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    Enzymes

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    Bin Hip
    Enzymes are protein catalysts that increase the rate of chemical reactions in living cells without changing themselves. They contain an active site that binds to substrate molecules and converts them to products. Enzymes achieve catalytic efficiency through mechanisms like induced fit binding. Their activity can be regulated and they are located within cells for compartmentalization. Enzyme kinetics are described by the Michaelis-Menten equation and inhibition can be competitive or non-competitive. Factors like temperature, pH, and inhibitors influence enzyme activity. Clinically, enzymes serve as drug receptors and disease biomarkers when their levels are elevated, such as for CPK isoenzymes in muscle damage.

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    Enzymes

    Uploaded by

    Bin Hip
    148 views17 pages
    Enzymes are protein catalysts that increase the rate of chemical reactions in living cells without changing themselves. They contain an active site that binds to substrate molecules and converts them to products. Enzymes achieve catalytic efficiency through mechanisms like induced fit binding. Their activity can be regulated and they are located within cells for compartmentalization. Enzyme kinetics are described by the Michaelis-Menten equation and inhibition can be competitive or non-competitive. Factors like temperature, pH, and inhibitors influence enzyme activity. Clinically, enzymes serve as drug receptors and disease biomarkers when their levels are elevated, such as for CPK isoenzymes in muscle damage.

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    Enzymes are protein catalysts that increase the rate of chemical reactions in living cells without changing themselves. They contain an active site that binds to substrate molecules and converts them to products. Enzymes achieve catalytic efficiency through mechanisms like induced fit binding. Their activity can be regulated and they are located within cells for compartmentalization. Enzyme kinetics are described by the Michaelis-Menten equation and inhibition can be competitive or non-competitive. Factors like temperature, pH, and inhibitors influence enzyme activity. Clinically, enzymes serve as drug receptors and disease biomarkers when their levels are elevated, such as for CPK isoenzymes in muscle damage.

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    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    148 views17 pages

    Enzymes

    Uploaded by

    Bin Hip
    Enzymes are protein catalysts that increase the rate of chemical reactions in living cells without changing themselves. They contain an active site that binds to substrate molecules and converts them to products. Enzymes achieve catalytic efficiency through mechanisms like induced fit binding. Their activity can be regulated and they are located within cells for compartmentalization. Enzyme kinetics are described by the Michaelis-Menten equation and inhibition can be competitive or non-competitive. Factors like temperature, pH, and inhibitors influence enzyme activity. Clinically, enzymes serve as drug receptors and disease biomarkers when their levels are elevated, such as for CPK isoenzymes in muscle damage.

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    of 17

    ENZYMES

    PHARMACEUTICAL BIOCHEMISTRY
    ENZYMES
    -- protein catalysts for chemical reactions in biological systems
    -- increase the rate of chemical reactions taking place within living
    cells without changing themselves

    SUBSTRATE
    -- molecule being acted upon by an enzyme
    -- molecule that enters into an enzymatic reaction

    ZYMOGEN
    -- inactive form of an enzyme
    ENZYMES
    APOENZYME
    -- protein portion of an enzyme
    -- enzyme without a bound non-protein component

    HOLOENZYME
    -- Active form of the enzyme
    -- Apoenzyme + NON-PROTEIN COMPONENT
    COENZYME
     small organic molecule
     derived from vitamins
    COSUBSTRATE – transient association
    PROSTHETIC GROUP – permanent association
    ENZYMES
    COENZYME VITAMIN SOURCE FUNCTION
    Thiamine pyrophosphate Vitamin B1 Aldehyde group transfer
    FAD Vitamin B2 Electron transfer
    NAD Vitamin B3 Electron transfer
    Coenzyme A Vitamin B5 Acetyl group transfer
    Pyridoxal Phosphate Vitamin B6 Amino group transfer
    ENZYMES
    HOLOENZYME
    -- Apoenzyme + NON-PROTEIN COMPONENT
    COFACTOR
     metal ion -- Metalloenzymes

    METAL METALLOENZYME
    Zinc Carbonic anhydrase, alcohol dehydrogenase
    Magnesium Hexokinase
    Copper Tyrosinase, Cytochrome oxidase, Superoxide Dismutase
    Iron Cytochrome Oxidase, Catalase, Peroxidase, Xanthine Oxidase
    Selenium Glutathione peroxidase
    ENZYME CLASSIFICATION
    ENZYME CLASSIFICATION
    ENZYMES PROPERTIES
    A. ACTIVE SITE
    -- enzymes contain as special pocket/ cleft

    B. CATALYTIC EFFICIENCY
    -- enzyme-catalyzed reactions are efficient, proceeding from 103-108
    times faster than uncatalyzed reactions

    C. SPECIFICITY
    -- enzymes are highly specific, interacting with one or few substrates
    and catalyzing only one type of chemical reaction
    ENZYMES PROPERTIES
    D. REGULATION
    -- enzyme activity can be regulated, that is,
    increased or decreased, so that the rate of
    product formation responds to cellular need

    E. LOCATION WITHIN THE CELL


    -- compartmentalization to isolate cellular
    reactions
    MODELS of ENZYME-SUBSTRATE BINDING
    A. FISCHER’S TEMPLATE THEORY
    -- lock and key
    -- the 3-D structure of the enzyme’s active site is
    complementary to the substrate

    B. KOSHLAND’S INDUCED-FIT THEORY


    -- conformational changes by the enzyme to accommodate
    the substrate
    MODE of ACTION of ENZYMES
    A. TRANSITION-STATE ANALOGUE MODEL
    -- virtually all chemical reactions have an
    energy barrier separating the reactants and
    the products

    -- TRANSITION STATE

    -- FREE ENERGY OF ACTIVATION


    High energy of activation  SLOW
     without enzymes; insufficient
    energy to achieve the transition
    state
    ENZYME KINETICS
    A. MICHAELIS-MENTEN EQUATION
    REACTION MODEL

    EQUATION
    ENZYME KINETICS
    B. LINEWEAVER-BURK PLOT
    EQUATION
    -- used to identify inhibition of enzyme
    activity
    -- any substance that can diminish the
    velocity of an enzyme-catalyzed
    reaction is called an INHIBITOR
    ENZYME KINETICS
    B. LINEWEAVER-BURK PLOT
    A. COMPETITIVE INHIBITION
    ENZYME KINETICS
    B. LINEWEAVER-BURK PLOT
    B. NON-COMPETITIVE INHIBITION
    FACTORS INFLUENCING ENZYME ACTIVITY
    1. ENZYME CONCENTRATION
    2. SUBSTRATE CONCENTRATION
    3. EFFECT OF CONCENTRATION OF PRODUCTS
    4. EFFECT OF TEMPERATURE
    5. EFFECT OF pH
    6. ENZYME ACTIVATION
    7. ENZYME INHIBITION
    CLINICAL IMPORTANCE OF ENZYMES
    1. Serve as Drug Receptors

    2. Disease Biomarkers

    Assignment:
    Enzyme Disease associated if levels 1. Creatine Kinase (CPK 1, 2 , and 3)
    are elevated 2. Lactate Dehydrogenase
    3. Alkaline Phosphatase
    4. ALT and AST
    5. GGT
    6. PSA
    7. Acetylcholinesterase

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