Predict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactions **Question 3: Predict the effect of each of the following amino acid substitutions on the \( K_M \) and \( k_{cat} \) of the enzyme-catalyzed reaction.**(a) **Substitution of Ser 195 of chymotrypsin with Ala**(b) **Substitution of Asp 189 of trypsin with His**(c) **Substitution of Asp 102 of chymotrypsin with Glu**(d) **Substitution of His 57 of trypsin with Ala**(e) **Substitution of Ser 189 of chymotrypsin with Lys**

Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

3. Predict the effect of each of the following amino acid substitutions on the KM and keat of the catalyzed reaction. (a) Substitution of Ser 195 of chymotrypsin with Ala (b) Substitution of Asp 189 of trypsin with His (c) Substitution of Asp 102 of chymotrypsin with Glu (d) Substitution of His 57 of trypsin with Ala (e) Substitution of Ser 189 of chymotrypsin with Lys enzyme-

3. Predict the effect of each of the following amino acid substitutions on the KM and keat of the catalyzed reaction. (a) Substitution of Ser 195 of chymotrypsin with Ala (b) Substitution of Asp 189 of trypsin with His (c) Substitution of Asp 102 of chymotrypsin with Glu (d) Substitution of His 57 of trypsin with Ala (e) Substitution of Ser 189 of chymotrypsin with Lys enzyme-

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

The induced-fit theory aims to explain how the interactions between an enzyme and a sub- strate facilitate the catalysis of chemical reactions. Which of the following properties of enzyme-substrate interaction best explains enzymatic catalysis according to the induced-fit model? A B с D Environmental conditions can alter the affinity between a substrate and an enzyme by changing the conformation of the enzyme. Conformation changes in both the enzyme and the substrate due to their chemical in- teractions lower the activation energy of the catalyzed reactions. The interactions between an enzyme and a substrate depend on both structural and chemical compatibility and are therefore highly specific. Enzymes remain chemically unaltered between cycles of enzymatic catalysis while sub- strates are transformed into products.
Can you help solve this and write differential equation for the rates
Derive the rate law for the following enzyme reaction chain. Linear the equation you have derived as a Lineweaver-Burk type equation.
Describe the lengths of the products of the transketolase reaction when the two substrates are both five-carbon sugars.
Calculate the numerical relationship between KM and [S] when a reaction enzymatically catalyzed reaches 80% of Vmax.
How temperature, pH and salt affects the enzyme activity in terms of protein structure (primary, secondary, tertiary, quaternary) and other factors? Please explain briefly.
List the local effectors of enzyme kinetics and give an example for one of them.
A purely competitive inhibitor of an enzyme has which of the following kinetic effects? decrease in Km increase in Vmax decrease in Vmax increase in Km Question 60 The Michaelis-Menten constant (KM) has the following characteristics, EXCEPT: The dimension for KM is concentration, such as molarity It is equal to ½ of Vmax It is the substrate concentration necessary to reach ½ of Vmax
The above reaction coordinate diagram in the presence of enzyme is inconsistent with the "lock and key" model of enzyme-substrate l binding. Draw and properly label the reaction. coordinate diagram for the enzymatic reaction according to the "lock and key" model. Explain why this model is inconsistent with catalytic properties of enzymes.
In a bisubstrate reaction, a small amount of the fi rst product P is isotopically labeled (P*) and added to the enzyme and the fi rst substrate A. No B or Q is present. Will A (= P—X) become isotopically labeled (A*) if the reaction follows a Sequential mechanism?
Give an example of one enzyme that participates in both glycolysis and gluconeogenesis. Evaluate the structures of chemical reactants and products and the enthalpic and entropic contributions to Gibbs free energy change for the reaction. Explain how the enzyme is able to catalyze the reaction (either direction.)
Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)