D
uring an enzymatic reaction, a product is produced, a substrate is used, and the catalyzing enzyme remains unconsumed. Therefore, to analyze the kinetics of an enzyme, a measure of the rate of change in concentration of the substrate being used up and/or the product being formed is typically determined. Conventional parameters such as the Michaelis-Menten constant (KM) and maximum velocity (Vmax) require the concentration of an enzyme to be static while various concentrations of substrate are examined.1 Spectrophotometric assessment of the change in concentration at the start of the enzyme–substrate reaction is preferred for an accurate representation of the kinetics.1
Procedural Tip: Get it Right from the Start
The beginning of an enzyme–substrate reaction is critical for the estimation of KM and Vmax due to the quick and linear increase in concentration of the product known to occur.1...
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