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Discuss two ways in which drugs prevent ...

Discuss two ways in which drugs prevent the attachment of native substrate on active site of an enzyme.

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Name one type of bond that bind substrates to the active sites of the enzymes.

Amino acid serine , aspratic acid and phenylalamine are present on the active site of an enzyme . Exaplain which forces may be involved in binding the durg to the enzyme if the drug inhibits the holding of substrate on the active site of enzyme .

Knowledge Check

  • Active site of an enzyme is formed of

    A
    Amino groups of some amino acids.
    B
    Carboxyl groups of some amino acids
    C
    `-"HS bonds of amino acids"`
    D
    R-groups of selected amino acids

  • Drugs which inhibit the attachment of substrate on active site of enzymers by binding to allosteric site are called

    A
    Enzyme inhibitors
    B
    Noncompetitive inhibitors
    C
    Both (1) and (2)
    D
    Competitive inhibitors

  • Active site of enzyme is formed by

    A
    Primary structure of protein
    B
    Secondary structure of protein
    C
    Tertiary structure of proteoin
    D
    Quaternary structure of protein

    • Similar Questions

    Explore conceptually related problems

    Amino acids serine, aspartic acid and phenylalanine are present on the active site of an enzyme . Structure of these amino acids are given in the book. Explain which forces may be involved in binding the drug to the enzyme if the drug inhibits the holding of substrate on the active site of enzyme/

    State two ways by which rusting can be prevented ?

    Number of active sites in allosteric enzyme is

    Assertion : Enzymes have active sites that hold substrate molecule for a chemical reaction. Reason : Drugs complete with natural substrate by attaching covalently to the active site of enzyme.

    Assertion : Competitiv inhibitros compete with the natural substrate for their attachment on the active sites of enzymes. Reason : In competitive inhibition, inhibitor binds to allosteric site of the enzyme.

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