Match the defining characteristics for an enzyme catalyzing a sequential reaction and an enzyme catalyzing adouble-displacement reaction.Sequential reactionreleases one or more products before all substrates bind the enzymeAnswer Bankrequires the binding of all substrates to the enzyme before any product is releasedformation of a temporarily substituted enzyme intermediateDouble-displacement reactionformation of a ternary complex in a bisubstrate reaction

In a sequential enzyme catalyzed reactions all substrates bind in a kind of sequential order to its…

Answered: Sequential reaction releases one or…

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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You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] [E] [ES] O [P] O not enough information provided
Explain all aspects of enzyme kinetics. You must explain all terms that relateto measuring and comparing enzyme velocity. What are the two enzyme"constants" you would teach to a senior level undergraduate course. Howwould you determine values of these under experimental conditions (i.e. invitro).
Several factors contribute to enzyme catalysis. What arethey? Briefly explain the effect of each.
A generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.
Identify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.
Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate  delta delta G〒 on your sketch: Chemical step is rate limiting
An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Michaelis–Menten kinetics Lineweaver–Burk plot Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.
The milieu wherein enzymes occur in vivo is dramatically different from in vitro experiments, which is often used to investigate enzyme. Give an overview of this as well as the nature of enzyme reactions in vivo. Name, in addition, the factors affecting the concentration of enzymes in vivo.
The characterization of an enzyme usually includes the determination of key kinetic parameters. Indicate which of the following statements are true. (This is a multi- select question ). KM is useful to when comparing different substrates, and how well they bind to the enzyme's active site. Kcat is a useful indicator of an enzyme's speed at 1/2 V Vm max is the maximal initial velocity of the enzyme when it is saturated with substrate. An enzyme is considered to approach "catalytic perfection" if it rarely makes an error. Enzymes are usually studied after boiling them in buffer, to remove the chance that contaminating microorganisms are responsible for the observed catalytic events.
True or False Immobilization improves the stability of the enzyme. EnaLne, has a half-life of 10 days in free solution, but under identical conditions of temperature, pH, and medium composition, the measured half-life of a packed column is 30 days. The enzyme is immobilized in a porous sphere 5 mm in diameter.
Which of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active site
Briefly describe why the Michaelis-Menten equilibrium-assumption cannotbe applicable to all enzyme-catalyzed reactions

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