Question 1 **Question Completion Status:****QUESTION 1**An uncompetitive inhibitor of a Michaelis-Menten enzyme influences the Km and Vmax as:- Km Vmax - ○ increase ○ no change - ○ decrease ○ decrease - ○ decrease ○ increase - ○ increase ○ decrease - ○ decrease ○ no change**QUESTION 2**Consider Figures 1 and 2. Choose the statement that is TRUE.(Graph images showing reaction pathways)1. Figure 1 - Free energy vs. Progress of Reaction graph: - Displays a peak representing the transition state above reactants and products, indicating energy required for activation.2. Figure 2 - Free energy vs. Progress of Reaction graph: - Shows a lower peak or activation energy requirement compared to Figure 1.*Instructions: Click Save and Submit to save and submit. Click Save All Answers to save all answers.*

Answered: Question 1

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

Related questions

Question

Question 1

Expert Solution

Step 1

Uncompetitive inhibition, also known as anti-competitive inhibition, occurs when an enzyme inhibitor binds exclusively to the enzyme-substrate complex (the E-S complex). In reactions involving two or more substrates or products, uncompetitive inhibition is common. Non-competitive inhibition can occur with or without the presence of the substrate, whereas uncompetitive inhibition necessitates the formation of an enzyme-substrate complex. Two characteristics separate uncompetitive inhibition from competitive inhibition: first, uncompetitive inhibition cannot be reversed by increasing [S], and second, the Lineweaver–Burk plot reveals parallel rather than intersecting lines.