ArticleJournal of computer-aided molecular design2014
Structural and functional analysis of a novel psychrophilic β-mannanase from Glaciozyma antarctica PI12.
Article in Journal of computer-aided molecular design, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 34 citations in OpenAlex.
- Structural Insights into Cold-Active Lipase from Glaciozyma antarctica PI12: Alphafold2 Prediction and Molecular Dynamics Simulation.Journal of molecular evolution · 2024Article
- Research and application progress of microbial β-mannanases: a mini-review.World journal of microbiology & biotechnology · 2024Review
- Cold Adaptation Strategies and the Potential of Psychrophilic Enzymes from the Antarctic Yeast,Journal of fungi (Basel, Switzerland) · 2021Review
- Psychrophilic enzymes: structural adaptation, pharmaceutical and industrial applications.Applied microbiology and biotechnology · 2021Review
- Molecular and biochemical characterizations of a new low-temperature active mannanase.Folia microbiologica · 2015Article
- Structural prediction of a novel laminarinase from the psychrophilic Glaciozyma antarctica PI12 and its temperature adaptation analysis.Journal of molecular modeling · 2015Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structure of a novel psychrophilic β-mannanase enzyme from Glaciozyma antarctica PI12 yeast has been modelled and analysed in detail. To our knowledge, this is the first attempt to model a psychrophilic β-mannanase from yeast. To this end, a 3D structure of the enzyme was first predicted using a threading method because of the low sequence identity (<30%) using MODELLER9v12 and simulated using GROMACS at varying low temperatures for structure refinement. Comparisons with mesophilic and thermophilic mannanases revealed that the psychrophilic mannanase contains longer loops and shorter helices, increases in the number of aromatic and hydrophobic residues, reductions in the number of hydrogen bonds and salt bridges and numerous amino acid substitutions on the surface that increased the flexibility and its efficiency for catalytic reactions at low temperatures.
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Registered trials
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