Article3 Biotech2018
In silico analysis of the α-amylase family GH57: eventual subfamilies reflecting enzyme specificities.
Article in 3 Biotech, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Transformation of Starch into an Equilibrium Pool of Glucose and Small Maltosaccharides by a Hyperthermophilic Enzyme Exhibiting Coupled (Exo)Amylase-Glucanotransferase Functions.Applied biochemistry and biotechnology · 2026Article
- The role of N185D substitution in enhancing activity of BaqA∆C α-amylase.Scientific reports · 2025Article
- Diversity, metabolic potential and global distribution of the anaerobic fermentative bacteria Phylum Candidatus Cloacimonadota.Environmental microbiome · 2025Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- The Distinctive Permutated Domain Structure of Periplasmic α-Amylase (MalS) from Glycoside Hydrolase Family 13 Subfamily 19.Molecules (Basel, Switzerland) · 2023Article
- Analyzing the genetic diversity and biotechnological potential ofFrontiers in microbiology · 2022Article
- Structural elements determining the transglycosylating activity of glycoside hydrolase family 57 glycogen branching enzymes.Proteins · 2022Article
- Comparative genome analysis of fourComputational and structural biotechnology journal · 2022Article
- Acceptor dependent catalytic properties of GH57 4-α-glucanotransferase fromFrontiers in microbiology · 2022Article
- Aspects and Recent Trends in Microbial α-Amylase: a Review.Applied biochemistry and biotechnology · 2021Review
- Comparative transcriptome analysis of cells from different areas reveals ROS responsive mechanism at sclerotial initiation stage in Morchella importuna.Scientific reports · 2021Article
- Extension of the taxonomic coverage of the family GH126 outside Firmicutes and in silico characterization of its non-catalytic terminal domains.3 Biotech · 2020Article
- Article
- A new GH13 subfamily represented by the α-amylase from the halophilic archaeon Haloarcula hispanica.Extremophiles : life under extreme conditions · 2020Article
- Unravelling the diversity of glycoside hydrolase family 13 α-amylases from Lactobacillus plantarum WCFS1.Microbial cell factories · 2019Article
- Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.Applied microbiology and biotechnology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycoside hydrolases (GHs) have been classified in the CAZy database into 153 GH families. Currently, there might be four α-amylase families: the main family GH13, the family GH57 with related GH119 and, eventually, also GH126. The family GH57 was established in 1996 as the second and smaller α-amylase family. In addition to α-amylase, it contains 4-α-glucanotransferase, α-glucan branching enzyme, amylopullulanase, dual-specificity amylopullulanase-cyclomaltodextrinase, non-specified amylase, maltogenic amylase and α-galactosidase. The family GH57 enzymes employ the retaining reaction mechanism, share five typical conserved sequence regions and possess catalytic (β/α)
Indexed as
Identifiers
What OpenQuestion holds
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.