proximity Read ↗

A Molecular Dynamics Simulation Study of the Effects of βGln114 Mutation on the Dynamic Behavior of the Catalytic Site of the Tryptophan Synthase.Semantic proximity Read ↗

Recombinant protein production driven by the tryptophan promoter is tightly controlled in ICONE 200, a new genetically engineered E. coli mutant.Semantic proximity Read ↗

A molecular characterization of spontaneous frameshift mutagenesis within the trpA gene of Escherichia coli.Semantic proximity Read ↗

The conserved active site motif A of Escherichia coli DNA polymerase I is highly mutable.Semantic proximity Read ↗

Design and evaluation of a tryptophanless RecA protein with wild type activity.Semantic proximity Read ↗

Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli.Semantic proximity Read ↗

A single amino acid switch within the "hinge" region of the tryptophan synthase beta subunit of Escherichia coli that leads to diminished association with alpha subunit and arrested conversion of ESII to product.Semantic proximity Read ↗

Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein.Semantic proximity Read ↗

A dispensable peptide from Acidithiobacillus ferrooxidans tryptophanyl-tRNA synthetase affects tRNA binding.Semantic proximity Read ↗

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