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  • Answer: Enzyme Kinetics (Michaelis Menten/Lineweaver Burke/Eadie-Hostee)

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    Ryan Borazon Garcia
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    The document discusses enzyme kinetics concepts including: - The Michaelis Menten equation which describes the rate of reaction at saturation. It defines Vmax as the maximum rate and Km as the substrate concentration that yields half Vmax. - Competitive inhibitors bind the active site, increasing apparent Km in Lineweaver Burke plots and having the same intercept on the x-axis. Noncompetitive inhibitors affect Vmax and have the same intercept on both axes. - Suicide inhibitors irreversibly inactivate the enzyme through its catalytic machinery.

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    Enzyme Kinetics

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    The document discusses enzyme kinetics concepts including: - The Michaelis Menten equation which describes the rate of reaction at saturation. It defines Vmax as the maximum rate and Km as the substrate concentration that yields half Vmax. - Competitive inhibitors bind the active site, increasing apparent Km in Lineweaver Burke plots and having the same intercept on the x-axis. Noncompetitive inhibitors affect Vmax and have the same intercept on both axes. - Suicide inhibitors irreversibly inactivate the enzyme through its catalytic machinery.

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    9 views2 pages

    Answer: Enzyme Kinetics (Michaelis Menten/Lineweaver Burke/Eadie-Hostee)

    Uploaded by

    Ryan Borazon Garcia
    The document discusses enzyme kinetics concepts including: - The Michaelis Menten equation which describes the rate of reaction at saturation. It defines Vmax as the maximum rate and Km as the substrate concentration that yields half Vmax. - Competitive inhibitors bind the active site, increasing apparent Km in Lineweaver Burke plots and having the same intercept on the x-axis. Noncompetitive inhibitors affect Vmax and have the same intercept on both axes. - Suicide inhibitors irreversibly inactivate the enzyme through its catalytic machinery.

    Copyright:

    Attribution Non-Commercial (BY-NC)
    Download as DOCX, PDF, TXT or read online from Scribd
    Flag for inappropriate content
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    Enzyme Kinetics (Michaelis Menten/Lineweaver Burke/Eadie-Hostee)

    Question What is the Michaelis Menten equation? Define Vmax. The rate of the reaction at saturation substrate concentrations for a given amount of enzyme defines what concept? Define Km. The substrate concentration that results in 50% Vmax defines what? An inhibitor that binds to the active site and competes with the substrate for its occupation is called a _________ inhibitor. An inhibitor that binds to, and takes an enzyme out of commission is called a ____________ inhibitor. Competitive inhibitors ____________ (increase / decrease) the apparent Km. In a Lineweaver Burke plot, a competitive inhibitor will have _______________ (same / different) point on the x axis. In a Lineweaver Burke plot, a noncompetitive inhibitor will have _______________ (same / different) point on the x axis. In a Lineweaver Burke plot, a competitive inhibitor will have _______________ (same / different) point on the y axis. In a Lineweaver Burke plot, a noncompetitive inhibitor will have _______________ (same / different) point on the y axis.

    Answer v=Vmax [S] / [S] + Km The rate of the reaction at saturation substrate concentrations for a given amount of enzyme. Vmax The substrate concentration that results in 50% Vmax. Km Competitive inhibitor

    Noncompetitive inhibitor Increase Different

    Same

    Same

    Different

    This type of inhibitor binds to the active site and is acted upon by the enzyme just as if it was a normal substrate. The enzyme uses its own catalytic machinery to inactivate itself. Fluorouracil is what type of inhibitor? The Y axis on the Lineweaver Burke plot indicates ___________. The X axis on the Lineweaver Burke plot indicates ____________. The Y axis on the Eadie-Hofstee plot indicates _________. The X axis on the Eadie-Hofstee plot indicates _________. The slope of the Eadie-Hofstee plot indicates __________. True or False: Both competitive and noncompetitive inhibition is reversible. True or False: Both competitive and noncompetitive inhibition is irreversible.

    Suicide inhibitor Suicide inhibitor 1/Vmax -1/Km Vmax Vmax/Km -Km True False

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