3. Rennin is an enzyme that follows the following reaction mechanism: S + E <==1==> ES ==2==> P+E The first reaction has kinetic constants k₁ and k₁, while k₂ is the rate constant for the second reaction. A. Look up rennin and classify it as one of the 6 types of enzymes discussed in class. B. Give an example of a substrate used with rennin, and what product/type of product results in industry. C. Given values for the kinetic constants: k₁ = 1.75*10² L/mol-s k.₁ = 2.66 * 104 s¹ K₂=9.53 * 10³ S-¹ What is the Michaelis Constant for this enzyme if you use the Rapid Equilibrium, RE, Assumption? What is the Michaelis Constant for this enzyme if you use the Quasi Steady State Assumption, QSSA? (Note: we found the relationship between the kinetic constants and Km and Vmax in class for this mechanism using both approaches} D. Using the values in (C), for a rennin concentration of 1.27 * 105 M, and the Michaelis-Menten equation with Km values from part C, determine the initial reaction velocities (for both RE and QSSA) when the substrate is at a concentration of 4.88 x 10³ M? (Note: both RE and QSSA will predict the same maximum reaction velocity, Vmax, for THIS mechanism}

1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions.  a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain.  b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?

15) The graph at right shows the results of reaction rate vs. substrate concentration for a Michaelis-Menten type enzyme 16) Th a. True b. False* reaction rate substrate concentration

8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.

Knowing that for a bacterial colony to be able to grow it must produce product "3" AND "4", use the information in the image to describe which enzyme(s) are that are Non-Functional in Colony C? Please note error in enzyme description at bottom of image. X converts 1 into 2; Y converts 1 into 3; and z converts 2 into 4.

1. Consider the following parameters related to an enzyme that follows Michaelis-Menten kinetics for the reaction: k(1) k(2) S ----> ES ----> P k(-1)

a. What is the Vmax of this enzyme WITHOUT inhibitor? Please show your work.   b. What is the Km of this enzyme WITHOUT inhibitor? Please show your work. c. The specificity constant of enzyme X is 8 x 10^7 /(M * seconds) What is the kcat of enzyme X WITHOUT inhibitor? Please show your work d. What was the concentration of enzyme used for measuring the kinetics of enzyme X WITHOUT inhibitor? Please show your work

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

Although we have introduced catalytic strategies separately, an enzyme typically employs more than one during a reaction. The catalytic strategies employed by serine protease include: Select one or more: O a. reduction of ASt b. transition state stabilization Oc. metal-assisted catalysis O d. acid/base catalysis O e. covalent catalysis