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    MCQ Adua

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    AG Khan
    This document contains 20 multiple choice questions assessing knowledge of key concepts in enzyme kinetics and regulation. The questions cover topics such as the historical discovery of enzymes and biological catalysts in the late 1600s and early 1700s; early experiments revealing the existence of enzymes like pepsin, trypsin, and yeast; models of enzyme action including the lock and key and induced fit models; properties of allosteric enzymes including sigmoidal kinetics and regulation by effectors; and concepts like cooperativity, K0.5, and how heterotropic allosteric enzymes can have a lower K0.5 when an activator binds.

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    MCQ Adua

    Uploaded by

    AG Khan
    140 views4 pages
    This document contains 20 multiple choice questions assessing knowledge of key concepts in enzyme kinetics and regulation. The questions cover topics such as the historical discovery of enzymes and biological catalysts in the late 1600s and early 1700s; early experiments revealing the existence of enzymes like pepsin, trypsin, and yeast; models of enzyme action including the lock and key and induced fit models; properties of allosteric enzymes including sigmoidal kinetics and regulation by effectors; and concepts like cooperativity, K0.5, and how heterotropic allosteric enzymes can have a lower K0.5 when an activator binds.

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    Enzymes chapters MCQ's with answer

    Original Title

    116553658-Mcq-Adua

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    This document contains 20 multiple choice questions assessing knowledge of key concepts in enzyme kinetics and regulation. The questions cover topics such as the historical discovery of enzymes and biological catalysts in the late 1600s and early 1700s; early experiments revealing the existence of enzymes like pepsin, trypsin, and yeast; models of enzyme action including the lock and key and induced fit models; properties of allosteric enzymes including sigmoidal kinetics and regulation by effectors; and concepts like cooperativity, K0.5, and how heterotropic allosteric enzymes can have a lower K0.5 when an activator binds.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    140 views4 pages

    MCQ Adua

    Uploaded by

    AG Khan
    This document contains 20 multiple choice questions assessing knowledge of key concepts in enzyme kinetics and regulation. The questions cover topics such as the historical discovery of enzymes and biological catalysts in the late 1600s and early 1700s; early experiments revealing the existence of enzymes like pepsin, trypsin, and yeast; models of enzyme action including the lock and key and induced fit models; properties of allosteric enzymes including sigmoidal kinetics and regulation by effectors; and concepts like cooperativity, K0.5, and how heterotropic allosteric enzymes can have a lower K0.5 when an activator binds.

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    MCQ

    1. When the biological catalyst was first recognized?


    A. Early 1600s.

    B. late 1600s

    C. early 1700s

    D. late 1700s

    2. Which experiment first revealed the existence of biological catalyst?


    A. digestion of meat by stomach secretion B. conversion of starch to sugar by saliva
    C. fermentation of sugar by yeast

    D. none of them.

    3. Who was the discoverer of the function ability of enzyme without the
    presence of the cell?
    A. Louis Pasteur B. Eduard Buchner. C. Sumner D. None of them.
    4. Pepsin, trypsin were crystallized by
    A. John Northrop B. Moses Kunitz C. Both of them D. Sumner
    5. Enzyme- was named by
    A. Linus Pauling B. Haldane C. Kuhne D. William Jencks
    6. Sumners postulation all enzymes are protein was widely accepted inA. 1927

    B. 1930

    C. 1830

    D. 1929

    7. Enzyme substrate complex was first proposed by


    A. Michael Polanyi, 1921
    D. None of them.

    B. Wurtz, 1903

    C. Charles-Adolph Wurtz, 1880

    8. Enzyme - was written by


    A. Kuhne

    B. Kunitz C. Haldane

    D. Wurtz

    9. Lock and Key model was proposed by Emile Fisher in


    A. 1890

    B. 1891 C. 1892 D. 1894

    10. Daniel Koshland gave which model?


    A. lock and key

    B. induced fit.

    C. sequential model

    D. both B & C

    E. only B
    11. Allosteric enzymes are regulated by the binding ofA. Allosteric modulators B. Allosteric effectors

    C. both of them D. regulators

    12. Fine tuning of metabolic pathways are done by


    A. Allosteric non covalent regulation B. Allosteric regulation
    C. Covalent modification

    D. Irreversible regulation

    13. When does the enzyme call as heterotropic?


    A. same substrate and modulator

    B. different substrate and modulator

    C. different substrate and inhibitor

    D. none of them

    14. When the enzyme is homotropic?


    A. same substrate and inhibitor

    B. same substrate and product

    C. same substrate and modulator

    D. all of them

    15. What is the property of homotropic enzyme?


    A.

    same active site and regulatory site

    B.

    active site and regulatory site both are in different subunits

    C.

    modulator binds covalently

    D.

    none of them
    16. Which kinetic behavior belongs to Allosteric enzymes?

    A. follow Michaelis-Menten behavior fully


    B. show hyperbolic curve in V0 vs. S
    C. show sigmoid curve in V0 vs. S
    D. show parabolic curve in V0 vs. S
    17. The substrate concentration giving half maximal velocity of reaction
    catalyzed by an allosteric enzyme is represented byA. km

    B. k0.5

    C. S0.5

    D. both B & C

    E. both A & C

    18. Cooperative interactions between protein subunits are reflected byA. hyperbolic curve in V vs. S diagram
    B. sigmoid curve in V vs. S diagram
    C. linear relationship between V & S
    D. all of them
    19. Which two models explain sigmoid kinetic behave?
    A. lock and key & induced fit model
    B. concerted model & sequential model
    C. MWC model & sequential model
    D. both B & C
    20. When does the k0.5 become lower in case of heterotropic allosteric enzymes?
    A. when inhibitor binds to the enzyme
    B. when the substrate concentration rises
    C. when the activator binds to the enzyme
    D. all of them

    ANSWER
    1.D 2.A. 3.B 4.C 5.C 6.B 7.C 8.C 9.D 10.D 11.C
    14. C 15.A 16.C 17.C

    18.B

    19.D

    20.C

    12.A 13.B

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