Refer to the following graph when answering questions.These words may be used to fill: competitive, uncompetitive, noncompetitive,irreversible.-1mg, μmol min-1v-10.20.1THA-4-2CBA+2 4[S]-1, (mM-1)Word1, The value of Km for the enzyme depicted by curve A is2, The value of Vmax for the enzyme depicted by curve A is3, Curve B depicts the effect of an inhibitor on the system described by curve A.This inhibitor is ainhibitor.4, Curve C depicts the effect of a different inhibitor of the system described by curveA. This second inhibitor is ainhibitor.D

Km is the Michelle's menton constant which is equal to the substrate concentration at half of the…

Answered: 1² L-^ 0.1 + ||| -4-2 |||| 24 [S]-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

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Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the Km of the reaction represented by Line (B).
What step ends the first-half of the chymotrypsin mechanism? Attack of water on the acyl-enzyme intermediate. Selected Collapse of the first tetrahedral intermediate, releasing of the C-terminal peptide fragment and formation of the acyl-enzyme intermediate. Deprotonation of serine by the histidine. Collapse of the second tetrahedral intermediate leading to the final products. REVIEW QUESTION 1/1 CONTINUE MacBook Pro https://virginiacommonwealth.instructure.com/courses/42082/assignments/271397 esc OT
Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. QUESTION: Line (A) represents ____________. A. an enzyme-catalyzed reaction in the absence of any inhibitor. B. an enzyme-catalyzed reaction in the presence of a competitive inhibitor. C. an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor. D. an enzyme-catalyzed reaction in the presence of a noncompetitive, or mixed, inhibitor.
The inhibitory effect of an uncompetitive inhibitor is greater at high [S] than at low [S]. Explain this observation.
The table contains data about how different ASFV mutants affect enzyme activity-- for example the D29A mutant, where the D at position 29 was mutated to an A. Select three mutants at random, and for each mutant explain how that mutation could affect intermolecular force interactions (an example: hydrogen bonding could be disrupted by this mutation because…
1/v 1/[S] Compound I is a substrate for the enzyme reverse transcriptase and compounds Il and lll are inhibitors. The inhibition plots for each compound are Illustrated above. The line labeled E is the enzyme with substrate alone (no inhibitor present). Answer the following questions by filling în the blanks. Line A most likely belongs to compound because it is a inhibitor. Line B belongs to compound because it is a inhibitor.
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 potent inhibitor effectively inhibits an enzyme catalyzed reaction. What kind of a Ki value you would expect for a potent inhibitor?
Give a possible set of bacterial factors (or lack thereof) and what properties they have that would explain an increase in the 50% inhibitory concentration for tetracycline by 1,000-fold in an organism.
4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.
Please explain your reasoning for every answer
Amino acid alanine

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