Which of the following are true when enzymesand substrate interact?kıE + S●ES--Pk-1the rate of the formation of ES = k1 [ES]the rate of the formation of the product = k2[ES]k1 [ES] = k-1 [ES]the rate of breakdown of ES to reform theenzyme and substrate = K-1[E][S]the rate of formation of ES = k1[E][S]

Assuming the enzyme follows the first order kinetics, The rate of a formation is given by the…

Answered: Which of the following are true when…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter17: Metabolism: An Overview

Section: Chapter Questions

Problem 12P: How Do Vitamin-Derived Coenzymes Aid Metabolism? What chemical functionality is provided to enzyme...

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An enzyme reversibly binds a substrate. The rate constant (kcat) for catalytic conversion of enzyme-substrate complex into product and free enzyme is 1.0 s-1. The rate constant for dissociation of enzyme-substrate complex (k-1) is 9.0s^-1. 1) For each substrate binding event, what is the probability that substrate is converted into product rather than dissociated without conversion? 2) What is the probability that 20 consecutive binding events result in no product formation? 3) If you evaluated 1,000 different sets of 20 consecutive binding events, what would be the average number of product molecules formed (per 20 binding events)? 4) What is the probability that 20 consecutive binding events result in a number of product molecules at least equal to this average?
In a Lineweaver-Burk graph, the place where the line crosses the Y-axis represents: a) Km b) Vmax c) 1/Km d) 1/Vmax Which coenzyme is most often used in dehydrogenation reactions of the type –CH2CH2- = -CH=CH- ? a) NAD b) FAD c) NADP d) FMN Which one of these transports fructose? A) GLUT-2 b) GLUT-3 c) GLUT-4 d) GLUT-5 The pyruvate dehydrogenase complex converts pyruvate to which molecule? A) oxaloacetate b) glycogen c) acetyl-CoA d) citrate The pyruvate dehydrogenase complex produces how many ATP molecules at the substrate level? A) 0 b) 1 c) 3 d) 4 The pyruvate dehydrogenase complex produces how many ATP molecules indirectly via oxidative phosphorylation per glucose molecule? A) 1 b) 3 c) 5 d) over 30
Which of the following is the process where there is transfer of phosphate group to produce ATP or GTP from an intermediate or substrate? Group of answer choices Oxidative decarboxylation Oxidative phosphorylation Substrate-level phosphorylation Substrate-level decarboxylation
The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.
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. Zymogen activation Covalent modification Competitive inhibition Allosteric activation Allosteric inhibition
The place on the enzyme where the substrate binds is called the: a) coenzyme b) transition state c) active site d) enzyme-substrate complex The enzyme-bound substrate is also called: a) coenzyme b) transition state c) active site d) enzyme-substrate complex The enzyme-bound substrate facilitates the formation of the: a) coenzyme b) transition state c) active site d) enzyme-substrate complex The binding of substrates to most enzymes may be best described as: a) lock and key b) induced fit c) backside attachment d) cofactor displacement
For each of the statements below about the dUTPase enzyme, mark whether it is true or false. If it is false, change the language to make the statement true. _______If the dUTPase enzyme is the rate determining step in a larger metabolic pathway, the reaction likely lies near to equilibrium and is irreversible. _______For the dUTPase reaction, it is not likely that DG’ = DG°’ _______ dUTPase has a higher affinity for its substrate than for its product, but both of these are higher than the affinity for the transition state _______Kinetic analysis of dUTPase using Michaelis-Menten methods assumes that the formation of the E*S complex has a large negative value for DG
When studying the mechanism of the enzymatic reaction, functional groups were found that ensure the connection of the enzyme molecule with the substrate and take a direct part in the act of catalysis. What are these areas of the enzyme formed by these groups called? What functional structures form them and why?
A(n) _________ reaction converts glycylalanine to glycine and alanine. This reaction requires __________. Blank 1 options- Oxidation-reduction Hydrolysis Isomerization Group transfer Internal rearrangement Blank 2 options- H2O and apeptidase or a protease H2O and a phosphatase ADP and a phosphatase NAD+ and a peptidase or a protease
the Km of an enzyme for its substrate is 50mM. At what concentration of substrate would the enzymaticslly catalyzed reaction be at 60% maximum - 30 - 60 -75 - 50 -80
Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
A hypothetical three-step metabolic pathway consists of intermediates W, X, Y, and Z and enzymes A, B, and C. Deduce the order of the enzymatic steps in the pathway from the following information: 1. Compound Q, a metabolic inhibitor of enzyme B, causes Z to build up. 2. A mutant in enzyme C requires Y for growth. 3. An inhibitor of enzyme A causes W, Y, and Z to accumulate. 4. Compound P, a metabolic inhibitor of enzyme C, causes W and Z to build up.

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