Scribd Logo
Upload

Welcome to Scribd!

  • 89 views

    Enzymes: A Protein With Catalytic Properties Due To Its Power of Specific Activation

    Uploaded by

    Akash Singh
    Enzymes are protein catalysts that speed up chemical reactions by lowering the activation energy. They are highly specific and function optimally at body temperature, pH, and pressure. Enzymes achieve their catalytic power and specificity through precise binding of substrates in their active sites. While some environmental factors like temperature and pH can impact enzyme function, inhibitors are chemicals that directly reduce enzymatic reaction rates, and are used in both drugs and poisons.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPT, PDF, TXT or read online from Scribd

    Enzymes: A Protein With Catalytic Properties Due To Its Power of Specific Activation

    Uploaded by

    Akash Singh
    89 views35 pages
    Enzymes are protein catalysts that speed up chemical reactions by lowering the activation energy. They are highly specific and function optimally at body temperature, pH, and pressure. Enzymes achieve their catalytic power and specificity through precise binding of substrates in their active sites. While some environmental factors like temperature and pH can impact enzyme function, inhibitors are chemicals that directly reduce enzymatic reaction rates, and are used in both drugs and poisons.

    Original Title

    Lecture 9 Enzymes

    Copyright

    © Attribution Non-Commercial (BY-NC)

    Available Formats

    PPT, PDF, TXT or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    Enzymes are protein catalysts that speed up chemical reactions by lowering the activation energy. They are highly specific and function optimally at body temperature, pH, and pressure. Enzymes achieve their catalytic power and specificity through precise binding of substrates in their active sites. While some environmental factors like temperature and pH can impact enzyme function, inhibitors are chemicals that directly reduce enzymatic reaction rates, and are used in both drugs and poisons.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    89 views35 pages

    Enzymes: A Protein With Catalytic Properties Due To Its Power of Specific Activation

    Uploaded by

    Akash Singh
    Enzymes are protein catalysts that speed up chemical reactions by lowering the activation energy. They are highly specific and function optimally at body temperature, pH, and pressure. Enzymes achieve their catalytic power and specificity through precise binding of substrates in their active sites. While some environmental factors like temperature and pH can impact enzyme function, inhibitors are chemicals that directly reduce enzymatic reaction rates, and are used in both drugs and poisons.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    You are on page 1of 35

    ENZYMES

    A protein with catalytic properties due to its


    power of specific activation
    Enzymes speed up chemical reactions
    ENZYMES
     In the test tube, catalysts such as charcoal and
    platinum facilitate reactions but usually only
    at high temperatures or pressures, at extremes
    of high or low pH, or in organic solvents.
     As the cell’s protein catalysts, however,
    enzymes must function effectively in aqueous
    environment at 37C, 1 atmosphere pressure,
    and pH 6.5–7.5.
    ENZYMES
     Two striking properties
     1. Enormous Catalytic Power
    rates of enzymatically catalyzed reactions to be 106–1012 times that of the
    corresponding uncatalyzed reactions under otherwise similar conditions.

     2. Specificity
    enzyme-catalyzed reactions of L-amino acids take place much more rapidly than do
    those of D-amino acids, even though both stereoisomers of a given amino acid are
    the same size and possess the same R groups
     Around 3700 different enzymes in enzyme database.
     Some common (like protein, nucleic acid, phospholipid synthesis)
     Some specific (like for conversion of tyrosine to dopamine (a neurotransmitter) in
    nerve cells)
    Chemical reactions
     Every chemical reaction between molecules
    - involves bond breaking and bond forming
     The initial energy needed to start a chemical reaction
    -called the free energy of activation (Activation energy
    (AE)
     During this part of the reaction the molecules are said to
    be in a transition state.
     Activation energy is often supplied in the form of heat
    from the surroundings
    Making reactions go faster
     Increasing the temperature make molecules move faster
     Biological systems are very sensitive to temperature
    changes.
     Enzymes can increase the rate of reactions without
    increasing the temperature.
     They do this by lowering the activation energy.
     They create a new reaction pathway “a short cut”
     Enzymes do not affect the change in free energy (ΔG),
    instead they hasten reactions that would occur eventually
     (thus would catalyze only energy favourable reactions)
    Reaction Pathway
    An enzyme controlled pathway

     As the cell’s protein catalysts, however, enzymes must function


    effectively in aqueous environment at 37C, 1 atmosphere pressure, and
    pH 6.5–7.5.
    Enzyme structure
     Enzymes are
    proteins
     They have a
    globular shape
     A complex 3-D
    structure

    Human pancreatic amylase


    The active site
     The region on the
    enzyme where substrate
    binds is called the active
    site.
     The shape and the
    chemical environment
    inside the active site
    permits a chemical
    reaction to proceed more
    easily
    ACTIVE SITE
     Certain amino acid side chains of an enzyme are important in determining its
    specificity and catalytic power. In the native conformation of an enzyme,
    these side chains are brought into proximity, forming the active site.
     Active sites thus consist of two functionally important regions:
    1. Substrate recognition and binding
    2. catalytic –the one that catalyzes reaction once substrate is bound.
    In some enzymes, the catalytic region is part of the substrate-binding region;
    in others, the two regions are structurally as well as functionally distinct.
    Cofactors
     Non-protein enzyme helpers
    Cytochroma C with
     Organic cofactors can be heme coenzyme
    1. Tightly bound cofactors are )

    called prosthetic groups


    2. Cofactors that are bound and
    released easily are called
    coenzymes (NADH,
    NADPH, ATP)
     Many vitamins are
    coenzymes
     Vitamin C (Ascorbic Acid-
    Scurvy)

    Nitrogenase enzyme with Fe, Mo and ADP cofactors


    )
    The substrate
     The substrate of an enzyme are the reactants
    that are activated by the enzyme
     Enzymes are specific to their substrates
     The specificity is determined by the active
    site
    The Lock and Key Hypothesis
     Fit between the substrate and the active site of the enzyme is
    exact
     Like a key fits into a lock very precisely
     The key is analogous to the enzyme and the substrate
    analogous to the lock.
     Temporary structure called the enzyme-substrate complex
    formed
     Products have a different shape from the substrate
     Once formed, they are released from the active site
     Leaving it free to become attached to another substrate
    The Lock and Key Hypothesis

    S
    E
    E
    E

    Enzyme- Enzyme may


    substrate be used again
    complex P

    Reaction coordinate
    The Lock and Key Hypothesis
     This explains enzyme specificity
     This explains the loss of activity when
    enzymes denature
    The Induced Fit Hypothesis
     Some proteins can change their shape
    (conformation)
     When a substrate combines with an enzyme, it
    induces a change in the enzyme’s conformation
     The active site is then moulded into a precise
    conformation
     Making the chemical environment suitable for the
    reaction
     The bonds of the substrate are stretched to make the
    reaction easier (lowers activation energy)
    The Induced Fit Hypothesis

    Hexokinase (a) without (b) with glucose substrate

     This explains the enzymes that can react with a


    range of substrates of similar types
    Factors affecting Enzymes
     substrate concentration
     pH
     temperature
     inhibitors
    Substrate concentration: Non-enzymic reactions

    Reaction
    velocity

    Substrate concentration

     The increase in velocity is proportional to the


    substrate concentration
    Substrate concentration: Enzymic reactions

    Vmax

    Reaction
    velocity

    Substrate concentration
     Faster reaction but it reaches a saturation point when all the
    enzyme molecules are occupied.
     If you alter the concentration of the enzyme then Vmax will
    change too.
    The effect of pH
     Extreme pH levels will produce denaturation
     The structure of the enzyme is changed
     The active site is distorted and the substrate
    molecules will no longer fit in it
     At pH values slightly different from the enzyme’s
    optimum value, small changes in the charges of the
    enzyme and it’s substrate molecules will occur
     This change in ionisation will affect the binding of
    the substrate with the active site.
    The effect of pH
    The effect of temperature
     For most enzymes the optimum temperature is about
    30°C
     Many are a lot lower, cold water fish will die at
    30°C because their enzymes denature
     A few bacteria have enzymes that can withstand very
    high temperatures up to 100°C
     Most enzymes however are fully denatured at 70°C
    The effect of temperature
    Enzymes in a Common Pathway constitute
    multienzyme complexes
    Structure and function of pyruvate
    dehydrogenase, a large multimeric enzyme
    complex that converts pyruvate into acetyl CoA.

    (a) The complex consists of 24 copies of pyruvate


    decarboxylase (E1), 24 copies of lipoamide
    transacetylase (E2), and 12 copies of dihydrolipoyl
    dehydrogenase (E3). The E1 and E3 subunits are
    bound to the outside of the core formed by the E2
    subunits.

    (b) The reactions catalyzed by the complex include


    several enzyme-bound intermediates (not shown).
    The tight structural integration of the three
    enzymes increases the rate of the overall reaction
    and minimizes possible side reactions.
    COMPARTMENTALIZATION
    Cells have another way of increasing the rate of metabolic reactions.

    A large increase in the concentration of interacting molecules can be achieved by


    confining them to the same membrane-bounded compartment as in a eucaryotic cell.
    If, for example, the compartment occupies a total of 10% of the volume of the cell,
    the concentration of reactants in the compartment can be 10 times greater than in a
    similar cell with no compartmentalization
    Inhibitors
     Inhibitors are chemicals that reduce the rate
    of enzymic reactions.
     The are usually specific and they work at low
    concentrations.
     They block the enzyme but they do not
    usually destroy it.
     Many drugs and poisons are inhibitors of
    enzymes in the nervous system.
    Enzyme inhibitors
    Allosteric Inhibition
    Allosteric activation results when the
    binding of an activator molecule to an
    allosteric site causes a change in the active
    site that makes it capable of binding
    substrate.

    Allosteric (noncompetitive) inhibition results


    from a change in the shape of the active site
    when an inhibitor binds to an allosteric site.
    When this occurs the substrate cannont bind
    to it's active site due to the fact that the
    active site has changed shape and the
    substrate no longer fits.
    Feedback Inhibition
    Uses of inhibitors
     Since inhibitors modulate the function of enzymes they are
    often used as drugs. An common example of an inhibitor that
    is used as a drug is aspirin, which inhibits the COX-1 and
    COX-2 enzymes that produce the inflammation messenger
    prostaglandin, thus suppressing pain and inflammation.
     However, other enzyme inhibitors are poisons. For example,
    the poison cyanide is an irreversible enzyme inhibitor that
    combines with the copper and iron in the active site of the
    enzyme cytochrome c oxidase and blocks cellular respiration.
    [69
    INDUSTRIAL APPLICATIONS

    Dairy Industry-
    Laundry Industry- Baking Industry- Rennin
    Proteases, lipases Amylase Manufacture of cheese
    Brewing Industry-
    Amylase, glucanase, protease
    Split polysaccharide and proteins in malt
    INDUSTRIAL APPLICATIONS

    Paper Industry- Meat Tenderizer


    Amylases, Xylanases, Papain Molecular Biology
    Cellulases and Ligases, Restriction enzymes PCR
    ligninases
    INDUSTRIAL APPLICATIONS
     Up until now, the jeans have gone through the same
    procedure, and it is during finishing that jeans are
    betrothed their own colour and personality. Formerly,
    jeans were sanded roughly with pumice stones
    ( stonewashing), placing the stones and fabric in a
    rotating washing machine to achieve the faded look.
    However, since pumice stones are volcanic rock, they
    are strip-mined and therefore not very environmentally
    friendly. In addition, a small amount of enzyme can do
    the same job as several kilograms of pumice stones,
    plus laundry machines can then contain fewer stones
    and more garments, increasing productivity.

    Textile Industry-
    amylase, pectinase, catalase and cellulase

    You might also like