ReviewCellular and molecular life sciences : CMLS2016
Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.
Review in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 108 citations in OpenAlex.
- Mangiferin as a Polyphenolic Scaffold for Enzyme Targeted Molecular Regulation of Carbohydrate Hydrolyzing Enzymes in Diabetes Management.Applied biochemistry and biotechnology · 2026Article
- Glucansucrases as versatile biocatalysts: structural insights, synthesis of emerging prebiotic oligosaccharides, and their functional roles in food matrices.Antonie van Leeuwenhoek · 2026Review
- Soybean α-Amylase Gene Family: Structure and Expression in Response to Abiotic Stresses.International journal of molecular sciences · 2026Article
- Evolution of the α-Glucosidase Gene Family in Apoidea.Ecology and evolution · 2026Article
- Effects of Dietary Dandelion Supplementation on Ruminal Morphology, Fermentation, Microbiome, and Inflammation in Lambs Under High-Concentrate Feeding.Animals : an open access journal from MDPI · 2026Article
- Proteomic profiling of amylases secreted by3 Biotech · 2026Article
- Recombinant Expression and Characterization of a New Endogenous and Halophilic GH13_5 Subfamily α-Amylase from Paenibacillus pabuli.Applied biochemistry and biotechnology · 2026Article
- Degradation of Resistant α-1,4-glucan by Vaginal Gardnerella Species is Associated with Bacterial Vaginosis.Current microbiology · 2025Article
- Probing the function of C-terminal region of recombinant α-amylase BmaN1 fromMicrobiology spectrum · 2024Article
- Two newly established and mutually related subfamilies GH13_48 and GH13_49 of the α-amylase family GH13.Applied microbiology and biotechnology · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Advances in Amylases-What's Going on?Molecules (Basel, Switzerland) · 2023Article
- Characterization of cold-active trehalose synthase from Pseudarthrobacter sp. for trehalose bioproduction.Bioresources and bioprocessing · 2023Article
- Identification and Characterization of Novel Malto-Oligosaccharide-Forming Amylase AmyCf fromFoods (Basel, Switzerland) · 2023Article
- Whole genome sequencing and the lignocellulose degradation potential of Bacillus subtilis RLI2019 isolated from the intestine of termites.Biotechnology for biofuels and bioproducts · 2023Article
- Binding Specificity of a Novel Cyclo/Maltodextrin-Binding Protein and Its Role in the Cyclodextrin ABC Importer System from Thermoanaerobacterales.Molecules (Basel, Switzerland) · 2023Article
- Article
- 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
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The α-amylase is a ubiquitous starch hydrolase catalyzing the cleavage of the α-1,4-glucosidic bonds in an endo-fashion. Various α-amylases originating from different taxonomic sources may differ from each other significantly in their exact substrate preference and product profile. Moreover, it also seems to be clear that at least two different amino acid sequences utilizing two different catalytic machineries have evolved to execute the same α-amylolytic specificity. The two have been classified in the Cabohydrate-Active enZyme database, the CAZy, in the glycoside hydrolase (GH) families GH13 and GH57. While the former and the larger α-amylase family GH13 evidently forms the clan GH-H with the families GH70 and GH77, the latter and the smaller α-amylase family GH57 has only been predicted to maybe define a future clan with the family GH119. Sequences and several tens of enzyme specificities found throughout all three kingdoms in many taxa provide an interesting material for evolutionarily oriented studies that have demonstrated remarkable observations. This review emphasizes just the three of them: (1) a close relatedness between the plant and archaeal α-amylases from the family GH13; (2) a common ancestry in the family GH13 of animal heavy chains of heteromeric amino acid transporter rBAT and 4F2 with the microbial α-glucosidases; and (3) the unique sequence features in the primary structures of amylomaltases from the genus Borrelia from the family GH77. Although the three examples cannot represent an exhaustive list of exceptional topics worth to be interested in, they may demonstrate the importance these enzymes possess in the overall scientific context.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.