QM/MM Studies Reveal How Substrate-Substrate and Enzyme-Substrate Interactions Modulate Retaining Glycosyltransferases Catalysis and Mechanism

• Published in: Advances in protein chemistry and structural biology Vol. 100; p. 225
• Main Authors: Gómez, Hansel, Mendoza, Fernanda, Lluch, José M, Masgrau, Laura
• Format: Journal Article
• Language: English
• Published: Netherlands 2015
• Subjects: Bacteria - chemistry; Bacteria - enzymology; Bacterial Proteins - chemistry; Biocatalysis; Galactosyltransferases - chemistry; Glycosyltransferases - chemistry; Humans; Hydroxylation; Kinetics; Molecular Dynamics Simulation; Monosaccharides - chemistry; N-Acetylgalactosaminyltransferases - chemistry; Polypeptide N-acetylgalactosaminyltransferase; Quantum Theory; Stereoisomerism; Substrate Specificity; Thermodynamics; Front-side attack; Substrate-assisted catalysis; QM/MM; Retaining glycosyltransferases; Double-displacement mechanism

Glycosyltransferases (GTs) catalyze the biosynthesis of glycosidic linkages by transferring a monosaccharide from a nucleotide sugar donor to an acceptor substrate, and they do that with exquisite regio- and stereospecificity. Retaining GTs act with retention of the configuration at the anomeric car...