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.
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.
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.
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.)
How many of the following statements are true? Allosteric enzymes display sigmoidal kinetics for plots of V versus [S] Allosteric enzymes exist in T and R states Allosteric enzymes display kinetics that becomes less sigmoidal in the presence of activators
Regarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level. Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?
Please Explain each part to the best of your ability. This is Biochemistry. Thank you
If you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the structure of the transition state right after the enzyme attacks the first substrate. Think hard about what we have covered, and visualize that transition state accurately:
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction O c. The enzyme stabilizes the transition state for the reaction Od. The reaction is exergonic е. The reaction is now spontaneous due to the addition of enzyme Released Energy