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    The document describes an experiment investigating the activity of two forms of the enzyme glucose-6-phosphate dehydrogenase (G6PD), called forms J and K. Form K contains a single amino acid mutation compared to form J. The results show that form K has a higher maximum reaction rate (Vmax) but also a higher Michaelis constant (Km) than form J. This indicates that the mutation increases the enzyme's activity but also lowers its affinity for the substrate. Both forms of G6PD can exist as dimers of two identical polypeptide chains or tetramers of four identical chains due to the symmetrical structure of proteins.

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    The document describes an experiment investigating the activity of two forms of the enzyme glucose-6-phosphate dehydrogenase (G6PD), called forms J and K. Form K contains a single amino acid mutation compared to form J. The results show that form K has a higher maximum reaction rate (Vmax) but also a higher Michaelis constant (Km) than form J. This indicates that the mutation increases the enzyme's activity but also lowers its affinity for the substrate. Both forms of G6PD can exist as dimers of two identical polypeptide chains or tetramers of four identical chains due to the symmetrical structure of proteins.

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    © All Rights Reserved
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    3 views2 pages

    Graph 1

    Uploaded by

    luna.art2007
    The document describes an experiment investigating the activity of two forms of the enzyme glucose-6-phosphate dehydrogenase (G6PD), called forms J and K. Form K contains a single amino acid mutation compared to form J. The results show that form K has a higher maximum reaction rate (Vmax) but also a higher Michaelis constant (Km) than form J. This indicates that the mutation increases the enzyme's activity but also lowers its affinity for the substrate. Both forms of G6PD can exist as dimers of two identical polypeptide chains or tetramers of four identical chains due to the symmetrical structure of proteins.

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    © All Rights Reserved
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    of 2

    6

    3 The enzyme glucose 6-phosphate dehydrogenase (G6PD) is composed of two identical polypeptide
    chains.

    (a) Students investigated the activity of two forms of G6PD, J and K, at different concentrations
    of substrate. K is a form of the enzyme that results from a mutation that changes one amino
    acid in the polypeptide.

    The results are shown in Fig. 3.1.

    70

    J
    60

    K
    50
    rate of reaction
    / μmol min–1

    40

    30

    20

    10

    0
    0.0 0.2 0.4 0.6 0.8 1.0 1.2 1.4 1.6 1.8 2.0
    concentration of substrate / mmol dm–3

    Fig. 3.1

    © UCLES 2020 9700/21/M/J/20


    7

    (i) Use Fig. 3.1 to complete Table 3.1 by stating:

    • the Vmax and the Km for enzymes J and K

    • the units for Vmax and Km.

    Table 3.1

    Vmax / Km /

    [3]

    (ii) With reference to Fig. 3.1 and Table 3.1, describe the effect of the mutation on the activity of
    G6PD and suggest an explanation for this effect.

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    ...........................................................................................................................................

    ...........................................................................................................................................

    ..................................................................................................................................... [4]

    (b) In certain conditions, G6PD may also exist as four identical polypeptide chains rather than
    two identical polypeptide chains.

    Explain why both of these types of G6PD have all four levels of protein structure.

    ...................................................................................................................................................

    ...................................................................................................................................................

    ...................................................................................................................................................

    ...................................................................................................................................................

    ............................................................................................................................................. [2]
    [Total: 9]
    © UCLES 2020 9700/21/M/J/20 [Turn over

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