Enzyme Nomenclature Quiz
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Questions and Answers

What is the term for structurally similar compounds that have the same functional groups?

  • Group similarity
  • Functional equivalence
  • Group specificity (correct)
  • Functional uniformity
  • What does linkage specificity refer to in enzyme activity?

  • Breaking down all types of bonds
  • Recognition of specific bonds for catalysis (correct)
  • Bonding with any nearby molecule
  • Cleavage of amino acids from any end of the peptide chain
  • Why does higher temperature lead to increased enzyme activity?

  • Higher kinetic energy and more reactant collisions (correct)
  • Decreased substrate concentration
  • Increased denaturation rate
  • Enhanced protein stability
  • What is the optimum temperature for human enzymes according to the text?

    <p>37ºC</p> Signup and view all the answers

    How do drastic changes in pH affect enzyme activity?

    <p>Lead to denaturation of proteins</p> Signup and view all the answers

    At a constant enzyme concentration, what happens to enzyme activity with increased substrate concentration?

    <p>Activity increases</p> Signup and view all the answers

    What is the enzyme specificity where an enzyme can catalyze a particular reaction for only one substrate?

    <p>Absolute specificity</p> Signup and view all the answers

    In which model for substance binding to enzymes does the enzyme have a predetermined shape for the active site?

    <p>Lock-and-key model</p> Signup and view all the answers

    Which type of interactions play a role in determining substrate binding to enzymes?

    <p>Hydrophobic interactions, London dispersion forces, hydrogen bonding, van der Waals forces</p> Signup and view all the answers

    What is the intermediate reaction species formed when the substrate binds with the active site of an enzyme?

    <p>Enzyme-substrate complex</p> Signup and view all the answers

    Which factor can affect enzyme activity by allowing a small change in space to accommodate a substrate?

    <p>Temperature</p> Signup and view all the answers

    Which enzyme has stereochemical specificity in distinguishing between L-amino acids and D-amino acids?

    <p>L-Amino-acid oxidase</p> Signup and view all the answers

    What type of reaction does an oxidoreductase enzyme catalyze?

    <p>Oxidation-reduction</p> Signup and view all the answers

    Which suffix is commonly found in the names of some digestive enzymes?

    <p>-in</p> Signup and view all the answers

    What is the role of a hydrolase enzyme?

    <p>Catalyzes hydrolysis reactions</p> Signup and view all the answers

    Which coenzyme is required for an oxidoreductase enzyme?

    <p>NAD+ or NADP+</p> Signup and view all the answers

    What is the primary function of enzymes with the suffix -ase?

    <p>Catalyze hydrolysis reactions</p> Signup and view all the answers

    How are oxidation and reduction reactions related in the context of oxidoreductase enzymes?

    <p>They are linked processes</p> Signup and view all the answers

    What is the major function of B Vitamins?

    <p>Aid in the formation of proteins involved in regulating blood clotting</p> Signup and view all the answers

    Which vitamin is synthesized by bacteria in the colon?

    <p>Vitamin K2</p> Signup and view all the answers

    What is the role of vitamin A in vision?

    <p>Combines with opsin protein to form rhodopsin</p> Signup and view all the answers

    Which vitamin has a hydrocarbon-like structure with fewer functional groups?

    <p>Vitamin A</p> Signup and view all the answers

    What is the source of approximately half of the dietary need for Vitamin K?

    <p>Synthesized by bacteria in the colon</p> Signup and view all the answers

    Which Vitamin is also known as pyridoxine, pyridoxal, and pyridoxamine?

    <p>Vitamin B6</p> Signup and view all the answers

    What is the process in which enzyme activity is altered by covalently modifying the enzyme structure?

    <p>Covalent modification</p> Signup and view all the answers

    Which family of antibiotics inhibits specific enzymes essential to life processes of bacteria?

    <p>Penicillin family</p> Signup and view all the answers

    What is the most common covalent modification involving the addition and removal of a group from an enzyme?

    <p>Phosphorylation</p> Signup and view all the answers

    Which type of enzymes catalyze the removal of phosphate group in covalent modification?

    <p>Phosphatases</p> Signup and view all the answers

    What happens if premature production of pepsin occurs in the stomach?

    <p>Destruction of stomach lining</p> Signup and view all the answers

    Zymogens are also known as:

    <p>Proenzymes</p> Signup and view all the answers

    Study Notes

    Structural Similarity

    • Analogs are structurally similar compounds that have the same functional groups

    Specificity of Enzymes

    • Linkage specificity refers to the enzyme's ability to catalyze a reaction at a specific bond or linkage in a substrate molecule.

    Temperature and Enzyme Activity

    • Higher temperatures increase enzyme activity by increasing molecular motion and collisions between enzymes and substrates, leading to faster reaction rates.
    • The optimum temperature for human enzymes is 37 °C (98.6 °F)

    pH and Enzyme Activity

    • Drastic changes in pH can affect enzyme activity by altering their three-dimensional structure (conformation), damaging their active sites, and reducing their efficiency.

    Substrate Concentration and Enzyme Activity

    • At a constant enzyme concentration, increasing substrate concentration increases enzyme activity until a saturation point is reached, where all active sites are occupied by substrate.

    Types of Enzyme Specificity

    • Absolute specificity refers to when an enzyme can catalyze a particular reaction for only one substrate.

    Models for Enzyme-Substrate Binding

    • The lock-and-key model proposes that an enzyme has a predetermined shape for the active site that perfectly complements the substrate.
    • Induced fit model states that the active site is flexible and adjusts its shape in response to substrate binding.

    Forces Involved in Substrate Binding

    • Noncovalent interactions, including hydrogen bonds, ionic interactions, van der Waals forces, and hydrophobic interactions, play a role in determining substrate binding to enzymes.

    Enzyme-Substrate Intermediate

    • The formation of an enzyme-substrate complex (ES complex) represents an intermediate reaction species formed when a substrate binds with the enzyme's active site.

    Inductive Fit and Active Site Flexibility

    • Inductive fit allows a slight change in the active site's shape to accommodate a substrate.

    Stereochemical Specificity

    • Stereochemical specificity occurs in enzymes that can distinguish between L-amino acids and D-amino acids, for example, L-amino acid oxidase catalyzes the oxidation of L-amino acids but not D-amino acids.

    Oxidoreductase Enzymes

    • Oxidoreductases catalyze oxidation-reduction reactions, which involve the transfer of electrons between molecules, with one molecule being oxidized and the other reduced.

    Naming Digestive Enzymes

    • The suffix "-ase" is commonly found in the names of some digestive enzymes, e.g., peptidase, lipase, and amylase.

    Hydrolase Enzyme Function

    • Hydrolases catalyze the hydrolysis reaction, cleaving chemical bonds by adding a water molecule.

    Coenzymes in Oxidoreductases

    • Nicotinamide adenine dinucleotide (NAD+) is a common coenzyme required for oxidoreductase enzymes.

    Function of "-ase" Suffix

    • Enzymes with the suffix "-ase" primarily function as biological catalysts, speeding up chemical reactions in living organisms without changing the equilibrium of the reaction.

    Oxidation and Reduction in Oxidoreductases

    • Oxidation and reduction reactions are coupled processes in oxidoreductases, where one molecule loses electrons (oxidation) while another gains electrons (reduction).

    Vitamins: Structure and Function

    • B Vitamins function as coenzymes in various metabolic reactions.
    • Vitamin K is synthesized by bacteria in the colon and is also obtained from dietary sources (approximately 50%).
    • Vitamin A plays a crucial role in vision by converting retinal to rhodopsin, a light-sensitive pigment.
    • Vitamin E has a hydrocarbon-like structure with fewer functional groups and acts as an antioxidant.

    Covalent Modification of Enzymes

    • Covalent modification is a process in which enzyme activity is altered by covalently modifying the enzyme's structure.

    Antibiotics and Enzyme Inhibition

    • Penicillin belongs to a family of antibiotics that inhibit specific enzymes essential to the life processes of bacteria.

    Phosphorylation

    • Phosphorylation, the addition and removal of a phosphate group, is the most common covalent modification of enzymes.
    • Phosphatases are enzymes that catalyze the removal of a phosphate group in covalent modification.

    Premature Pepsin Production

    • Premature production of pepsin in the stomach can lead to gastric ulcers, as it starts to digest the stomach lining.

    Zymogens

    • Zymogens are inactive precursors of enzymes, also known as proenzymes.

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    Description

    Test your knowledge of enzyme nomenclature with this quiz! Learn about the naming conventions for enzymes based on suffixes and prefixes indicating their function and the type of reactions they catalyze.

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