Bio1332 Biochemistry - Lecture Fourteen - Allosteric Enzymes

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Bio1332 Biochemistry - Lecture Fourteen - Allosteric Enzymes - Quiz

Appreciate that enzyme rates can be altered by various mechanisms. Understand the concept of allostery, and how it might occur in a protein. Discriminate between the different types of inhibitors and their properties. Knowhowquaternarystructurechangesthe properties of an enzyme.


Questions and Answers
  • 1. 

    Please complete the following sentence:___________ is where a chemical binds to an enzyme away from the active site, influencing the kinetic properties of the enzyme.

    Explanation
    Allostery is a phenomenon where a chemical molecule binds to an enzyme at a site other than the active site, leading to changes in the enzyme's kinetic properties. This binding can either enhance or inhibit the enzyme's activity, ultimately affecting its function. Allostery is an important mechanism for regulating enzyme activity and is crucial for various biological processes.

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  • 2. 

    What is the average size of an enzyme?

    • A.

      300 amino acids

    • B.

      30 amino acids

    • C.

      200 amino acids

    • D.

      20 amino acids

    Correct Answer
    A. 300 amino acids
    Explanation
    The average size of an enzyme is typically around 300 amino acids. Enzymes are proteins that catalyze chemical reactions in living organisms, and they are composed of long chains of amino acids. While the size of enzymes can vary, 300 amino acids is a common average length for these biological catalysts.

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  • 3. 

    Please complete the following sentences (separate your answers with commas):An ________________ is any molecule that can bind to an enzyme away from the active site, and by doing so change the enzyme's activity for its substrate. These effectors can either increase the rate of reaction (named __________________), or reduce the rate of reaction (named _______________).

    Correct Answer
    Allosteric effector, allosteric activators, allosteric inhibitors
    Allosteric effector, allosteric activator, allosteric inhibitor
    Explanation
    An allosteric effector is any molecule that can bind to an enzyme away from the active site, and by doing so change the enzyme's activity for its substrate. These effectors can either increase the rate of reaction (named allosteric activators), or reduce the rate of reaction (named allosteric inhibitors).

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  • 4. 

    Please complete the following sentence:An __________ is any molecule that acts to reduce the rate of an enzymatic reaction.

    Correct Answer
    Inhibitor
    Explanation
    An inhibitor is any molecule that acts to reduce the rate of an enzymatic reaction. Inhibitors can bind to the enzyme and prevent it from interacting with its substrate, thereby inhibiting the formation of the enzyme-substrate complex. This can occur through various mechanisms, such as blocking the active site of the enzyme or changing its conformation. Inhibitors are important in regulating enzyme activity and can be used as therapeutic agents to target specific enzymes involved in diseases.

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  • 5. 

    Please fill answer below: 
    • Many enzymes are made from more than one protein chain (quaternary structure).
    • The chains can be identical or different.
    • In some cases, the binding of substrate to one subunit (chain) influences the binding to other subunits.
    • This results in ___________ between the subunits. 

    Correct Answer
    co-operativity
    cooperativity
    co operativity
    Explanation
    Many enzymes are made from more than one protein chain, known as quaternary structure. These chains can be identical or different. In some cases, when a substrate binds to one subunit (chain), it can influence the binding to other subunits. This phenomenon is referred to as cooperativity, or co-operativity, or co operativity. It describes the interaction and communication between the subunits of an enzyme, leading to a coordinated and efficient enzymatic activity.

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