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    Introduction To Enzymes

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    Hamsa Ehsan
    1) Enzymes lower the activation energy needed for chemical reactions to occur, allowing reactions to proceed faster. They do this by providing an alternative reaction pathway that requires less energy. 2) Enzymes form complexes with their substrate molecules. This binding of the enzyme and substrate is believed to facilitate the chemical reaction. 3) The activity of enzymes can be affected by various factors like concentration of enzyme and substrate, temperature, and pH. The reaction rate generally increases with increasing enzyme or substrate concentration up to a maximum, and increases with temperature up to an optimal point. Each enzyme also has an optimal pH range for activity.

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    Introduction To Enzymes

    Uploaded by

    Hamsa Ehsan
    24 views6 pages
    1) Enzymes lower the activation energy needed for chemical reactions to occur, allowing reactions to proceed faster. They do this by providing an alternative reaction pathway that requires less energy. 2) Enzymes form complexes with their substrate molecules. This binding of the enzyme and substrate is believed to facilitate the chemical reaction. 3) The activity of enzymes can be affected by various factors like concentration of enzyme and substrate, temperature, and pH. The reaction rate generally increases with increasing enzyme or substrate concentration up to a maximum, and increases with temperature up to an optimal point. Each enzyme also has an optimal pH range for activity.

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    Introduction to Enzymes

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    Introduction to Enzymes

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    1) Enzymes lower the activation energy needed for chemical reactions to occur, allowing reactions to proceed faster. They do this by providing an alternative reaction pathway that requires less energy. 2) Enzymes form complexes with their substrate molecules. This binding of the enzyme and substrate is believed to facilitate the chemical reaction. 3) The activity of enzymes can be affected by various factors like concentration of enzyme and substrate, temperature, and pH. The reaction rate generally increases with increasing enzyme or substrate concentration up to a maximum, and increases with temperature up to an optimal point. Each enzyme also has an optimal pH range for activity.

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    24 views6 pages

    Introduction To Enzymes

    Uploaded by

    Hamsa Ehsan
    1) Enzymes lower the activation energy needed for chemical reactions to occur, allowing reactions to proceed faster. They do this by providing an alternative reaction pathway that requires less energy. 2) Enzymes form complexes with their substrate molecules. This binding of the enzyme and substrate is believed to facilitate the chemical reaction. 3) The activity of enzymes can be affected by various factors like concentration of enzyme and substrate, temperature, and pH. The reaction rate generally increases with increasing enzyme or substrate concentration up to a maximum, and increases with temperature up to an optimal point. Each enzyme also has an optimal pH range for activity.

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    © All Rights Reserved
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    of 6

    Group No.

    Roll No.

     16761
     16726
     16721

    Introduction to Enzymes
    The following has been excerpted from a very popular Worthington
    publication which was originally published in 1972 as the Manual of
    Clinical Enzyme Measurements. While some of the presentation may seem
    somewhat dated, the basic concepts are still helpful for researchers who
    must use enzymes but who have little background in enzymology.

    Enzyme Kinetics: Energy Levels


    Chemists have known for almost a century that for most chemical
    reactions to proceed, some form of energy is needed. They have
    termed this quantity of energy, "the energy of activation." It is the
    magnitude of the activation energy which determines just how fast the
    reaction will proceed. It is believed that enzymes lower the activation
    energy for the reaction they are catalyzing. Figure 3 illustrates this
    concept.

    The enzyme is thought to reduce the "path" of the reaction. This


    shortened path would require less energy for each molecule of
    substrate converted to product. Given a total amount of available
    energy, more molecules of substrate would be converted when the
    enzyme is present (the shortened "path") than when it is absent.
    Hence, the reaction is said to go faster in a given periods of time.

    Enzyme Kinetics: The Enzyme Substrate Complex


    A theory to explain the catalytic action of enzymes was proposed by
    the Swedish chemist Savante Arrhenius in 1888. He proposed that the
    substrate and enzyme formed some intermediate substance which is
    known as the enzyme substrate complex. The reaction can be
    represented as:

    If this reaction is combined with the original reaction equation [1], the
    following results:

    The existence of an intermediate enzyme-substrate complex has been


    demonstrated in the laboratory, for example, using catalase and a
    hydrogen peroxide derivative. At Yale University, Kurt G. Stern
    observed spectral shifts in catalase as the reaction it catalyzed
    proceeded. This experimental evidence indicates that the enzyme first
    unites in some way with the substrate and then returns to its original
    form after the reaction is concluded.

    This is likewise true of enzymatically catalyzed reactions. This is due to


    the reversibility of most reactions. In general:

    where K+1 is the forward reaction rate constant and K-1 is the rate
    constant for the reverse reaction.

    Combining the two reactions gives:


    Applying this general relationship to enzymatic reactions allows the
    equation:

    Equilbrium, a steady state condition, is reached when the forward


    reaction rates equal the backward rates. This is the basic equation
    upon which most enzyme activity studies are based.

    Factors Affecting Enzyme Activity

    Enzyme Concentration
    In order to study the effect of increasing the enzyme concentration
    upon the reaction rate, the substrate must be present in an excess
    amount; i.e., the reaction must be independent of the substrate
    concentration. Any change in the amount of product formed over a
    specified period of time will be dependent upon the level of enzyme
    present. Graphically this can be represented as:

    These reactions are said to be "zero order" because the rates are
    independent of substrate concentration, and are equal to some
    constant k. The formation of product proceeds at a rate which is linear
    with time. The addition of more substrate does not serve to increase
    the rate. In zero order kinetics, allowing the assay to run for double
    time results in double the amount of product.

    Substrate Concentration
    It has been shown experimentally that if the amount of the enzyme is
    kept constant and the substrate concentration is then gradually
    increased, the reaction velocity will increase until it reaches a
    maximum. After this point, increases in substrate concentration will
    not increase the velocity (delta A/delta T). This is represented
    graphically in Figure.

    Temperature Effects
    Like most chemical reactions, the rate of an enzyme-catalyzed reaction
    increases as the temperature is raised. A ten degree Centigrade rise in
    temperature will increase the activity of most enzymes by 50 to 100%.
    Variations in reaction temperature as small as 1 or 2 degrees may
    introduce changes of 10 to 20% in the results. In the case of
    enzymatic reactions, this is complicated by the fact that many
    enzymes are adversely affected by high temperatures. As shown in
    Figure 13, the reaction rate increases with temperature to a maximum
    level, then abruptly declines with further increase of temperature.
    Because most animal enzymes rapidly become denatured at
    temperatures above 40°C, most enzyme determinations are carried
    out somewhat below that temperature.

    Over a period, enzymes will be deactivated at even moderate


    temperatures. Storage of enzymes at 5°C or below is generally the
    most suitable. Some enzymes lose their activity when frozen.

    Effects of pH
    Enzymes are affected by changes in pH. The most favorable pH value -
    the point where the enzyme is most active - is known as the optimum
    pH. This is graphically illustrated in Figure 14.

    Extremely high or low pH values generally result in complete loss of


    activity for most enzymes. pH is also a factor in the stability of
    enzymes. As with activity, for each enzyme there is also a region of pH
    optimal stability.

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