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(5): 229, 2021 May.
Article
en En
| MEDLINE
| ID: mdl-33968573
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. SUPPLEMENTARY INFORMATION The online version contains supplementary material available at 10.1007/s13205-021-02787-8.
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1
Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
3 Biotech
Año:
2021
Tipo del documento:
Article
País de afiliación:
Eslovaquia