6s9v
From Proteopedia
Crystal structure of sucrose 6F-phosphate phosphorylase from Thermoanaerobacter thermosaccharolyticum
Structural highlights
FunctionSUCPP_THETC Catalyzes the reversible phosphorolysis of sucrose 6(F)-phosphate into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose 6-phosphate. May be involved in a new pathway for the degradation of sucrose, which could become phosphorylated on its fructose moiety during uptake via a PTS system. To a lesser extent, can also reversibly act on sucrose in vitro (PubMed:24599311). Is also able to catalyze transglycosylation reactions in vitro (PubMed:26074151).[1] [2] Publication Abstract from PubMedIn family GH13 of the carbohydrate-active enzyme database, subfamily 18 contains glycoside phosphorylases that act on alpha-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 group in subsite +1 were found to differ considerably between the two enzymes. Furthermore, several variants that introduce a higher degree of substrate promiscuity in the strict SPP from I. coccineus were designed. These results contribute to an expanded structural knowledge of enzymes in subfamily GH13_18 and facilitate their rational engineering. Structural Comparison of a Promiscuous and a Highly Specific Sucrose 6(F)-Phosphate Phosphorylase.,Franceus J, Capra N, Desmet T, Thunnissen AWH Int J Mol Sci. 2019 Aug 11;20(16). pii: ijms20163906. doi: 10.3390/ijms20163906. PMID:31405215[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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