The enzyme carboxylate peptides catalyzes the hydrolysis of the CBGP peptide which is the substrate. In the initial velocity measurement, vo, as a function of the initial substrate concentration O (CBGP,] the following results were obtained: (CBGP)0 (UM) vo (UM s-) 3. 25.104 0.0125 0.0400 6.69-104 Use Excel to solve this 0.0600 8. 59.10+ 0.0750 1.00-10 -When the phenylbutyrate inhibitor was added at a concentration of 2.10-3M , the following results were obtained: (CBGP Jo (UM) 0.0125 vo (uM s-) 1.72-104 3.01-104 1. Calculate the constant Michaelis Manten KM, and the maximum speed, Vmax 2. What type of delay is obtained from phenylbutyrate? Calculate the constant equilibrium of the inhibitor. 3. What type of delay is obtained from the benzoate ion? Calculate the constant equilibrium of the inhibitor. The constant equilibrium constant of the inhibitor is defined according to K [EI] 0.0250 0.0400 4.31.10+ 0.0550 5.61-104 When the benzoate ion inhibitor was added at a concentration of 5-10 M , the following results were obtained: [E] 1] (CBGP) (UM) 0.0175 0.0250 VO (UM s') 1.83-10-4 2.01-104 2.31.104 2.46-104 0.0500 0.1000