Question

Problem 3: A) Draw the mechanistic modifications associated with chymotripsin enzyme and its substrate up to the formation of acyl enzyme intermediate. Specify the role of each of the amino acids in the catalytic triad. B) Provide a Michaelis-Menten rate-law equation. Subsequently, on the same graph draw Lineweaver-Burk plots for i) enzyme which is not inhibited: ii) enzyme inhibited by a non-competitive inhibitor, C) The Km and kcat for hexokinase with as a glucose substarte are 5-10 M and 8-10² 1/s, respectively. When fructose is the substrate the Km and keat are 3-10 M and 9.101/s, respectively. What do the data tell you about the binding affinity and efficiency of the enzyme hexokinase with respect to each substrate?

Answer 1

The active site of chymotrypsin contains a catalytic triad a collection of 3 residues that work together to promote the hydrolysis & peptidel sépti de bionda, Anfior digest ser-19s . it its The ser 195 of alcohol form is not strong nucleophile. To transform into a Strong ie strong a nearby tin-57 nelophie pulls away the hydrogen ion to form on alkoxide At the same time a third residue aop -102 position estabilizes the histidine So, that it cancarry out the defrot oration Peaction mechanisin:- .X H. "Oun H-NA w oxyanion hole m . OHN unt-Nit Tetra hedral inter mediate of suborate (peptide?

ka (8) Ets X I ES K E +P wher, & Engine, So Sulostraté Pe product ES= Enzone Substrate complex Rate law: dp] = K2 [ES] un componibitor combe ti tive line weaver Bark plot e slope kan man t = m + veux A no inhibitor Vimax, app 51 Vo= Initial velocity of the recer Kwa Michaelin constant (s] = substrate concentr Vmax shaxinum In uncompetitive inhibitor kmf Vmax both decrease. velocity un competitive inhibitor bind to Es complex