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Enzymes at work are enzymes in motion

Protein motions and water both play key roles in enzyme catalysis Enzymes provide the necessary impetus for chemical reactions to occur at a rate that can support biological life. They do so by forming a unique enzyme-substrate complex and thus lowering the energy required for a substrate to convert to a product. Numerous approaches have been used for more than 50 years to unravel the mechanisms of enzyme-mediated catalysis (1). Initial kinetic experiments helped to ascertain substrate specificity. Spectroscopic data have shown that enzymes are not static, and more recently, atomic-resolution nuclear magnetic resonance (NMR) data have revealed the extent and duration of the structural fluctuations (2–4). On page 262 of this issue, Kim et al. (5) use structural and computational methods to provide evidence for the crucial roles of protein dynamics and water in enzyme catalysis.