Prediction and experimental verification of compact versus extended enzyme active sites

Understanding the efficiency and specificity of enzymes is a fundamental question in biochemistry of great practical importance. Although progress in biochemical and structural studies has enriched our knowledge of enzymes, the role of remote residues in enzyme catalysis is largely unexplored. This thesis investigates the importance of remote residues in enzyme catalysis using both computational and experimental techniques. Two enzymes, keto steroid isomerase (KSI) and phosphoglucose isomerase (PGI), are investigated and the role of remote residues in their catalysis is explored.