Scribd Logo
Upload

Welcome to Scribd!

  • 122 views

    BIO307 Lecture 5 (Enzyme Kinetics I)

    Uploaded by

    Phenyo Mmereki
    Enzymes accelerate reactions by lowering the activation energy needed to reach the transition state through the formation of an enzyme-substrate complex, in which the substrate binds to the active site of the enzyme via weak interactions. This facilitates the formation of the transition state and increases the reaction rate by increasing the concentration of the transition state, as enzymes precisely lower the free energy of activation. While enzymes alter only the reaction rate and not the equilibrium, they accelerate both the forward and reverse reactions to the same degree, reaching equilibrium faster than non-enzymatic reactions.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd

    BIO307 Lecture 5 (Enzyme Kinetics I)

    Uploaded by

    Phenyo Mmereki
    122 views11 pages
    Enzymes accelerate reactions by lowering the activation energy needed to reach the transition state through the formation of an enzyme-substrate complex, in which the substrate binds to the active site of the enzyme via weak interactions. This facilitates the formation of the transition state and increases the reaction rate by increasing the concentration of the transition state, as enzymes precisely lower the free energy of activation. While enzymes alter only the reaction rate and not the equilibrium, they accelerate both the forward and reverse reactions to the same degree, reaching equilibrium faster than non-enzymatic reactions.

    Original Description:

    Original Title

    BIO307 Lecture 5 (Enzyme kinetics I).ppt

    Copyright

    © © All Rights Reserved

    Available Formats

    PPT, PDF, TXT or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    Enzymes accelerate reactions by lowering the activation energy needed to reach the transition state through the formation of an enzyme-substrate complex, in which the substrate binds to the active site of the enzyme via weak interactions. This facilitates the formation of the transition state and increases the reaction rate by increasing the concentration of the transition state, as enzymes precisely lower the free energy of activation. While enzymes alter only the reaction rate and not the equilibrium, they accelerate both the forward and reverse reactions to the same degree, reaching equilibrium faster than non-enzymatic reactions.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    122 views11 pages

    BIO307 Lecture 5 (Enzyme Kinetics I)

    Uploaded by

    Phenyo Mmereki
    Enzymes accelerate reactions by lowering the activation energy needed to reach the transition state through the formation of an enzyme-substrate complex, in which the substrate binds to the active site of the enzyme via weak interactions. This facilitates the formation of the transition state and increases the reaction rate by increasing the concentration of the transition state, as enzymes precisely lower the free energy of activation. While enzymes alter only the reaction rate and not the equilibrium, they accelerate both the forward and reverse reactions to the same degree, reaching equilibrium faster than non-enzymatic reactions.

    Copyright:

    © All Rights Reserved
    Download as PPT, PDF, TXT or read online from Scribd
    Download as ppt, pdf, or txt
    of 11

    Enzymes alter only the reaction rate

    and not the reaction equilibrium


    Enzymes accelerate the forward and
    reverse reactions by precisely the same factor

    kF forward rate constant


    kR reverse rate constant

    Equilibrium concentration of B is 100 times more than A,


    whether an enzyme is present or not, but with an enzyme the equilibrium is reached faster
    Enzymes accelerate reactions by facilitating
    the formation of a transition state

    Enzymes lower the


    activation energy

    Enzymes accelerate
    reaching the
    equilibrium
    One approach to understanding how enzymes achieve this
    facilitation is to assume that the substrate in transition state (S‡)
    and the substrate (S) are in equilibrium.

    in which K‡ is the equilibrium constant for the formation of


    S‡, and v is the rate of formation of product from S‡.
    The rate of the reaction is proportional to the concentration of S‡:

    because only S‡ can be converted into product. The


    concentration of S‡ is in turn related to the free energy
    difference between S‡ and S, because these two chemical
    species are assumed to be in equilibrium; the greater the
    difference between these two states, the smaller the amount of
    S‡.
    Because the reaction rate is proportional to the
    concentration of S‡, and the concentration of S‡ depends
    on ΔG‡, the rate of reaction V depends on ΔG‡.
    Specifically,

    In this equation, k is Boltzmann's constant, and h is Planck's


    constant. The value of kT/h at 25°C is 6.2 × 1012 s-1.
    Suppose that the free energy of activation is 6.82 kcal mol-1
    (28.53 kJ mol-1). The ratio [S‡]/[S] (=K’eq) is then 10-5 (see Table
    8.4). If we assume for simplicity's sake that [S] = 1 M, then the
    reaction rate V is 6.2 × 107 s-1.
    If ΔG‡ were lowered by 1.36 kcal mol-1 (5.69 kJ mol-1), the
    ratio [S‡]/[S] is then 10-4, and the reaction rate would be 6.2 × 108
    s-1. As Table 8.4 shows, a decrease of 1.36 kcal mol-1 in ΔG‡
    yields a tenfold larger V. A relatively small decrease in ΔG‡ (20%
    in this particular reaction) results in a much greater increase in V.
    Table 8.4. Relation between ΔG°′ and K′eq (at 25°C)

    ΔG°′
    K′eq kcal mol-1 kJ/mol-1

    10-5 6.82 28.53


    10-4 5.46 22.84
    10-3 4.09 17.11
    10-2 2.73 11.42
    10-1 1.36 5.69
    1 0 0
    10 -1.36 -5.69
    102 -2.73 -11.42
    103 -4.09 -17.11
    104 -5.46 -22.84
    105 -6.82 -28.53
    The formation of an enzyme-substrate
    complex is the first step in enzymatic
    catalysis
    Spectroscopic characteristics of many enzymes
    and substrates change on formation of an ES
    complex
    Tryptophan synthase – Pyridoxal phosphate as co-factor
    (Tryptophan from
    serine and an indole derivative)
    The active sites of enzymes have
    some common features
    Active site: region in enzyme that binds
    substrates and cofactors if any

    Catalytic groups: residues that participate


    in bond-formation

    Interaction of enzyme and substrate at the


    active site promotes the formation of the
    transition state,

    The active site is the region of the enzyme


    where the free energy is lowered.
    The active site is a 3-dimesional cleft
    formed by groups that come from different
    parts of the aa - sequence

    Lysozyme
    Degrades the cell wall
    of bacteria
    • The active site takes up a relatively small
    part of the total volume of an enzyme

    Myoglobin

    • Active sites are located in clefts/crevices


    Substrates are bound to enzymes by
    multiple weak attractions
    H-bonds
    Electrostatic interactions
    Van der Waals forces
    Hydrophobic interactions

    ES-complexes:
    Equilibrium constants
    10-2 – 10-8
    Free energies of interaction
    -3 to -12 kcal/mol

    Covalent bonds:
    Energies -50 to -110 kcal/mol
    Ribonuclease: part of active site

    You might also like