Structural and phylogenetic analysis of α-glucosidase protein in insects

Abstract

α-Glucosidases (αglus) (EC 3.2.1.20) have been detected in a wide range of plants, animals and microorganisms and are described by their ability to catalyze the hydrolysis of 1,4-α-glucosidic linkages, releasing α-glucose. In this study, 96 αglu protein sequences from 33 organisms species including different insects species, plants (including thale cress and rice), mammals (including human and mouse) and Mycobacterium tuberculosis as a bacterium were aligned. Sequences were analyzed by computational tools to predict the protein properties, such as molecular mass, isoelectric point, signal peptide, conserved motifs, transmembrane domain and secondary structure. Drosophila melanogaster (GenBank Accession No.: NP 610382) was chosen as one of the representatives of insects for further analyses. The tertiary structure of representative samples were acquired using the tertiary structure of oligo-1,6-glucosidase from Bacillus cereus (Protein Data Bank code: 1UOK) as a template by Phyre2 server. Protein structure analysis revealed there is a high identity among insects and other organisms. There were some similar functional domains between D. melanogaster and M. tuberculosis. The modeled αglu has a typical spatial structure in insects and exhibits a high similarity with other organisms, especially Arabidopsis thaliana. Phylogenetic analysis indicated that D. melanogaster αglu has a close relationship with other αglus from different insect families. According to these results, αglu in insects should be evolved from a common ancestor.

Curcumin as a mild natural α‐glucosidase inhibitor: a study on its mechanism in vitro

“…The α‐helix was found to decrease with the increase in curcumin ratio while the β‐sheet was increased. These results were consistent with the similar reported conclusion suggesting that the inhibitor could change the secondary structure of α‐glucosidases protein (Seddigh & Darabi, 2015).…”

Molecular evolutionary mechanisms driving functional diversification of α-glucosidase in Lepidoptera

“…In this study, we predicted the tertiary structure and sucrose binding sites of BmSUH using Phyre2 and 3DLigandSite software 29 30 . Our predicted result was concordant with the estimation of Seddigh, who conducted homology modelling of α-glucosidase, such as Dm-NP610382 ( D. melanogaster ), Am-XP006560868 ( A. mellifera ), At-NP196733 ( A. thaliana ), Hs-NP937784 ( H. sapiens ) and Mt-YP007966392 ( M. tuberculosis ) 41 . This similarity of tertiary structure prediction analysis indicated that the 3D structures of α-glucosidase are conserved during evolution.…”

Site-Directed Mutagenesis: Improving the Acid Resistance and Thermostability of Bacillus velezensis α-Amylase and Its Preliminary Feed Application

“…A disulfide bond connects the A domain to the C domain, the function of which remains unknown. 6 Glycoside hydrolases are important enzymes that can increase the hydrolysis rate of polysaccharides to 10 17 times and provide nutrition and development for organisms. 7 The αamylases belonging to the family GH 13 are famous, for having excellent substrate specificity and efficient catalytic ability, which can effectively improve the utilization rate and production efficiency of starch raw materials.…”

“…B is the second large domain located between C and A. A disulfide bond connects the A domain to the C domain, the function of which remains unknown …”