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Publication Abstract from PubMed

Members of glycosyltransferase family 75 (GT75) not only reversibly catalyze the autoglycosylation of a conserved arginine residue with specific NDP-sugars but also exhibit NDP-pyranose mutase activity that reversibly converts specific NDP-pyranose to NDP-furanose. The latter activity provides valuable NDP-furanosyl donors for glycosyltransferases and requires a divalent cation as a cofactor instead of FAD used by UDP-D-galactopyranose mutase. However, details of the mechanism for NDP-pyranose mutase activity are not clear. Here we report the first crystal structures of GT75 family NDP-pyranose mutases. The novel structures of GT75 member MtdL in complex with Mn(2+) and GDP, GDP-D-glucopyranose, GDP-L-fucopyranose, GDP-L-fucofuranose, respectively, combined with site-directed mutagenesis studies, reveal key residues involved in Mn(2+) coordination, substrate binding, and catalytic reactions. We also provide a possible catalytic mechanism for this unique type of NDP-pyranose mutase. Taken together, our results highlight key elements of an enzyme family important for furanose biosynthesis.

Structures of the NDP-pyranose mutase belonging to glycosyltransferase family 75 reveal residues important for Mn(2+) coordination and substrate binding.,Du X, Chu X, Liu N, Jia X, Peng H, Xiao Y, Liu L, Yu H, Li F, He C J Biol Chem. 2023 Feb;299(2):102903. doi: 10.1016/j.jbc.2023.102903. Epub 2023 , Jan 13. PMID:36642179^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.