Biochemistry: Meta Ions and Cofactors
40 Questions
0 Views

Choose a study mode

Play Quiz
Study Flashcards
Spaced Repetition
Chat to lesson

Podcast

Play an AI-generated podcast conversation about this lesson

Questions and Answers

What is one of the roles that metas can play in enzyme reactions?

  • They can permanently bond with substrates.
  • They can contribute to substrate orientation. (correct)
  • They act only as catalytic agents.
  • They exclusively increase reaction temperature.
  • How do cofactors differ from prosthetic groups?

  • Cofactors bind weakly and transiently. (correct)
  • Cofactors have no impact on enzyme stability.
  • Cofactors are not required for catalysis.
  • Cofactors bind strongly and permanently.
  • Which statement accurately describes the necessity of cofactors in catalysis?

  • Cofactors are not always present in the environment
  • Cofactors solely support the enzyme structure.
  • Cofactors do not influence the formation of enzyme-substrate complexes.
  • Cofactors must be present in the surrounding environment for catalysis to occur. (correct)
  • What type of bonding do cofactors utilize with enzymes or substrates?

    <p>Weak and transient associations.</p> Signup and view all the answers

    Which role can meta ions serve in enzymatic reactions?

    <p>They can increase the nucleophilicity of substrates.</p> Signup and view all the answers

    Which of the following best describes the function of cofactors?

    <p>Cofactors have no enzymatic activity on their own.</p> Signup and view all the answers

    Which property of metas enhances substrate reactivity?

    <p>They convert substrates to electron-rich or electron-poor states.</p> Signup and view all the answers

    What distinguishes meta ions from other cofactors?

    <p>Meta ions form the most numerous class of cofactors.</p> Signup and view all the answers

    Which enzyme is known to cleave peptide bonds on the carboxy-terminal side of large hydrophobic amino acids?

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

    What term is used to describe distinct enzyme forms that catalyze the same reaction?

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

    What concept explains the evolutionary relationship of enzymes based on specific amino acids in relative positions?

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

    What is commonly observed in higher organisms regarding enzyme forms?

    <p>They elaborate several physically distinct versions of a given enzyme.</p> Signup and view all the answers

    What mechanism is often used in higher eukaryotes to generate various forms of enzymes?

    <p>Gene duplication</p> Signup and view all the answers

    Which of the following statements about enzyme assays is true?

    <p>Enzyme assays are frequently used for assessing catalytic activity.</p> Signup and view all the answers

    In the context of enzyme evolution, what does the term 'evolutionarily conserved residues' refer to?

    <p>Amino acids that remain unchanged in position over evolutionary time.</p> Signup and view all the answers

    What does trypsin cleave peptide bonds adjacent to?

    <p>Basic amino acids</p> Signup and view all the answers

    What role do coenzymes play in one-carbon metabolism?

    <p>They act as substrate shuttles transporting reactive species.</p> Signup and view all the answers

    How do enzymes discriminate between their substrates?

    <p>Through high specificity based on coenzyme components.</p> Signup and view all the answers

    What is suggested by describing the enzyme's active site as a 'lock'?

    <p>It selectively binds specific substrates much like a key fits a lock.</p> Signup and view all the answers

    What do FADH2 and NADH stabilize during enzymatic reactions?

    <p>Reactive species like hydrogen atoms or hydride ions.</p> Signup and view all the answers

    What is the primary function of coenzymes according to their described properties?

    <p>To transport and stabilize reactive species.</p> Signup and view all the answers

    What aspect of coenzymes contributes to their ability to serve as substrate shuttles?

    <p>Their recyclability and capacity to stabilize reactive species.</p> Signup and view all the answers

    What can be inferred about enzymatic active sites from the description provided?

    <p>They facilitate chemical transformations through an optimal environment.</p> Signup and view all the answers

    What is a characteristic feature of several coenzymes mentioned?

    <p>They include components like adenine, ribose, and phosphate.</p> Signup and view all the answers

    What role does the nucleophile His 392 play in the enzymatic reaction?

    <p>It transfers a phosphoryl group to His 258.</p> Signup and view all the answers

    Which molecule assists in the nucleophilic attack resulting in the formation of inorganic phosphate?

    <p>Glu 327</p> Signup and view all the answers

    What is high-throughput screening (HTS) primarily used for?

    <p>To conduct large-scale enzyme assays rapidly.</p> Signup and view all the answers

    In what manner do isozymes differ from one another?

    <p>They provide a backup for essential enzymes.</p> Signup and view all the answers

    At which site does the fructose-6-phosphate leave the enzyme in the reaction process?

    <p>Upon the release of inorganic phosphate.</p> Signup and view all the answers

    What is the wavelength at which NAD(P)H absorbs light?

    <p>340 nm</p> Signup and view all the answers

    What types of methods complement high-throughput screening?

    <p>Data processing and robotics.</p> Signup and view all the answers

    What happens to absorbance at 340 nm when NAD(P)+ is reduced?

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

    Which of the following statements is true regarding the role of arginine residues in the process described?

    <p>They are involved in the release of inorganic orthophosphate.</p> Signup and view all the answers

    Which enzyme is primarily indicated in the coupled enzyme assay for hexokinase activity?

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

    How do isozymes enhance survival according to the provided information?

    <p>By acting as backup copies of essential enzymes.</p> Signup and view all the answers

    Which enzyme's analysis plays a central role in diagnosing disease processes, as mentioned?

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

    What is a possible product of the glucose-6-phosphate dehydrogenase reaction?

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

    Which of the following is NOT a function of NAD(P)+?

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

    Which component is necessary for the conversion of glucose into glucose-6-phosphate?

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

    In the coupled enzyme assay, what is formed from NAD+ when it undergoes reduction?

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

    Study Notes

    Meta Ions and Their Role

    • Meta ions facilitate binding and orientation of substrates in enzymatic reactions.
    • They form covalent bonds with reaction intermediates, such as Co2+ in coenzyme B12.
    • Acting as Lewis acids or bases, they influence the electrophilicity (electron-poor) or nucleophilicity (electron-rich) of substrates, increasing their reactivity.

    Cofactors and Enzyme Interaction

    • Cofactors interact reversibly with enzymes or substrates, forming transient complexes required for catalysis.
    • Unlike prosthetic groups, cofactors need to be present in the environment for successful enzyme-substrate interaction.
    • They can stabilize reactive species like hydrogen atoms or hydride ions, aiding in substrate transport and reactivity.

    Coenzymes as Substrate Shuttles

    • Coenzymes serve as recyclable shuttles, transporting reactive substrates within cells.
    • They stabilize highly reactive intermediates that cannot endure for extended periods.
    • The active site of an enzyme not only recognizes substrates but also provides an environment for chemical transformation.

    Isozymes: Distinct Enzyme Forms

    • Isozymes are different physical forms of an enzyme that catalyze the same reaction.
    • They may arise from gene duplication or alternative mRNA splicing in evolved organisms.
    • Isozymes can differ in regulatory sensitivity and are adapted for specific tissues, providing backup for essential enzymes.

    Enzyme Activity Analysis and Disease Diagnosis

    • Enzyme assays are crucial in research and clinical settings for diagnosing diseases.
    • Common enzymes in blood plasma include pseudocolinesterase and lipoprotein lipase, serving as functional constituents in disease processes.
    • Reduced coenzymes NADH and NADPH absorb light at 340 nm, allowing quantification of enzymatic activity through absorbance changes in assays.

    Studying That Suits You

    Use AI to generate personalized quizzes and flashcards to suit your learning preferences.

    Quiz Team

    Related Documents

    Description

    Explore the crucial roles of meta ions and cofactors in enzymatic reactions. This quiz delves into how coenzymes function as substrate shuttles and the interactions between enzymes and cofactors. Test your understanding of these essential biochemical components.

    More Like This

    Common Ions and Their Charges Flashcards
    80 questions
    Common Polyatomic Ions Flashcards
    22 questions
    Flashcards de Ions Poliatomicos Comunes
    22 questions
    Chemistry: Ions and Isotopes Quiz
    14 questions
    Use Quizgecko on...
    Browser
    Browser