A Broad-Spectrum alpha-Glucosidase of Glycoside Hydrolase Family 13 from Marinovum sp., a Member of the Roseobacter Clade

Li, J; Mui, JW; da Silva, BM; Pires, DEV; Ascher, DB; Madiedo Soler, N; Goddard-Borger, ED; Williams, SJ

Author(s): Li, J; Mui, JW; da Silva, BM; Pires, DEV; Ascher, DB; Madiedo Soler, N; Goddard-Borger, ED; Williams, SJ;
Details: Publication Year 2024-09,Volume 196,Issue #9,Page 6059-6071
Journal Title: Applied Biochemistry and Biotechnology
Abstract: Glycoside hydrolases (GHs) are a diverse group of enzymes that catalyze the hydrolysis of glycosidic bonds. The Carbohydrate-Active enZymes (CAZy) classification organizes GHs into families based on sequence data and function, with fewer than 1% of the predicted proteins characterized biochemically. Consideration of genomic context can provide clues to infer possible enzyme activities for proteins of unknown function. We used the MultiGeneBLAST tool to discover a gene cluster in Marinovum sp., a member of the marine Roseobacter clade, that encodes homologues of enzymes belonging to the sulfoquinovose monooxygenase pathway for sulfosugar catabolism. This cluster lacks a gene encoding a classical family GH31 sulfoquinovosidase candidate, but which instead includes an uncharacterized family GH13 protein (MsGH13) that we hypothesized could be a non-classical sulfoquinovosidase. Surprisingly, recombinant MsGH13 lacks sulfoquinovosidase activity and is a broad-spectrum alpha-glucosidase that is active on a diverse array of alpha-linked disaccharides, including maltose, sucrose, nigerose, trehalose, isomaltose, and kojibiose. Using AlphaFold, a 3D model for the MsGH13 enzyme was constructed that predicted its active site shared close similarity with an alpha-glucosidase from Halomonas sp. H11 of the same GH13 subfamily that shows narrower substrate specificity.
Publisher: Springer
Keywords: *alpha-Glucosidases/genetics/chemistry/metabolism; *Roseobacter/enzymology/genetics; Substrate Specificity; Multigene Family; Bacterial Proteins/genetics/chemistry/metabolism; Models, Molecular; Bioinformatics; Carbohydrates; Enzymes; Glycosidase
Research Division(s): Chemical Biology
PubMed ID: 38180643
Publisher's Version: https://doi.org/10.1007/s12010-023-04820-3
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2024-01-25 09:18:03

Last Modified: 2024-12-05 10:33:39