Scribd Logo
Upload

Welcome to Scribd!

  • Additional Slides For L06

    Uploaded by

    bebble bopple
    3 views10 pages
    Here are the key steps: 1) In the absence of inhibitor, the lines intersect on the y-axis. This indicates Michaelis-Menten kinetics. 2) In the presence of inhibitor, the lines do not intersect on the y-axis but rather have parallel slopes. 3) Parallel lines indicate that the inhibitor does not affect Vmax but rather increases Km. Therefore, the nature of inhibition is competitive inhibition since the inhibitor competes with substrate for the active site but does not prevent substrate from binding once the inhibitor dissociates. In summary, the parallel slopes in the Lineweaver-Burk plot indicate that the inhibitor increases Km but not Vmax, consistent with

    Original Description:

    Slides for lecture 6

    Original Title

    Additional slides for L06

    Copyright

    © © All Rights Reserved

    Available Formats

    PDF, TXT or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    Report this Document
    Here are the key steps: 1) In the absence of inhibitor, the lines intersect on the y-axis. This indicates Michaelis-Menten kinetics. 2) In the presence of inhibitor, the lines do not intersect on the y-axis but rather have parallel slopes. 3) Parallel lines indicate that the inhibitor does not affect Vmax but rather increases Km. Therefore, the nature of inhibition is competitive inhibition since the inhibitor competes with substrate for the active site but does not prevent substrate from binding once the inhibitor dissociates. In summary, the parallel slopes in the Lineweaver-Burk plot indicate that the inhibitor increases Km but not Vmax, consistent with

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Flag for inappropriate content
    Download as pdf or txt
    3 views10 pages

    Additional Slides For L06

    Uploaded by

    bebble bopple
    Here are the key steps: 1) In the absence of inhibitor, the lines intersect on the y-axis. This indicates Michaelis-Menten kinetics. 2) In the presence of inhibitor, the lines do not intersect on the y-axis but rather have parallel slopes. 3) Parallel lines indicate that the inhibitor does not affect Vmax but rather increases Km. Therefore, the nature of inhibition is competitive inhibition since the inhibitor competes with substrate for the active site but does not prevent substrate from binding once the inhibitor dissociates. In summary, the parallel slopes in the Lineweaver-Burk plot indicate that the inhibitor increases Km but not Vmax, consistent with

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Flag for inappropriate content
    Download as pdf or txt
    of 10

    Additional slides for L06

    How to Determine Velocity-Substrate curve by experiments?

    S P enzyme timer
    d [P] d [S]
    v = ─── or v = - ─── substrate
    dt dt
    spectrophotometer
    buffer
    The Km for an enzyme at the absence and presence
    of 3 M of competitive inhibitor is 8 M and 12 M,
    respectively. Calculate Ki.
    ⚫ The Km for an enzyme at the absence and
    presence of 3 M of competitive inhibitor is 8 M
    and 12 M, respectively. Calculate Ki.

    Vmax [S]
    12 M v0 =
    a= = 1.5 αKM + [S]
    8 M

    a =1+
    I 1.5 = 1 +
    3 uM
    Ki =6 M
    Ki Ki
    Following the purification of a recombinant enzyme E, a research
    assistant carried out an enzymatic kinetic study in the absence or
    presence of inhibitor X. The Lineweaver-Burk plot is shown below.

    Based on the data provided in the plot,


    What is the nature of the inhibition? How
    you arrive your answer?

    You might also like