d. Which of the substrates is likely to have a higher Vmax. What is your reasoning?e. Can you propose a molecule that might act as an inhibitor to this reaction? Explain your reasoning. ### Chymotrypsin Enzyme Activity and Substrate InteractionChymotrypsin is a serine protease enzyme involved in the breakdown of proteins. It functions by interacting with specific substrates, enabling the hydrolysis of peptide bonds.#### Kinetics of Chymotrypsin- **N-acetylvaline ethyl ester:** The Michaelis constant (\(K_m\)) for its reaction with chymotrypsin is \(8.8 \times 10^{-2}\).- **N-acetyltyrosine ethyl ester:** The \(K_m\) for its reaction with chymotrypsin is \(6.6 \times 10^{-4}\) M.#### Chemical Structures- **N-acetyl valine:** Displays a standard amino acid structure with an acetyl group attached to the nitrogen. - **N-acetyl tyrosine:** Similar to N-acetyl valine, but with a phenolic hydroxyl group on the aromatic ring, characteristic of tyrosine.#### Diagram: Chymotrypsin Active SiteThe diagram illustrates the active site of chymotrypsin, showing the catalytic triad composed of:- **Serine 195 (Ser 195)**- **Histidine 57 (His 57)**- **Aspartate 102 (Asp 102)**These residues are essential for enzymatic activity and facilitate the cleavage of peptide bonds. The active site is depicted with interactions like hydrogen bonding and the nucleophilic attack mechanism involved in substrate processing.This detailed representation helps in understanding the specific structural components that contribute to the catalytic efficiency of chymotrypsin in proteolysis.

d. Km is the substrate concentration at which Vmax is half. Substrate with higher Km will have high…

Answered: Which of the substrates is likely to…

Which of the substrates is likely to have a higher Vmax. What is your reasoning? e. Can you propose a molecule that might act as an inhibitor to this reaction? Explain your reasoning.

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

To investigate the effects of a newly discovered inhibitor and enzymology list obtained the results showed in the figure below. Which statement best describes the binding of its inhibitor on the enzyme? ~y=0.768r+4.7425 3-0.568x+46576 19 . . . . ● x X The inhibitor binds at the active site. The inhibitor binds away from the active site, but after substrate binding. The inhibitor binds away from the active site before or after substrate binding. The inhibitor binds close to the active site, but after substrate binding. The inhibitor binds close to the active site, but prior to substrate binding. red by a strain
Can you explain the answe?
Please name the differences between competitive and noncompetitive inhibition.
Strategies to Regular Enzyme Activity: Give an example of an enzyme that uses the strategy shown and describe how the activity of the enzyme is regulated. Regulatory Strategy 1. Covalent Modification 2. Feedback Inhibition 3. Cascade of Reaction Enzyme Describe how the regulatory strategy is employed
Describe the specific multi-enzyme example discussed in class of how enzyme activity can be altered by changing its substrate to product ratio.
Don't give Handwritten answer
None
pls help me
Do answer and explain plz.
A. How does each of the following irreversible inhibitors interact with the Enzymes? IV. 1. Cyanide 2. Heavy-metal ions B. List an antidote for each of these two poisons and describe how each functions.
Calculate KI' of the inhibitor from the information given. All information may not be needed to calculate. K'm = (29Ki+1.45x10^-10)/Ki Vmax = 11.7 µMs-1 Kcat = 130 s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM Inhibitor Concentration = 5x10^-12
a. How does an enzyme speed up the reaction of a substrate? b. After the products have formed, what happens to the enzyme?