Structural Comparison of a Promiscuous and a Highly Specific Sucrose 6^F-Phosphate Phosphorylase.

ABSTRACT: In family GH13 of the carbohydrate-active enzyme database, subfamily 18 contains glycoside phosphorylases that act on α-sugars and glucosides. Because their phosphorolysis reactions are effectively reversible, these enzymes are of interest for the biocatalytic synthesis of various glycosidic compounds. Sucrose 6^F-phosphate phosphorylases (SPPs) constitute one of the known substrate specificities. Here, we report the characterization of an SPP from Ilumatobacter coccineus with a far stricter specificity than the previously described promiscuous SPP from Thermoanaerobacterium thermosaccharolyticum. Crystal structures of both SPPs were determined to provide insight into their similarities and differences. The residues responsible for binding the fructose 6-phosphate g

SUBMITTER: Franceus J 

PROVIDER: S-EPMC6720575 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature