Fill in the blanks.:WriteCif 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 enzyme catalyzes a reaction by providing an alternative reaction pathwaythat has a lower energy of activation.B. The enthalpy of the enzyme-catalyzed reaction decreases significantly as compared to theuncatalyzed reaction.

Enzymes are the biological catalysts which enhance the rate of reaction.

Answered: Hif only statement B is correct, E if…

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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Write Cif only statement A is correct, Hif only statement B is correct, Eif both statements are correct, Mif both statements are incorrect. A. A lower Ky reflects a less efficient enzyme. B. The KM is equivalent to the substrate concentration at 50% of the reaction's velocity limit.
Which of the following is NOT true? a. For many enzymes, Vmax is essentially equal to k3. b. Km is the reaction rate at 1/2 Vmax. c. At steady state the formation of ES is equal to the breakdown of ES. d. A Lineweaver-Burke plot generates a straight line. e. An Eadie-Hofstee plot generates a straight line.
Enzymes work by lowering the energy of activation. True O False QUESTION 10 The enzyme stabilizes the transition-state complex more than it stabilizes the substrate complex. O True O False QUESTION 11 Which of the following statement is FALSE ? pKa values of active site residues can be shifted from typical pKa values Enzymes increase Keq Near attack complexes have reacting molecules close enough to form Va der Waals contacts O The transition state contains at least one partial bond. QUESTION 12 The angle m in a peptide best describes: it Glick Save All Answers to save all answers. 78 F Mostly cioudy
please answer
1. ( . tion can be represented by the so-called Michaelis equation ) The velocity of an enzyme catalyzed reac- Vmax [S] Vo = Km Vo = max kcat [Eo] [So] (Км + [Sol) V max where [So] is the initial substrate concentration, [Eo] is the total enzyme concentration, kcat is the cataly- tic rate constant or turnover number, and KM repre- sents the Michaelis constant. The graph on the right illustrates the dependence of the velocity of the reaction as a function of substrate concentration. Ex- Km [S] (mm) plain why the maximal velocity can be represented by the expression Vmax = Kcat [Eo] at very high substrate concentrations. Vo (µm/min)
Please help with both the parts
In Lineweaver Burk plot: O a. The slope of the plot is the Vmax/Km O b. The intercept on X-axis is 1/Km. O c. The intercept on y-axis is 1/Vmax O d. double-reciprocal plot of enzyme kinetics is generated, where 1/VO is plotted as a function [S]. O e. All answers are correct
ANSWER A AND B PLS
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
Select all FALSE statements about allosteric enzymes. a. They interconvert between a more active form and a less active form. b. They tend to have a hyperbolic curve of ?0 vs. [S]. c.They conform to Michaelis–Menten kinetics. d. They are generally small single subunit proteins. e. They may have binding sites for regulatory molecules that are separate from active sites.
Correct option carefully asap
Although we have introduced catalytic strategies separately, an enzyme typically employs more than one during a reaction. The catalytic strategies employed by serine protease include: Select one or more: O a. reduction of ASt b. transition state stabilization Oc. metal-assisted catalysis O d. acid/base catalysis O e. covalent catalysis

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