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

Cold inactivation and dissociation into dimers of Escherichia coli tryptophanase and its W330F mutant form.

Biochimica et biophysica acta - 19 May 1998

Erez T, Gdalevsky GYa, Torchinsky Y M, Phillips R S, Parola A H

Abstract excerpt

The kinetics and mechanism of reversible cold inactivation of the tetrameric enzyme tryptophanase have been studied. Cold inactivation is shown to occur slowly in the presence of K+ ions and much faster in their absence. The W330F mutant tryptophanase undergoes rapid cold inactivation even in the presence of K+ ions. In all cases the inactivation is accompanied by a decrease of the coenzyme 420-nm CD and...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Chromatography, High Pressure Liquid

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

Share to Cold Temperature

Share to Dimerization

Share to Enzyme Repression

Share to Escherichia coli

Share to Mutation

Share to Potassium

Source

Identifiers

PMID: 9659398
DOI: 10.1016/s0167-4838(98)00031-4

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

Cold inactivation and dissociation into dimers of Escherichia coli tryptophanase and its W330F mutant form.PMID 9659398Read ↗

Cold-induced enzyme inactivation: how does cooling lead to pyridoxal phosphate-aldimine bond cleavage in tryptophanase?Semantic proximity Read ↗

A structural view of the dissociation of Escherichia coli tryptophanase.Semantic proximity Read ↗

New insights into the mechanism of enzymatic chlorination of tryptophan.Semantic proximity Read ↗

Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase.Semantic proximity Read ↗

The dead-end elimination method, tryptophan rotamers, and fluorescence lifetimes.Semantic proximity Read ↗

Reversible dissociation/association of D-amino acid transaminase subunits: properties of isolated active dimers and inactive monomers.Semantic proximity Read ↗

Mutation of Trp(93) of MauG to tyrosine causes loss of bound Ca(2+) and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis.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 ↗

Kinetic and thermodynamic studies of the folding/unfolding of a tryptophan-containing mutant of ribonuclease A.Semantic proximity Read ↗

Thermal repair of tryptophan synthase mutations in a regulatory intersubunit salt bridge. Evidence from arrhenius plots, absorption spectra, and primary kinetic isotope effects.Semantic proximity Read ↗

Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein.Semantic proximity Read ↗

Homodimers of mutant tryptophan synthase alpha-subunits in Escherichia coli.Semantic proximity Read ↗

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