ArticleExtremophiles : life under extreme conditions2011
In silico characterization of thermostable lipases.
Article in Extremophiles : life under extreme conditions, 2011. 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, 25 citations in OpenAlex.
- Molecular Adaptations of Thermophilic Proteins-From Mechanistic Understanding to Machine Learning Approaches.ChemistryOpen · 2026Review
- Further Characterization of Lipase B from Ustilago maydis Expressed in Pichia pastoris: a Member of the Candida antarctica Lipase B-like Superfamily.Applied biochemistry and biotechnology · 2025Article
- Identification of a Novel Lipase with AHSMG Pentapeptide in Hypocreales and Glomerellales Filamentous Fungi.International journal of molecular sciences · 2022Article
- Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) fromJournal of biological research (Thessalonike, Greece) · 2018Article
- Article
- Characterization of a Novel Alkalophilic Lipase From Aneurinibacillus thermoaerophilus: Lid Heterogeneity and Assignment to Family I.5.The protein journal · 2017Article
- Directed Evolution of Recombinant C-Terminal Truncated Staphylococcus epidermidis Lipase AT2 for the Enhancement of Thermostability.International journal of molecular sciences · 2017Article
- Multifactorial level of extremostability of proteins: can they be exploited for protein engineering?Extremophiles : life under extreme conditions · 2017Review
- Bioprospecting hot spring metagenome: lipase for the production of biodiesel.Environmental science and pollution research international · 2017Article
- Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes.Microorganisms · 2015Review
- cDNA cloning and molecular modeling of procerain B, a novel cysteine endopeptidase isolated from Calotropis procera.PloS one · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermostable lipases are of high priority for industrial applications as they are endowed with the capability of carrying out diversified reactions at elevated temperatures. Extremophiles are their potential source. Sequence and structure annotation of thermostable lipases can elucidate evolution of lipases from their mesophilic counterparts with enhanced thermostability hence better industrial potential. Sequence analysis highlighted the conserved residues in bacterial and fungal thermostable lipases. Higher frequency of AXXXA motif and poly Ala residues in lid domain of thermostable Bacillus lipases were distinguishing characteristics. Comparison of amino acid composition among thermostable and mesostable lipases brought into light the role of neutral, charged and aromatic amino acid residues in enhancement of thermostability. Structural annotation of thermostable lipases with that of mesostable lipases revealed some striking features which are increment of gamma turns in thermostable lipases; being first time reported in our paper, longer beta strands, lesser beta-branched residues in helices, increase in charged-neutral hydrogen bonding pair, hydrophobic-hydrophobic contact and differences in the N-cap and C-cap residues of the α helices. Conclusively, it can be stated that subtle changes in the arrangement of amino acid residues in the tertiary structure of lipases contributes to enhanced thermostability.
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