Enzymes: Biological Catalysts Overview
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Questions and Answers

Which of the following best describes the initial step in enzyme catalysis?

  • Transition of the substrate to the product
  • Binding of the substrate to the enzyme (correct)
  • Dissociation of the enzyme from the product
  • Formation of the product complex
  • What role do coenzymes typically play in enzyme function?

  • They assist in transferring functional groups (correct)
  • They act as substrates in all enzyme-catalyzed reactions
  • They provide energy by hydrolyzing ATP
  • They increase the enzyme concentration
  • Which class of enzymes is primarily responsible for catalyzing the addition or removal of hydrogen atoms?

  • Isomerases
  • Lyases
  • Hydrolases
  • Oxidoreductases (correct)
  • In the classification of enzymes, what does the four-digit number assigned to each enzyme signify?

    <p>Enzyme class, subclass, substrate, and reaction type</p> Signup and view all the answers

    Which of the following is NOT one of the six functional classes of enzymes according to the International Union of Biochemists?

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

    The formation of the enzyme-substrate complex (ES) leads to which transitional state during enzyme catalysis?

    <p>ES*</p> Signup and view all the answers

    What defines the trivial name of an enzyme as commonly used in everyday language?

    <p>The combination of substrate, product, and enzyme's functional class</p> Signup and view all the answers

    Which of the following best describes lyases as a class of enzymes?

    <p>They break bonds by adding or removing groups without hydrolysis</p> Signup and view all the answers

    Which step follows the formation of the enzyme-substrate complex in the enzyme catalysis process?

    <p>Transition state formation</p> Signup and view all the answers

    How are enzymes that catalyze isomerizations uniquely categorized?

    <p>As isomerases</p> Signup and view all the answers

    What term is used for enzymes that are wholly composed of protein?

    <p>Simple enzymes</p> Signup and view all the answers

    Which component of a holoenzyme is specifically the protein part?

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

    What type of enzyme requires a metal ion as part of its composition?

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

    Which of the following statements about coenzymes is true?

    <p>They are non-covalently bound to apoenzymes.</p> Signup and view all the answers

    What defines the specificity of enzymes towards substrates?

    <p>The unique chemical structure of each substrate.</p> Signup and view all the answers

    In what way do isozymes differ from one another?

    <p>They vary slightly in their genetic expression.</p> Signup and view all the answers

    Which of the following statements is true regarding the cytochrome coenzymes?

    <p>They may carry hydrogen or hydride ions among other groups.</p> Signup and view all the answers

    Which enzyme is best known for having multiple isozymes?

    <p>Lactate dehydrogenase</p> Signup and view all the answers

    What is the role of phosphate groups in coenzymes like pyridoxal phosphate?

    <p>They carry amino groups (-NH2).</p> Signup and view all the answers

    Which of the following best describes racemases?

    <p>Enzymes that convert D isomers to L isomers and vice versa.</p> Signup and view all the answers

    Study Notes

    Enzymes 1

    • Enzymes are biological catalysts
    • Almost all life processes rely on enzyme activity
    • Almost all enzymes are proteins, except for ribozymes (RNA modifying catalysts)
    • In enzyme-catalyzed reactions, substrate concentrations are typically higher than enzyme concentrations
    • Enzyme catalysis involves substrate binding to a specific site on the enzyme (active or catalytic site)
    • During enzyme catalysis, the ES complex forms, transitions to ES*, and then to the EP complex before dissociating into product and free enzyme.
    • Enzyme reactions follow this series: E + S <=> ES <=> ES* <=> EP <=> E + P
    • Initially, enzymes were named arbitrarily by their discoverers
    • As knowledge expanded, enzyme classification systems became more complex
    • Currently, enzymes are grouped into 6 classes by the International Union of Biochemists (IUB)
    • The IUB assigns a unique number to each enzyme and a textual name
    • Enzyme classification is based on the type of chemical reaction catalyzed

    IUB Enzyme Classifications

    • Oxidoreductases: Add or remove hydrogen atoms
    • Transferases: Transfer functional groups
    • Hydrolases: Add water across a bond, hydrolyzing it
    • Lyases: Add or remove water, ammonia, or carbon dioxide across double bonds
    • Isomerases: Catalyze isomerizations
    • Ligases: Join two chemical groups using energy from ATP

    Enzyme Nomenclature

    • Each enzyme is given a four-digit number specifying its class, subclass, substrate, and reaction type
    • Enzyme names combine the substrate name, product name, and functional class
    • In everyday use, enzymes are often called by their common (trivial) names.

    Enzyme Composition

    • Enzymes are also classified by their composition
    • Simple enzymes are composed entirely of protein
    • Complex enzymes are composed of protein plus a small organic molecule (cofactor)
    • Complex enzymes are also known as holoenzymes

    Coenzymes

    • Coenzymes act as transporters of chemical groups between reactants.
    • Chemical groups carried by coenzymes can vary in complexity
      • e.g., hydride ion (H+ + 2e-), a molecule of hydrogen, or an amine group (-NH2)
    • Coenzymes are chemically changed during enzyme action, thus they can be considered "second substrates"
    • Coenzymes are recycled to their original form after donating a chemical group to an acceptor molecule.

    Enzyme Specificity

    • Enzymes are highly specific for the type of reaction they catalyze
    • Enzymes are substrate specific
    • Some enzymes exhibit broad substrate specificity (e.g., alcohol dehydrogenase and hexokinase).
    • Enzymes are generally specific for a particular steric configuration (D or L optical isomers) of a substrate
    • Racemases are an exception; they convert D isomers to L isomers and vice-versa.

    Isozymes

    • Isozymes are multiple forms of an enzyme that work on the same substrate and produce the same product.
    • Isozymes result from slight variations in the genes.
    • Various isozymes are expressed in different tissues of the body -Example: Lactic dehydrogenase (LDH) is a tetrameric enzyme composed of two types of protein subunits (H and M) in different arrangements
    • Different subunit arrangements produce different isozymes, each with a specific tissue distribution -Example: HHHH (Heart-type), HHHM, HHMM, HMMM, MMMM (Muscle-type) - LDH isozymes are widely used clinically as markers of tissue damage.

    Enzyme-Substrate Interactions

    • Two models explain enzyme-substrate binding:
      • Key and lock model
      • Induced fit model
    • The induced fit model proposes that the initial enzyme-substrate interaction is weak and possibly not completely complementary but it induces conformational changes in the enzyme

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    Description

    This quiz covers the essential concepts of enzymes as biological catalysts crucial for various life processes. You'll learn about enzyme classification, mechanisms of action, and the formation of enzyme-substrate complexes. Test your knowledge on how enzymes function and their importance in biochemical reactions.

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