During the course of an enzymatic reaction, [S] decreases, and [P] increases. This results in an overall decrease in the reaction rate, as illustrated in Figure 1. To measure the reaction rate of an enzymatic reaction corresponding to a specific substrate concentration, it is, therefore, necessary to measure the reaction rate at the beginning of the reaction. At the beginning of the reaction, the substrate concentration can be assumed to be constant, and the progress curve is close to linear. Thus, the rate of the reaction, which is equal to the slope of the progress curve, can be obtained using linear regression. The reaction rate at the beginning of the reaction is called the initial reaction rate or V0 [1].

An illustration of a progress curve of a general enzymatic reaction. The graph has time on the x-axis and the formation of product on the y-axis. The curve reflects the general enzymatic reaction, which is shown as the change in concentration over time. The change is a result of the formation of the product created from the substrate. As time increases, so does the product in a linear fashion until the curve starts to plateau as a result of a decreasing reaction rate

Figure 1: Progress curve of a general enzymatic reaction.

References

  1. Atkins, Peter W.; de Paula, Julio; Friedman, Ronald (2009). Quanta, Matter, and Change: A molecular approach to physical chemistry. Oxford University Press. ISBN 978-0-19-920606-3.

  2. Lehninger, Albert L.; Nelson, David L.; Cox, Michael M. (2008). Principles of Biochemistry (5th ed.). New York, NY: W.H. Freeman and Company. ISBN 978-0-7167-7108-1.

Reaction rate

Km

Theory overview