Biochemistry Chapter 5.pdf

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    ___ catalyze group-transfer

    reactions.

    Transferases

    ___ catalyze hydrolysis. Hydrolases

    ___ catalyze ligation or

    joining of two substrates.

    Ligases

    ___ catalyze lysis of a

    substrate.

    Lyases

    ___ catalyze oxidation-

    reduction reactions.

    Oxidoreductases

    ___ catalyze structural change

    within a single molecule.

    Isomerases

    ___ is an allosteric inhibitor of PFK-1

    while ___ is an allosteric activator of

    PFK-1.

    PEP, ADP

    ___ is the affinity of the

    substrate for the enzyme.

    Km

    ___ is the slowest step and

    the turnover number.

    Kcat

    ___ is when there are no ways of intermediates and

    everything takes place because the enzyme acts as one

    complex without entering the bulk solvent.

    Metabolite channeling

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    A ___ is a coenzyme or metal ion that is

    tightly or covalently bound to the enzyme.prosthetic group

    A ___ is a complete active enzyme with

    its bound coenzyme and/or metal ions.holoenzyme

    A ___ is a compound that binds to an

    enzyme and interferes with its activity.inhibitor

    A ___ is the protein part of

    the holoenzyme.

    apoenzyme/apoprotein

    A high Kcat would be consistent

    with a ___ (fast, slow) reaction.fast

    African sleeping sickness is

    caused by ___.

    Trypanosomes

    Do allosteric enzymes exhibit

    typical Michaelis-Menten kinetics?No

    Do you want a high or low

    Km?

    Low

    For the unimolecular reaction S -->

    P, the rate equation is ___.V = k[S]

    If there is no spermine or spermidine

    then the cells cannot ___.divide

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    In competitive inhibition the

    Vmax ___ and Km ___.

    stays the same, increases

    In noncompetitive inhibition

    the Vmax ___ and Km ___.

    decreases, stays the same

    In the absence of a substrate

    the enzyme is in the ___ state.

    T

    In uncompetitive inhibition

    the Vmax ___ and Km ___.

    decreases, decreases

    Irreversible inhibition is bound ___

    while reversible inhibition is bound ___.covalently, noncovalently

    Is regulation by covalent modification

    faster or slower than allosteric

    regulation?

    slower

    Michaelis-Menten Kinetics is

    a ___ or ___ order reaction.

    zero, first

    More substrate would create a

    ___ (faster, slower) reaction.

    faster

    Sigmoidal has ___ (one,

    more than one) binding site.

    more than one

    Spermine and spermidine have ___

    (negative, positive) charges.positive

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    The ___ is the energy difference between

    the ground state and the transition state.energy of activation (Eact)

    The ___ is the starting point for either

    the forward or reverse reaction.ground state

    The formation of E + P is the

    ___ step.

    rate-limiting

    Trypanosomes are ___ (eukaryotes,

    prokaryotes) and ___ (multicellular,

    unicellular).

    eukaryotes, unicellular

    Vo vs. [S] curve is ___

    (hyperbolic, sigmoidal).

    sigmoidal

    When ES is kept at a constant

    rate, it is called the ___ state.

    steady

    When ES is still being formed,

    it is called the ___ state.

    pre-steady

    With an activator Km ___ and

    with an inhibitor Km ___.

    decreases, increases