ArticleExtremophiles : life under extreme conditions2020
A new GH13 subfamily represented by the α-amylase from the halophilic archaeon Haloarcula hispanica.
Article in Extremophiles : life under extreme conditions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 24 citations in OpenAlex.
- The role of N185D substitution in enhancing activity of BaqA∆C α-amylase.Scientific reports · 2025Article
- Therapeutic potential of a newly isolated bacteriophage against multi-drug resistant Enterococcus faecalis infections: in vitro and in vivo characterization.BMC microbiology · 2025Article
- Host-driven remodeling of rumen microbiota supports lactation metabolism in buffalo.Frontiers in microbiology · 2025Article
- Article
- Two newly established and mutually related subfamilies GH13_48 and GH13_49 of the α-amylase family GH13.Applied microbiology and biotechnology · 2024Article
- Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.International journal of molecular sciences · 2023Review
- Characterization of an Amylolytic Enzyme from Massilia timonae of the GH13_19 Subfamily with Mixed Maltogenic and CGTase Activity.Applied biochemistry and biotechnology · 2023Article
- A Novel Subfamily GH13_46 of the α-Amylase Family GH13 Represented by the Cyclomaltodextrinase fromMolecules (Basel, Switzerland) · 2022Article
- Article
- Structural and functional adaptation in extremophilic microbial α-amylases.Biophysical reviews · 2022Review
- 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
- Aspects and Recent Trends in Microbial α-Amylase: a Review.Applied biochemistry and biotechnology · 2021Review
- A novel pH and thermo-tolerant halophilic alpha-amylase from moderate halophile Nesterenkonia sp. strain F: gene analysis, molecular cloning, heterologous expression and biochemical characterization.Archives of microbiology · 2021Article
- Molecular strategies to enhance stability and catalysis of extremophile-derived α-amylase using computational biology.Extremophiles : life under extreme conditions · 2021Review
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2 authors at 1 institution in 1 country.
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Abstract
α-Amylase catalyzes the endohydrolysis of α-1,4-glucosidic linkages in starch and related α-glucans. In the CAZy database, most α-amylases have been classified into the family GH13 counting at present more than 80,000 sequences and ~ 30 different enzyme specificities. The family has already been divided into 42 subfamilies, but additional subfamilies are still emerging. The present bioinformatics study was undertaken in an effort to propose a novel GH13 subfamily around the experimentally characterized α-amylase from the halophilic archaeon Haloarcula hispanica, which until now has not been assigned to any GH13 subfamily. The in silico analysis resulted in collecting a convincing group of putative haloarchaeal α-amylase homologues sharing sequence similarities mainly in their conserved sequence regions (CSRs) and forming a cluster in the evolutionary tree, which is well separated from representatives of established GH13 subfamilies. One of the most exclusive sequence features of the novel GH13 subfamily is the tyrosine (Tyr79 in H. hispanica α-amylase numbering) succeeding the glycine at the beginning of the CSR-VI at the β2 strand of the catalytic TIM-barrel. Evolutionarily, the novel GH13 α-amylase subfamily was most closely related to two clusters of GH13 subfamilies with the specificity of α-amylase, i.e. subfamilies GH13_5, 6 and 7 as well as GH13_15, 24, 27 and 28.
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