An enzyme is a biological catalyst: It binds to a substrate, the resulting complex forms a biologically relevant product, and the enzyme is then regenerated to do its job all over again. In bulk, the ensemble-averaged kinetics of that process was well characterized back in 1913 by the Michaelis–Menten equation. Taught to medical students ever since, the MM equation serves as a role model for quantitative biology. A Harvard University group led by Sunney Xie has now explored the equation’s microscopic underpinnings. The researchers tethered a single bacterial enzyme (β-galactosidase, essential for using sugar) and recorded waiting times between individual product molecules of the catalyzed reaction, each product giving a burst of fluorescence. Xie and coworkers found that at high substrate concentrations, short waiting times tend to be followed by short ones, and long by long. Those results revealed that the enzyme molecule is a dynamic entity with...
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1 April 2006
April 01 2006
Citation
Stephen G. Benka; Zooming in on enzyme kinetics. Physics Today 1 April 2006; 59 (4): 9. https://doi.org/10.1063/1.2207009
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