Use graphs to illustrate enzyme activity as a function of the following: II. a. Substrate Concentration max velocity v max Rate Substrate Concentration b. Enzyme concentration Rate Enzyme Conc. с. рH Optimum Temperature Increasod temp. results in denaturation Rate Temperature d. Temperature Optimum pH Rate Increas ing pH

The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (µM). 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the inhibited enzyme reaction?

The enzymatic activity of an enzyme with Kg = 2 mM that converts substrate S into product P is measured at an initial substrate concentration S, of 10 µM. After 5 min, the substrate concentration is halved. What is the rate constant k, the maximal velocity vmax and the concentration of product after 12 min?

1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain

Explain how running a reaction with the enzyme aldolase at a pH of 14 affects its activity Enzyme Activity e Activity 765432TO Factors Affecting Enzyme Activity 0 6543 2 6 Solution pH 8 a) It significantly diminishes activity because enzyme is denatured b) It significantly diminishes activity because the enzyme becomes too reactive Oc) It will quadruple its activity because enzyme is denatured and free Question 9 (5 points) Estimate the optimum pH required for maximum enzyme activity 10 d) It will double its activity because enzyme now has more active sites 12 Factors Affecting Enzyme Activity

You measure the kinetics of an enzyme as a function of substrate concentration using the Lineweaver-Burke equation. The enzyme concentration is maintained constant at a level of 1 μM. From these data, determine the equation of the line, Vmax, KM, and kcat for the enzyme.   [S], μM   Velocity, μM/min  2 2.9 3 3.8 4 4.4 5 5.0 6 5.4 7 5.8 8 6.2 9 6.4 10 6.7   The Lineweaver-Burke equation is 1V=1V= ____________(1[S])(1[S]) + ___________. Therefore, the Vmax is ____________ μM/min, KM is ____________ μM, and kcat is ____________ /min.  Round-off all answers to four (4) decimal places.

Determine the Vo as a function of Vmax when the substrate concentration is equal to 10 KM or 20 KM. What does this tell you about an enzyme ability to reach Vmax?