A Perspective on Enzyme Catalysis
Abstract
The seminal hypotheses proposed over the years for enzymatic catalysis are scrutinized. The historical record is explored from both biochemical and theoretical perspectives. Particular attention is given to the impact of molecular motions within the protein on the enzyme's catalytic properties. A case study for the enzyme dihydrofolate reductase provides evidence for coupled networks of predominantly conserved residues that influence the protein structure and motion. Such coupled networks have important implications for the origin and evolution of enzymes, as well as for protein engineering.
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S.J.B. acknowledges funding from NIH grants GM13306 and GM24129. S.H.-S. acknowledges funding from NIH grant GM56207 and NSF grant CHE-0096357. We also thank Yolanda Small and James Watney for creating the figures.
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Volume 301 | Issue 5637
29 August 2003
29 August 2003
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