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

Epistasis effects of multiple ancestral-consensus amino acid substitutions on the thermal stability of glycerol kinase from Cellulomonas sp. NT3060.

Journal of bioscience and bioengineering - 1 May 2016

Fukuda Yasuhisa, Abe Asuka, Tamura Takashi, Kishimoto Takahide, Sogabe Atsushi, Akanuma Satoshi, Yokobori Shin-Ichi, Yamagishi Akihiko, Imada Katsumi, Inagaki Kenji

Abstract excerpt

Thermostable variants of the Cellulomonas sp. NT3060 glycerol kinase have been constructed by through the introduction of ancestral-consensus mutations. We produced seven mutants, each having an ancestral-consensus amino acid residue that might be present in the common ancestors of both bacteria and of archaea, and that appeared most frequently at the position of 17 glycerol kinase sequences in the multiple...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Biocatalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Consensus Sequence

Share to Enzyme Stability

Share to Epistasis, Genetic

Share to Half-Life

Share to Sequence Alignment

Share to Temperature

Source

Identifiers

PMID: 26493633
DOI: 10.1016/j.jbiosc.2015.09.011

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Epistasis effects of multiple ancestral-consensus amino acid substitutions on the thermal stability of glycerol kinase from Cellulomonas sp. NT3060.PMID 26493633Read ↗

Thermostability of ancestral mutants of Caldococcus noboribetus isocitrate dehydrogenase.Semantic proximity Read ↗

The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase.Semantic proximity Read ↗

Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree.Semantic proximity Read ↗

Random exchanges of non-conserved amino acid residues among four parental termite cellulases by family shuffling improved thermostability.Semantic proximity Read ↗

Parallel molecular mechanisms for enzyme temperature adaptation.Semantic proximity Read ↗

Utilization of low-stability variants in protein evolutionary engineering.Semantic proximity Read ↗

FireProt 2.0: web-based platform for the fully automated design of thermostable proteins.Semantic proximity Read ↗

[Improving the thermal stability of Bacillus subtilis lipase based on multiple computational design strategies].Semantic proximity Read ↗

Insights of conformational dynamics on catalytic activity in the computational stability design of Bacillus subtilis LipA.Semantic proximity Read ↗

A thermostable phospholipase C obtained by consensus designSemantic proximity Read ↗

Thermal Stabilization of a Bacterial Zn(II)-Dependent Phospholipase C through Consensus Sequence Design.Semantic proximity Read ↗

Additive effect of single amino acid replacements on the kinetic stability of β-glucosidase B.Semantic proximity Read ↗

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