ArticleThe protein journal2013
Cold-adapted RTX lipase from antarctic Pseudomonas sp. strain AMS8: isolation, molecular modeling and heterologous expression.
Article in The protein journal, 2013. 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, 29 citations in OpenAlex.
- Genomic and phenotypic characterization of AntarcticFrontiers in microbiology · 2026Article
- Catalytically active inclusion bodies of cold-adapted lipase: production and its industrial potential.AMB Express · 2025Article
- Templated folding of the RTX domain of the bacterial toxin adenylate cyclase revealed by single molecule force spectroscopy.Nature communications · 2022Article
- Gene cloning, heterologous expression, and partial characterization of a novel cold-adapted subfamily I.3 lipase from Pseudomonas fluorescence KE38.Scientific reports · 2020Article
- Article
- New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from PsychrophilicInternational journal of molecular sciences · 2019Article
- Isolation, Characterisation, and Lipase Production of a Cold-Adapted Bacterial StrainMolecules (Basel, Switzerland) · 2019Article
- Effects of Lid 1 Mutagenesis on Lid Displacement, Catalytic Performances and Thermostability of Cold-active Pseudomonas AMS8 Lipase in Toluene.Computational and structural biotechnology journal · 2019Article
- The Effect of N-Terminal Domain Removal towards the Biochemical and Structural Features of a Thermotolerant Lipase from an Antarctic Pseudomonas sp. Strain AMS3.International journal of molecular sciences · 2018Article
- The Role of Solvent-Accessible Leu-208 of Cold-Active Pseudomonas fluorescens Strain AMS8 Lipase in Interfacial Activation, Substrate Accessibility and Low-Molecular Weight Esterification in the Presence of Toluene.Molecules (Basel, Switzerland) · 2017Article
- Marine Metagenome as A Resource for Novel Enzymes.Genomics, proteomics & bioinformatics · 2015Review
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6 authors at 1 institution in 1 country.
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Abstract
A new strain of psychrophilic bacteria (designated strain AMS8) from Antarctic soil was screened for extracellular lipolytic activity and further analyzed using molecular approach. Analysis of 16S rDNA showed that strain AMS8 was similar to Pseudomonas sp. A lipase gene named lipAMS8 was successfully isolated from strain AMS8, cloned, sequenced and overexpressed in Escherichia coli. Sequence analysis revealed that lipAMS8 consist of 1,431 bp nucleotides that encoded a polypeptide consisting of 476 amino acids. It lacked an N-terminal signal peptide and contained a glycine- and aspartate-rich nonapeptide sequence at the C-terminus, which are known to be the characteristics of repeats-in-toxin bacterial lipases. Furthermore, the substrate binding site of lipAMS8 was identified as S(207), D(255) and H(313), based on homology modeling and multiple sequence alignment. Crude lipase exhibited maximum activity at 20 °C and retained almost 50 % of its activity at 10 °C. The molecular weight of lipAMS8 was estimated to be 50 kDa via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal expression level was attained using the recombinant plasmid pET32b/BL21(DE3) expressed at 15 °C for 8 h, induced by 0.1 mM isopropyl β-D thiogalactoside (IPTG) at E. coli growth optimal density of 0.5.
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