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

Mutagenesis of solvent-exposed amino acids in Photinus pyralis luciferase improves thermostability and pH-tolerance.

The Biochemical journal - 15 Jul 2006

Law G H Erica, Gandelman Olga A, Tisi Laurence C, Lowe Christopher R, Murray James A H

Abstract excerpt

Firefly luciferase catalyses a two-step reaction, using ATP-Mg2+, firefly luciferin and molecular oxygen as substrates, leading to the efficient emission of yellow-green light. We report the identification of novel luciferase mutants which combine improved pH-tolerance and thermostability and that retain the specific activity of the wild-type enzyme. These were identified by the mutagenesis of solvent-exposed...

Read the complete abstract on PubMed

Topics

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

Share to Hot Temperature
Share to Hydrogen-Ion Concentration

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

Share to Kinetics

Share to Models, Molecular

Share to Mutagenesis

Share to Mutation

Share to Protein Engineering

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 16551268
DOI: 10.1042/BJ20051847
PMCID: PMC1513288

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

Mutagenesis of solvent-exposed amino acids in Photinus pyralis luciferase improves thermostability and pH-tolerance.PMID 16551268Read ↗

A set of multicolored Photinus pyralis luciferase mutants for in vivo bioluminescence applications.Semantic proximity Read ↗

Thermostable red and green light-producing firefly luciferase mutants for bioluminescent reporter applications.Semantic proximity Read ↗

Improved thermostability of the North American firefly luciferase: saturation mutagenesis at position 354.Semantic proximity Read ↗

Design and characterization of novel trypsin-resistant firefly luciferases by site-directed mutagenesis.Semantic proximity Read ↗

Mutation of a protease-sensitive region in firefly luciferase alters light emission properties.Semantic proximity Read ↗

Increase in bioluminescence intensity of firefly luciferase using genetic modification.Semantic proximity Read ↗

Strategy of mutual compensation of green and red mutants of firefly luciferase identifies a mutation of the highly conservative residue E457 with a strong red shift of bioluminescence.Semantic proximity Read ↗

Discovery of Red-Shifting Mutations in Firefly Luciferase Using High-Throughput Biochemistry.Semantic proximity Read ↗

Mutation of conserved residues K329 and R330 on the surface of firefly luciferase: Effect on proteolytic degradation.Semantic proximity Read ↗

Histidine substitution in the most flexible fragments of firefly luciferase modifies its thermal stability.Semantic proximity Read ↗

Triple substitution G216N/A217L/S398M leads to the active and thermostable Luciola mingrelica firefly luciferase.Semantic proximity Read ↗

Delicate balance of electrostatic interactions and disulfide bridges in thermostability of firefly luciferase.Semantic proximity Read ↗

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