ReviewCellular and molecular life sciences : CMLS2014
α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Review in Cellular and molecular life sciences : CMLS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
148 citing papers in PubMed, 391 citations in OpenAlex.
- Gluconeogenic compensation renders glycogen phosphorylase non-essential as an insecticidal target ineLife · 2026Article
- Article
- Enzymatic Modification of Potato Starch: Starch-Acting Enzyme Resources, Structure-Function Relationships and Value-Added Applications.Foods (Basel, Switzerland) · 2026Review
- Selective α-Amylase Inhibition by Plant Defensins: Structural Determinants, Engineering Strategies, and Translational Prospects.Probiotics and antimicrobial proteins · 2026Review
- Autoimmune processes and production of catalytically active antibodies-abzymes in prone to amyotrophic lateral sclerosis FUS(1-359) mice.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026Article
- Ingestible probes for breath-based monitoring of drug-metabolizing activity from the microbiome.Science advances · 2026Article
- Beyond Branching: Unlocking the Catalytic Versatility of Branching Enzymes for the Design of Diverse α-Glucan Structures.Molecules (Basel, Switzerland) · 2026Review
- Structure and Function of Honeybee α-Amylase of Glycoside Hydrolase Family 13 Subfamily 15.Molecules (Basel, Switzerland) · 2026Article
- In Silico Study of Potential Binding Sites of the Family GH126 Enzyme CPF_2247 fromMolecules (Basel, Switzerland) · 2026Article
- Design, synthesis, biological evaluation, and in silico characterization of chalcone derivatives as antidiabetic hits.Scientific reports · 2026Article
- Enzyme-Responsive Polymeric Drug Delivery Systems for the Treatment of Inflammatory Bowel Diseases: A Review.Polymers · 2026Review
- α-Amylase: Its Structure, Molecular Modification, and Application in the Food Field.Foods (Basel, Switzerland) · 2026Review
- TMT Proteomics-Based Study of Proteins and Pathways Associated with β-Glucan Degradation in Barley Germination.Metabolites · 2026Article
- Streptomyces aurantiaciflavus sp. nov., a novel actinomycete isolated from rhizosphere soil with antifungal activity and plant growth-promoting ability.The Journal of antibiotics · 2026Article
- Absolute hand determination of glycofibrils from natural sources in cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Recombinant Expression and Characterization of a New Endogenous and Halophilic GH13_5 Subfamily α-Amylase from Paenibacillus pabuli.Applied biochemistry and biotechnology · 2026Article
- New multitarget antidiabetic potential agents based on sulfaguanidine: design, synthesis, and biological evaluation.RSC advances · 2026Article
- Gut microbiome components predict response to neoadjuvant short-course radiotherapy followed by camrelizumab and chemotherapy in locally advanced rectal cancer (UNION): a prospective study.Frontiers in pharmacology · 2026Article
- Genomic insights into dominant lactic acid bacteria in spoiled plant-based meat analogues.Current research in food science · 2026Article
- Genome-wide identification and functional characterization of alpha-amylase genes in Litopenaeus vannamei.PloS one · 2026Article
88 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Amylase (EC 3.2.1.1) represents the best known amylolytic enzyme. It catalyzes the hydrolysis of α-1,4-glucosidic bonds in starch and related α-glucans. In general, the α-amylase is an enzyme with a broad substrate preference and product specificity. In the sequence-based classification system of all carbohydrate-active enzymes, it is one of the most frequently occurring glycoside hydrolases (GH). α-Amylase is the main representative of family GH13, but it is probably also present in the families GH57 and GH119, and possibly even in GH126. Family GH13, known generally as the main α-amylase family, forms clan GH-H together with families GH70 and GH77 that, however, contain no α-amylase. Within the family GH13, the α-amylase specificity is currently present in several subfamilies, such as GH13_1, 5, 6, 7, 15, 24, 27, 28, 36, 37, and, possibly in a few more that are not yet defined. The α-amylases classified in family GH13 employ a reaction mechanism giving retention of configuration, share 4-7 conserved sequence regions (CSRs) and catalytic machinery, and adopt the (β/α)8-barrel catalytic domain. Although the family GH57 α-amylases also employ the retaining reaction mechanism, they possess their own five CSRs and catalytic machinery, and adopt a (β/α)7-barrel fold. These family GH57 attributes are likely to be characteristic of α-amylases from the family GH119, too. With regard to family GH126, confirmation of the unambiguous presence of the α-amylase specificity may need more biochemical investigation because of an obvious, but unexpected, homology with inverting β-glucan-active hydrolases.
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Registered trials
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.