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

Characterization of the low-temperature activity of Sulfolobus tokodaii glucose-1-dehydrogenase mutants.

Journal of bioscience and bioengineering - 1 Oct 2014

Sugii Taisuke, Akanuma Satoshi, Yagi Sota, Yagyu Kazuki, Shimoda Yukiko, Yamagishi Akihiko

Abstract excerpt

Thermophilic enzymes are potentially useful for industrial processes because they are generally more stable than are mesophilic or psychrophilic enzymes. However, a crucial drawback for their use in such processes is that most thermophilic enzymes are nearly inactive at moderate and low temperatures. We have previously proposed that modulation of the coenzyme-binding pocket of thermophilic dehydrogenases can...

Read the complete abstract on PubMed

Topics

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

Share to Archaeal Proteins
Share to Biocatalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cold Temperature

Share to Isoleucine

Share to Structural Homology, Protein

Share to Sulfolobus

Share to Valine

Source

Identifiers

PMID: 24742629
DOI: 10.1016/j.jbiosc.2014.03.002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of the low-temperature activity of Sulfolobus tokodaii glucose-1-dehydrogenase mutants.PMID 24742629Read ↗

Substitutions of coenzyme-binding, nonpolar residues improve the low-temperature activity of thermophilic dehydrogenases.Semantic proximity Read ↗

Evaluation of Three Mutations in Codon 385 of Glucose-6-Phosphate Dehydrogenase via Biochemical and In Silico Analysis.Semantic proximity Read ↗

Random mutagenesis improves the low-temperature activity of the tetrameric 3-isopropylmalate dehydrogenase from the hyperthermophile Sulfolobus tokodaii.Semantic proximity Read ↗

High-temperature behavior of hyperthermostable Thermotoga maritima xylanase XYN10B after designed and evolved mutations.Semantic proximity Read ↗

The stability of G6PD is affected by mutations with different clinical phenotypes.Semantic proximity Read ↗

A hydrogen-bonding network in mammalian sorbitol dehydrogenase stabilizes the tetrameric state and is essential for the catalytic power.Semantic proximity Read ↗

Biochemical and structural characterization of quinoprotein aldose sugar dehydrogenase from Thermus thermophilus HJ6: Mutational analysis of Tyr156 in the substrate-binding site.Semantic proximity Read ↗

In silico protein engineering shows that novel mutations affecting NAD+ binding sites may improve phosphite dehydrogenase stability and activity.Semantic proximity Read ↗

Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc.Semantic proximity Read ↗

From hyperthermophiles to psychrophiles: the structural basis of temperature stability of the amino acid dehydrogenases.Semantic proximity Read ↗

Ionic network at the C-terminus of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus: Functional role in the quaternary structure thermal stabilization.Semantic proximity Read ↗

Engineering the cofactor specificity of an alcohol dehydrogenase via single mutations or insertions distal to the 2'-phosphate group of NADP(H).Semantic proximity Read ↗

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