Interplay of catalytic subsite residues in the positioning of α-d-glucose 1-phosphate in sucrose phosphorylase.

Kinetic and molecular docking studies were performed to characterize the binding of α-d-glucose 1-phosphate (αGlc 1-) at the catalytic subsite of a family GH-13 sucrose phosphorylase (from ) in wild-type and mutated form. The best-fit binding mode of αGlc 1- dianion had the phosphate group placed relative to the glucosyl moiety (adopting a relaxed chair conformation) and was stabilized mainly by hydrogen bonds from residues of the enzyme׳s catalytic triad (Asp, Glu and Asp) and from Arg. Additional feature of the αGlc 1- docking pose was an intramolecular hydrogen bond (2.

Lipophilic sugar nucleotide synthesis by structure-based design of nucleotidylyltransferase substrates.

Structure-based design of alkyl sugar-1-phosphates provides an efficient nucleotidylyltransferase-catalyzed synthesis of a series of new lipophilic sugar nucleotides possessing long or branched alkyl chains, thereby demonstrating the utility of nucleotidylyltransferases to catalyze the synthesis of sugar nucleotides with potential applications in lipopolysaccharide and lipoglycopeptide biosynthesis.