ArticleExtremophiles : life under extreme conditions2012
Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57.
Article in Extremophiles : life under extreme conditions, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 57 citations in OpenAlex.
- Beyond Branching: Unlocking the Catalytic Versatility of Branching Enzymes for the Design of Diverse α-Glucan Structures.Molecules (Basel, Switzerland) · 2026Review
- The crystal structure of GH57 family amylopullulanase reveals its dual binding pockets sharing the same catalytic dyad.Communications biology · 2025Article
- Structural elements determining the transglycosylating activity of glycoside hydrolase family 57 glycogen branching enzymes.Proteins · 2022Article
- 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
- Deciphering Symbiotic Interactions of "mSystems · 2021Article
- Aspects and Recent Trends in Microbial α-Amylase: a Review.Applied biochemistry and biotechnology · 2021Review
- A putative novel starch-binding domain revealed by in silico analysis of the N-terminal domain in bacterial amylomaltases from the family GH77.3 Biotech · 2021Article
- Activity-Based Protein Profiling for the Identification of Novel Carbohydrate-Active Enzymes Involved in Xylan Degradation in the Hyperthermophilic EuryarchaeonFrontiers in microbiology · 2021Article
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- Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.Applied microbiology and biotechnology · 2019Article
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- In silico analysis of the α-amylase family GH57: eventual subfamilies reflecting enzyme specificities.3 Biotech · 2018Article
- Structure and Evolution of Glycogen Branching Enzyme N-Termini From Bacteria.Frontiers in microbiology · 2018Article
- Complete Genome of the Starch-Degrading Myxobacteria Sandaracinus amylolyticus DSM 53668T.Genome biology and evolution · 2016Article
- Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.Cellular and molecular life sciences : CMLS · 2016Review
- Distribution of glucan-branching enzymes among prokaryotes.Cellular and molecular life sciences : CMLS · 2016Review
- Structure and function of α-glucan debranching enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- Membrane-bound amylopullulanase is essential for starch metabolism of Sulfolobus acidocaldarius DSM639.Extremophiles : life under extreme conditions · 2015Article
- α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Cellular and molecular life sciences : CMLS · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycoside hydrolase family 57 (GH57) contains five well-established enzyme specificities: α-amylase, amylopullulanase, branching enzyme, 4-α-glucanotransferase and α-galactosidase. Around 700 GH57 members originate from Bacteria and Archaea, a substantial number being produced by thermophiles. An intriguing feature of family GH57 is that only slightly more than 2 % of its members (i.e., less than 20 enzymes) have already been biochemically characterized. The main goal of the present bioinformatics study was to retrieve from databases, and analyze in detail, sequences having clear features of the five GH57 enzyme specificities mentioned above. Of the 367 GH57 sequences, 56 were evaluated as α-amylases, 99 as amylopullulanases, 158 as branching enzymes, 46 as 4-α-glucanotransferases and 8 as α-galactosidases. Based on the analysis of collected sequences, sequence logos were created for each specificity and unique sequence features were identified within the logos. These features were proposed to define the so-called sequence fingerprints of GH57 enzyme specificities. Domain arrangements characteristic of the individual enzyme specificities as well as evolutionary relationships within the family GH57 are also discussed. The results of this study could find use in rational protein design of family GH57 amylolytic enzymes and also in the possibility of assigning a GH57 specificity to a hypothetical GH57 member prior to its biochemical characterization.
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