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    Su 3 Le 3-1

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    Francisca Manyisa
    The document discusses the kinetics of single substrate enzyme catalyzed reactions based on the Michaelis-Menten model. It covers assumptions of the model, derivations of the Michaelis-Menten equation, meanings of related terms, and deviations from the model's assumptions. Graphs for analyzing reaction kinetics are also mentioned.

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    Su 3 Le 3-1

    Uploaded by

    Francisca Manyisa
    9 views14 pages
    The document discusses the kinetics of single substrate enzyme catalyzed reactions based on the Michaelis-Menten model. It covers assumptions of the model, derivations of the Michaelis-Menten equation, meanings of related terms, and deviations from the model's assumptions. Graphs for analyzing reaction kinetics are also mentioned.

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    SU 3 LE 3-1 (2)

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    The document discusses the kinetics of single substrate enzyme catalyzed reactions based on the Michaelis-Menten model. It covers assumptions of the model, derivations of the Michaelis-Menten equation, meanings of related terms, and deviations from the model's assumptions. Graphs for analyzing reaction kinetics are also mentioned.

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    © All Rights Reserved
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    9 views14 pages

    Su 3 Le 3-1

    Uploaded by

    Francisca Manyisa
    The document discusses the kinetics of single substrate enzyme catalyzed reactions based on the Michaelis-Menten model. It covers assumptions of the model, derivations of the Michaelis-Menten equation, meanings of related terms, and deviations from the model's assumptions. Graphs for analyzing reaction kinetics are also mentioned.

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    SU 3

    Kinetics of single substrate enzyme


    catalysed reactions
    Michaelis- Menten
    Henri (1903) and Michaelis and Menten (1913) made the
    following assumptions for single substrate reactions with
    single binding site enzymes:
    • At to [P] can be ignored as well as k-2
    • Immediate equilibrium between E, S en ES – product
    production not a factor
    • [E] = [Eo] - [ES]
    • vo = k2[ES]
    • At ↑[S] is [Eo] = [ES], then vo = Vmax or Vmax = k2[Eo]
    • [So] >>> [Eo], thus at to [S] = [So]

    Which is to say: vo = (Vmax[So])/([So] + Ks)


    Know derivision!! (p106-107)
    Video link:
    https://www.youtube.com/watch?v=8PWF5OeB7Ec
    Briggs-Haldane modification
    • [ES] <<< [S], [ES] <<< [Eo]
    • [ES] stays constant, while [S] and [P] changes (steady-
    state)
    • Thus formation rate of ES = breakdown rate of ES
    • Km = (k-1 +k2)/k1 = ([E][S])/[ES]
    • Rest of assumption as M-M

    – vo = (Vmax[So])/([So] + Km) = M-M equation

    Know derivision!! (p108-109)


    Video link:
    https://www.youtube.com/watch?v=YSOJNKQeCtQ
    Meaning of M-M equation
    • For which reactions does it count? NB!
    – Single substrate, one S-binding site per enzyme
    – Single ES (I)
    – ES → EP rate limiting step
    • Kcat = turnover number
    • Vmax = maximum reaction rate at set
    conditions
    • Km vs Ks … what’s the difference and
    meaning?
    • Kcat/Km = Catalytic efficiency
    • See example of phosphofructokinase and
    triosephosphate isomerase NB!!
    Lineweaver-Burk plot
    Video link: https://www.youtube.com/watch?v=4aVOtcpGaZc
    Eadie-Hofstee graph (L-B x
    Hanes graph (L-B x [So])
    vo.Vmax)
    https://www.youtube.com/watch?v=n_
    https://www.youtube.com/watch?v= 3AkzEzLEY
    _qSJFBoxdwQ
    Deviations from stationary state
    kinetic assumptions
    • Assumption Critisism
    • At to, [P] and k2 is negligible ↓ Haldane relationship discusses this
    deviation
    • Immediate equilibrium between B-H says [ES] stationary while [S] [E],
    [S], [ES] and [P] change
    • [Eo] = [E] + [ES] and Enzyme unstable in vitro, thus
    • MM- eq true if [Eo] is constant [Eo] = [E] + [ES] + [Ed]
    • Vo = k2[ES] and [P] and –k2 negligible [P] en –k2 not always negligible
    • ES → E + P rate limiting step ES → E + P can be more complex
    thus k2 not constant for rate limiting step
    • At ↑[S] is [Eo] = [ES] and Vo = Vmax or This step can be blocked and is then
    Vmax = k2[ES] incompatable with the law of mass
    action

    6. At to is [S] = [So] or [So] >>>>[Eo] Not “assumption”, but “approximate”


    Theoretical progress curve
    Relaxation kinetics
    [Δ A] = [Δ A]₀ e –t/τ
    1/τ = k1([E ] + [S ]) + k-1
    eq eq
    • Kcat = Vmax/[Eo]

    • Vmax = 12 µmol/min of 12 x 10-6 mol/min

    • [E] = 10 ng met Mw = 60 000 g/mol


    • = 10 x 10-9g/60 000g/mol
    • = 1.667 x 10-13 mol

    • thus

    • Kcat = 12 x 10-6 mol/min/1.667 x 10-13 mol


    • = 72 000 000 min-1 of 7.2 x 107 min-1
    Introduction to enzyme kinetics:
    https://www.youtube.com/watch?v=kmyR1
    cYxRL4

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