ArticleJournal of molecular modeling2013
Sequence and structural investigation of a novel psychrophilic α-amylase from Glaciozyma antarctica PI12 for cold-adaptation analysis.
Article in Journal of molecular modeling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- The Unusual Dominance of the Yeast GenusJournal of fungi (Basel, Switzerland) · 2023Article
- Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications.3 Biotech · 2021Review
- In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites.Molecules (Basel, Switzerland) · 2021Article
- 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
- Comparative modelling studies of fruit bromelain using molecular dynamics simulation.Journal of molecular modeling · 2020Article
- Enzymes from Marine Polar Regions and Their Biotechnological Applications.Marine drugs · 2019Review
- Molecular Cloning and Optimization for High Level Expression of Cold-Adapted Serine Protease from Antarctic Yeast Glaciozyma antarctica PI12.Enzyme research · 2014Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel α-amylase was isolated successfully from Glaciozyma antarctica PI12 using DNA walking and reverse transcription-polymerase chain reaction (RT-PCR) methods. The structure of this psychrophilic α-amylase (AmyPI12) from G. antarctica PI12 has yet to be studied in detail. A 3D model of AmyPI12 was built using a homology modelling approach to search for a suitable template and to generate an optimum target-template alignment, followed by model building using MODELLER9.9. Analysis of the AmyPI12 model revealed the presence of binding sites for a conserved calcium ion (CaI), non-conserved calcium ions (CaII and CaIII) and a sodium ion (Na). Compared with its template-the thermostable α-amylase from Bacillus stearothermophilus (BSTA)-the binding of CaII, CaIII and Na ions in AmyPI12 was observed to be looser, which suggests that the low stability of AmyPI12 allows the protein to work at different temperature scales. The AmyPI12 amino acid sequence and model were compared with thermophilic α-amylases from Bacillus species that provided the highest structural similarities with AmyPI12. These comparative studies will enable identification of possible determinants of cold adaptation.
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