Question 13 of 13Fill in the blanks:WriteC if only statement A is correct,Hif only statement B is correct,E if both statements are correct,M if both statements are incorrect.A.An inhibitor that binds somewhere in the enzyme other than the active site is anuncompetitive inhibitor.B. With this mode of inhibitor binding, the substrate's affinity to the enzyme is affected and it decreases themaximum reaction velocity.

Uncompetitive inhibition When an inhibitor binds only to the enzyme and the substrate complex.

Answered: Fill in the blanks: Write C if only…

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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If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.
QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
The Lineweaver-Burke plots of a reaction without inhibitor and one with non-competitive inhibitor will have the same 1. Vmax2. Km3. Km/Vmax4. 1/Vmax
Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite Concentration in rat myocytes (M) ATP 8.05x10-3 ADP 0.93x10-3 Pi 8.05x10-3
Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions: (a) How do I run the experiment to find the kinetic properties of the enzyme, KMand Vmax? (b) The enzyme decreased in activity in the presence of NaCl. How do I find out if NaCl is a competitive or non-competitive inhibitor? Explain.
Briefly describe why the Michaelis-Menten equilibrium-assumption cannotbe applicable to all enzyme-catalyzed reactions
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Assume that an inhibitor (I) can bind to an enzyme and is modified by the enzyme. The modified inhibitor (I*) is then permanently associated with the active site of the enzyme, thus inhibiting the enzyme activity. Such inhibitors are called: Suicide substrates Transition-state analogs Both A and B Neither A nor Bwhich answer choice is correct im confused... thx
Answer TRUE or FALSE.a. According to the lock-and-key model of enzyme action, the active site of an enzyme is not flexible in shape.b. In an enzyme-catalyzed reaction, the compound that does not undergo a chemical change is called the substrate.c. The nonprotein portion of a conjugated enzyme is not the enzyme’s active sited. Simple enzymes are composed only of protein; conjugated enzymes have nonprotein cofactors.
Question 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.
Question 19 Which of the following would have the lowest (most negative) standard reduction potential (E’0)? a FADH2 b Glucose c O2 d NADH

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