ArticleThe protein journal2011
Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues.
Article in The protein journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- How Does Starch Structure Impact Amylolysis? Review of Current Strategies for Starch Digestibility Study.Foods (Basel, Switzerland) · 2022Review
- Article
- Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.Applied microbiology and biotechnology · 2019Article
- Article
- In silico analysis of the α-amylase family GH57: eventual subfamilies reflecting enzyme specificities.3 Biotech · 2018Article
- Structure and function of α-glucan debranching enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.Cellular and molecular life sciences : CMLS · 2016Review
- Unique carbohydrate binding platforms employed by the glucan phosphatases.Cellular and molecular life sciences : CMLS · 2016Review
- Analysis on evolutionary relationship of amylases from archaea, bacteria and eukaryota.World journal of microbiology & biotechnology · 2016Article
- Aspergillus Oryzae S2 α-Amylase Domain C Involvement in Activity and Specificity: In Vivo Proteolysis, Molecular and Docking Studies.PloS one · 2016Article
- α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Cellular and molecular life sciences : CMLS · 2014Review
- Close relationship of a novel Flavobacteriaceae α-amylase with archaeal α-amylases and good potentials for industrial applications.Biotechnology for biofuels · 2014Article
- Evolutionary history of eukaryotic α-glucosidases from the α-amylase family.Journal of molecular evolution · 2013Article
- Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57.Extremophiles : life under extreme conditions · 2012Article
- Global analysis of viral infection in an archaeal model system.Frontiers in microbiology · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycoside hydrolase family 57 (GH57) contains α-amylase and a few other amylolytic specificities. It counts ~400 members from Archaea (1/4) and Bacteria (3/4), mostly of extremophilic prokaryotes. Only 17 GH57 enzymes have been biochemically characterized. The main goal of the present bioinformatics study was to analyze sequences having the clear GH57 α-amylase features. Of the 107 GH57 sequences, 59 were evaluated as α-amylases (containing both GH57 catalytic residues), whereas 48 were assigned as GH57 α-amylase-like proteins (having a substitution in one or both catalytic residues). Forty-eight of 59 α-amylases were from Archaea, but 42 of 48 α-amylase-like proteins were of bacterial origin. The catalytic residues were substituted in most cases in Bacteroides and Prevotella by serine (instead of catalytic nucleophile glutamate) and glutamate (instead of proton donor aspartate). The GH57 α-amylase specificity has thus been evolved and kept enzymatically active mainly in Archaea.
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