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    Inhibition: Maria Roceline P. Sandoy 2MT01

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    Roceline Sandoy
    There are two main types of enzyme inhibitors - irreversible and reversible. Irreversible inhibitors chemically modify the enzyme and permanently inactivate it, while reversible inhibitors bind non-covalently and can be overcome by increasing substrate concentration. Reversible inhibitors are further classified as competitive, uncompetitive, or non-competitive based on how they affect the Michaelis-Menten kinetics parameters of Km and Vmax. Competitive inhibitors increase Km but not Vmax, uncompetitive inhibitors decrease both, and non-competitive inhibitors decrease Vmax but not Km. Enzyme inhibitors have important applications as drugs, poisons, herbicides, and more.

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    Inhibition: Maria Roceline P. Sandoy 2MT01

    Uploaded by

    Roceline Sandoy
    74 views15 pages
    There are two main types of enzyme inhibitors - irreversible and reversible. Irreversible inhibitors chemically modify the enzyme and permanently inactivate it, while reversible inhibitors bind non-covalently and can be overcome by increasing substrate concentration. Reversible inhibitors are further classified as competitive, uncompetitive, or non-competitive based on how they affect the Michaelis-Menten kinetics parameters of Km and Vmax. Competitive inhibitors increase Km but not Vmax, uncompetitive inhibitors decrease both, and non-competitive inhibitors decrease Vmax but not Km. Enzyme inhibitors have important applications as drugs, poisons, herbicides, and more.

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    INHIBITION report

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    There are two main types of enzyme inhibitors - irreversible and reversible. Irreversible inhibitors chemically modify the enzyme and permanently inactivate it, while reversible inhibitors bind non-covalently and can be overcome by increasing substrate concentration. Reversible inhibitors are further classified as competitive, uncompetitive, or non-competitive based on how they affect the Michaelis-Menten kinetics parameters of Km and Vmax. Competitive inhibitors increase Km but not Vmax, uncompetitive inhibitors decrease both, and non-competitive inhibitors decrease Vmax but not Km. Enzyme inhibitors have important applications as drugs, poisons, herbicides, and more.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPTX, PDF, TXT or read online from Scribd
    Download as pptx, pdf, or txt
    74 views15 pages

    Inhibition: Maria Roceline P. Sandoy 2MT01

    Uploaded by

    Roceline Sandoy
    There are two main types of enzyme inhibitors - irreversible and reversible. Irreversible inhibitors chemically modify the enzyme and permanently inactivate it, while reversible inhibitors bind non-covalently and can be overcome by increasing substrate concentration. Reversible inhibitors are further classified as competitive, uncompetitive, or non-competitive based on how they affect the Michaelis-Menten kinetics parameters of Km and Vmax. Competitive inhibitors increase Km but not Vmax, uncompetitive inhibitors decrease both, and non-competitive inhibitors decrease Vmax but not Km. Enzyme inhibitors have important applications as drugs, poisons, herbicides, and more.

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    of 15

    INHIBITION

    MARIA ROCELINE P. SANDOY


    2MT01
    Enzyme inhibitor

    • molecule that binds to enzymes and decreases their


    activity. Molecule that interact in some way with the
    enzyme to prevent it from working in the normal
    manner.
    • The binding of an inhibitor can stop a substrate from
    entering the enzyme's active site and/or hinder the
    enzyme from catalyzing its reaction.
    CLASSIFICATION:
    • IRREVERSIBLE INHIBITORS
    -usually react with the enzyme and change it chemically. These
    inhibitors modify key amino acids residues needed for enzymatic
    activity.
    -enzymes undergo irreversible inactivation when they are treated with
    agent capable of covalently and permanently modifying a functional
    group required for catalysis, making the enzyme molecule inactive
    •REVERSIBLE INHIBITORS

    -bind non-covalently and different types of inhibition are


    produced depending on whether these inhibitors bind the
    enzyme, the enzyme-substrate complex, or both.
    -it has three major types: Competitive, Uncompetitive and
    Non-competitive which can be experimentally distinguished
    by the effects of the inhibitors on the reaction kinetics of the
    enzyme, which maybe analyzed in terms of the basic
    Michaelic-Menten rete equation.
    Michaelis-Menten kinetics

    -is a model of enzyme kinetics.


    -describes the rates of irreversible
    enzymatic reactions by relating reaction
    rate to the concentration of the
    substrate.
    FORMULA:

    Vo = initial velocity

    Vmax = maximum reaction rate

    Km =Michaelic-Menten Constant

    [S] = substrate concentration


    • There are three kinds of reversible enzyme inhibitors. They
    are classified according to the effect of varying the
    concentration of the enzyme's substrate on the inhibitor

    3KINDS:
     COMPETITIVE
     UNCOMPETITIVE
     NON COMPETITIVE
    •Competitive Inhibition
    -at any given moment, the enzyme may be bound to the inhibitor,
    the substrate, or neither, but it cannot bind both at the same time.
    -In competitive inhibition, the maximum velocity (Vmax) of the
    reaction is unchanged, while the apparent affinity of the substrate to
    the binding site is decreased (the Kd dissociation constant is
    apparently increased). The change in Km (Michaelis-Menten
    constant) is parallel to the alteration in Kd. Any given competitive
    inhibitor concentration can be overcome by increasing the substrate
    concentration in which case the substrate will outcompete the
    inhibitor in binding to the enzyme.
    • EQUATION:
    E + I = EI
    • Dissociate constant:
    KI = (E)(I)/(EI)

    -Competitive inhibitors can bind to E, but not to


    ES. Competitive inhibition increases Km (i.e., the
    inhibitor interferes with substrate binding), but
    does not affect Vmax (the inhibitor does not
    hamper catalysis in ES because it cannot bind to
    ES).
    • Uncompetitive inhibitor
    This reduction in the effective concentration to
    the E-S complex increases the enzyme's
    apparent affinity for the substrate through Le
    Chatelier's principle (Km is lowered) and
    decreases the maximum enzyme activity (Vmax),
    as it takes longer for the substrate or product to
    leave the active site. Uncompetitive inhibition
    works best when substrate concentration is high.
    An uncompetitive inhibitor need not resemble
    the substrate of the reaction it is inhibiting.
    • EQUATION:
    ES + I = ESI
    • INHIBITOR CONSTANT
    KI = (ES)(I)/(ESI)
    •Non-competitive inhibition
    • This type of inhibition reduces the maximum rate of a
    chemical reaction without changing the apparent binding
    affinity of the catalyst for the substrate

    • Non-competitive inhibition models a system where the


    inhibitor and the substrate may both be bound to the
    enzyme at any given time. When both the substrate and the
    inhibitor are bound, the enzyme-substrate-inhibitor
    complex cannot form product and can only be converted
    back to the enzyme-substrate complex or the enzyme-
    inhibitor complex. Non-competitive inhibition is
    distinguished from general mixed inhibition in that the
    inhibitor has an equal affinity for the enzyme and the
    enzyme-substrate complex.
    • EQUATION:
    E + I = EI
    or
     ES + I = ESI

    INHIBITOR CONSTANT:
    KI=(E)(I)/(EI)
    or
    KI=(ES)(I)/(ESI)

    -Non-competitive inhibitors have identical affinities for E


    and ES (Ki = Ki'). Non-competitive inhibition does not
    change Km (i.e., it does not affect substrate binding) but
    decreases Vmax (i.e., inhibitor binding hampers catalysis).
    Uses of inhibitors

    • Enzyme inhibitors are found in nature and are also


    designed and produced as part of pharmacology and
    biochemistry. Natural poisons are often enzyme inhibitors
    that have evolved to defend a plant or animal against
    predators. These natural toxins include some of the most
    poisonous compounds known. Artificial inhibitors are
    often used as drugs, but can also be insecticides such as
    malathion, herbicides such as glyphosate, or disinfectants
    such as triclosan.
    …END…

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