ArticleBioengineered2017
A glutathione peroxidase from Antarctic psychrotrophic bacterium Pseudoalteromonas sp. ANT506: Cloning and heterologous expression of the gene and characterization of recombinant enzyme.
Article in Bioengineered, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Untangling the adaptive strategies of thermophilic bacterium Anoxybacillus rupiensis TPH1 under low temperature.Extremophiles : life under extreme conditions · 2024Article
- Biochemical and Functional Profiling of Thioredoxin-Dependent Cytosolic GPX-like Proteins inBiomolecules · 2024Article
- Actinobacterial peroxidase-mediated biodeterioration of hazardous explosive, 2, 4, 6, trinitrophenol by in silico and in vitro approaches.Environmental geochemistry and health · 2024Article
- Antimicrobial Coatings for Medical Textiles via Reactive Organo-Selenium Compounds.Molecules (Basel, Switzerland) · 2023Article
- Comprehensive insights on environmental adaptation strategies in Antarctic bacteria and biotechnological applications of cold adapted molecules.Frontiers in microbiology · 2023Review
- Article
- Metabolic regulation of ethanol-type fermentation of anaerobic acidogenesis at different pH based on transcriptome analysis ofBiotechnology for biofuels · 2020Article
- Stress-Based Production, and Characterization of Glutathione Peroxidase and Glutathione S-Transferase Enzymes FromFrontiers in bioengineering and biotechnology · 2020Article
- Enzymes from Marine Polar Regions and Their Biotechnological Applications.Marine drugs · 2019Review
- Article
- A Novel Cold-Adapted Leucine Dehydrogenase from Antarctic Sea-Ice BacteriumMarine drugs · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A glutathione peroxidase (GPx) gene, designated as PsGPx, was cloned from Antarctic psychrotrophic bacterium Pseudoalteromonas sp. ANT506 and expressed in Escherichia coli. The full-length PsGPx contained a 585-bp encoding 194 amino acids with predicted molecular masses of approx. 21.7 kDa. Multiple sequence alignments revealed that PsGPx belonged to the thioredoxin-like superfamily. PsGPx was heterologously overexpressed in E. coli, purified and characterized. The maximum catalytic temperature and pH value for recombinant PsGPx (rPsGPx) were 30°C and pH 9.0, respectively. rPsGPx retained 45% of the maximum activity at 0°C and exhibited high thermolability with a half-life of approx. 40 min at 40°C. In addition, the enzymatic activity of rPsGPx was still manifested under 3 M NaCl. The K
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