The anomeric effect in enzyme-catalyzed phosphoryl transfer

Phosphoryl transfer is central to cellular energy metabolism, and this dissertation explores the role of the anomeric effect in catalysis by phosphoryl transfer enzymes. Computational analyses reveal that hydrogen bonding can modulate the anomeric effect and scissile bond strength, suggesting enzymes exploit these interactions for catalytic gain. Structural surveys of phosphoryl transfer enzymes highlight active-site patterns that enhance hyperconjugation, and mutagenesis in arginine kinase confirms a link between the anomeric effect and catalytic rate. These findings uncover an overlooked mechanism contributing to rate enhancement, providing a unifying principle across diverse enzyme families.