Abstract
The family GH77 contains 4-α-glucanotransferase acting on α-1,4-glucans, known as amylomaltase in prokaryotes and disproportionating enzyme in plants. A group of bacterial GH77 members, represented by amylomaltases from Escherichia coli and Corynebacterium glutamicum, possesses an N-terminal extension that forms a distinct immunoglobulin-like fold domain, of which no function has been identified. Here, in silico analysis of 100 selected sequences of N-terminal domain homologues disclosed several well-conserved residues, among which Tyr108 (E. coli amylomaltase numbering) may be involved in α-glucan binding. These N-terminal domains, therefore, may represent a new type of starch-binding domain and define a new CBM family. This hypothesis is supported by docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree.
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Abbreviations
- CBM:
-
Carbohydrate-binding module
- β-CD:
-
β-Cyclodextrin
- CSR:
-
Conserved sequence region
- DPE:
-
Disproportionating enzyme
- G2:
-
Maltose
- G3:
-
Maltotriose
- G4:
-
Maltotetraose
- GH:
-
Glycoside hydrolase
- PDB:
-
Protein Data Bank
- SBD:
-
Starch-binding domain
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This work was financially supported by the Grant No. 2/0146/21 from the Slovak Grant Agency VEGA and by Grant No. 6108-00476B from Independent Research Fund Denmark ∣ Natural Sciences (FNU).
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FM collected data, analysed results, prepared figures and contributed to writing the manuscript; MSM and BS contributed to interpreting results and writing the manuscript; SJ designed the study, contributed to collecting data, analysed and interpreted results, prepared figures and wrote the manuscript. All the authors contributed to discussion of the research and approved the final version of the manuscript.
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Mareček, F., Møller, M.S., Svensson, B. et al. 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 11, 229 (2021). https://doi.org/10.1007/s13205-021-02787-8
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DOI: https://doi.org/10.1007/s13205-021-02787-8