Enzymes in Nutrition
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Questions and Answers

What is the role of the active site in enzymatic catalysis?

  • To inhibit the enzyme
  • To increase the energy barrier of the reaction
  • To denature the enzyme
  • To bind the substrate and facilitate the reaction (correct)
  • What is the term for a precursor of an enzyme that is inactive?

  • Holoenzyme
  • Proenzyme (correct)
  • Apoenzyme
  • Isoenzyme
  • What is the unit of measurement for enzymatic activity?

  • Molarity per minute
  • moles per liter per second
  • Molarity
  • International Unit (correct)
  • What is the term for a system of multiple enzymes working together?

    <p>Multienzyme system</p> Signup and view all the answers

    What is the factor that affects enzymatic activity by increasing the energy barrier of the reaction?

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

    What is Km in enzyme kinetics?

    <p>The substrate concentration at which the reaction rate is half of Vmax</p> Signup and view all the answers

    Which of the following enzymes has a high affinity for its substrate?

    <p>Alkaline phosphatase</p> Signup and view all the answers

    What is the name of the hypothesis proposed by Fischer to explain enzyme-substrate binding?

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

    What is the primary role of catalysts in biological systems?

    <p>To speed up chemical reactions</p> Signup and view all the answers

    What is the classification of enzymes based on?

    <p>The substrate they act on</p> Signup and view all the answers

    What is the purpose of enzymes in biological systems?

    <p>To catalyze chemical reactions</p> Signup and view all the answers

    What is the name of the organization that develops the classification system for enzymes?

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

    What is the reactant in the reaction Glucose-6-phosphate → Fructose-6-phosphate?

    <p>Glucose-6-phosphate</p> Signup and view all the answers

    What type of enzyme catalyzes the reaction Fructose-1,6-bisphosphate → Glyceraldehyde-3-phosphate + Dihydroxyacetone phosphate?

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

    What is the primary function of enzymes in metabolic pathways?

    <p>To catalyze specific chemical reactions</p> Signup and view all the answers

    What is the name of the process that involves the breakdown of glucose to produce energy?

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

    What is the product of the reaction glutámico + amoníaco?

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

    Which enzyme is involved in the reaction Sacarosa → Fructosa + Glucosa?

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

    What is the name of the product of the reaction Triacilglicerol →?

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

    Which of the following is a characteristic of Apoenzimas?

    <p>Naturaleza proteica</p> Signup and view all the answers

    What is the term used to describe enzymes that require a metal ion to be active?

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

    What is the product of the reaction Lactosa →?

    <p>Glucosa + Galactosa</p> Signup and view all the answers

    Which enzyme is involved in the reaction Pesinógeno →?

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

    What is the term used to describe the molecule that is converted to an active enzyme?

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

    What is the main characteristic of a suicidal inhibitor?

    <p>It permanently inactivates the enzyme</p> Signup and view all the answers

    What is the effect of a non-competitive inhibitor on the Km of an enzyme?

    <p>It has no effect on the Km</p> Signup and view all the answers

    What is the purpose of enzyme regulation?

    <p>To maintain homeostasis</p> Signup and view all the answers

    What is the characteristic of an enzyme cascade?

    <p>It is a series of enzyme reactions</p> Signup and view all the answers

    What is the definition of an isoenzyme?

    <p>A variant of an enzyme with different kinetic properties</p> Signup and view all the answers

    What is the effect of a competitive inhibitor on the enzyme-substrate binding?

    <p>It decreases the enzyme-substrate binding</p> Signup and view all the answers

    What is the purpose of using enzymes in the industry?

    <p>To reduce the cost and energy required for a reaction</p> Signup and view all the answers

    What is the effect of heat on enzyme activity?

    <p>It permanently inactivates the enzyme</p> Signup and view all the answers

    What is the diagnosis of Marcelo's symptoms?

    <p>Pancreatitis aguda</p> Signup and view all the answers

    What is the function of the pancreas in digestion?

    <p>Producing enzymes to digest food in the small intestine</p> Signup and view all the answers

    What is the effect of ethanol on pancreatic enzymes?

    <p>It denatures them</p> Signup and view all the answers

    What is the relationship between lithiasis biliar and pancreatitis?

    <p>Lithiasis biliar is a cause of pancreatitis</p> Signup and view all the answers

    What is the effect of pancreatitis on pancreatic exocrine secretion?

    <p>It decreases the secretion of digestive enzymes</p> Signup and view all the answers

    What type of enzymes are involved in pancreatic digestion?

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

    What is the consequence of pancreatitis on the pancreas itself?

    <p>It causes inflammation and tissue damage</p> Signup and view all the answers

    What is the dual function of the pancreas?

    <p>Producing hormones and digestive enzymes</p> Signup and view all the answers

    Study Notes

    Enzymes

    • Enzymes are biological molecules that accelerate chemical reactions in living organisms.
    • They are essential in biological systems as they increase reaction rates, allowing cells to maintain homeostasis and perform various functions.

    Classification of Enzymes

    • Enzymes can be classified into different groups based on their mode of action and the type of reaction they catalyze.
    • Examples of enzyme classes include oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.

    Metabolic Reactions

    • Glucose-6-phosphate is converted to fructose-6-phosphate in a reaction catalyzed by an aldose isomerase.
    • Fructose 1,6-bisphosphate is converted to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in a reaction catalyzed by an aldolase.
    • Acetylglutamic acid and ammonia are converted to glutamine in a reaction catalyzed by a glutamine synthetase.
    • Malate is converted to oxaloacetate in a reaction catalyzed by a malate dehydrogenase.

    Pre-metabolic Reactions

    • Sucrose is broken down into glucose and fructose in a reaction catalyzed by a sucrase.
    • Lactose is broken down into galactose and glucose in a reaction catalyzed by a lactase.
    • Triacylglycerol is broken down into β-monoacylglycerol and fatty acid salts in a reaction catalyzed by a lipase.

    Activation of Zymogens

    • Zymogens are inactive enzyme precursors that require activation to become functional enzymes.
    • Examples of zymogens include pepsinogen, trypsinogen, and chymotrypsinogen.

    Properties of Enzymes

    • Apoenzymes are protein components of enzymes that lack catalytic activity without a cofactor.
    • Coenzymes are non-protein molecules that bind to apoenzymes to form active enzymes.
    • Examples of coenzymes include NAD+, FAD, and CoA.

    Metalloenzymes

    • Metalloenzymes are enzymes that contain a metal ion as a cofactor.
    • Examples of metalloenzymes include iron-containing enzymes, copper-containing enzymes, zinc-containing enzymes, and magnesium-containing enzymes.

    Enzyme Catalysis

    • Enzyme catalysis involves the binding of a substrate to an enzyme's active site, followed by a conformational change that facilitates the reaction.
    • The enzyme-substrate complex is stabilized by weak bonds, allowing the reaction to proceed more quickly.

    Active Site

    • The active site is the region of an enzyme where substrate binding and catalysis occur.
    • The active site is typically a cleft or pocket on the enzyme surface that is lined with amino acid residues that participate in substrate binding and catalysis.

    Systems Multienzyme

    • Systems multienzyme are complexes of multiple enzymes that work together to catalyze a series of reactions.
    • Examples of systems multienzyme include fatty acid synthase and pyruvate dehydrogenase complex.

    Regulation of Enzyme Activity

    • Enzyme activity can be regulated through various mechanisms, including substrate inhibition, allosteric regulation, and covalent modification.

    Inhibition of Enzyme Activity

    • Enzyme inhibitors can be classified into competitive, non-competitive, and uncompetitive inhibitors.
    • Competitive inhibitors bind to the active site, preventing substrate binding, while non-competitive inhibitors bind to an allosteric site, changing the enzyme's conformation and reducing activity.

    Industrial Applications of Enzymes

    • Enzymes are used in various industries, including food, detergent, and pharmaceutical industries.
    • Examples of enzymes used in industry include papain, amylase, and lipase.

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    Description

    Quiz about enzymes in nutrition, covering their role as catalysts, classification, and graphical representation of enzyme-catalyzed reactions.

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