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Questions and Answers
What is one of the roles that metas can play in enzyme reactions?
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?
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?
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?
What type of bonding do cofactors utilize with enzymes or substrates?
Which role can meta ions serve in enzymatic reactions?
Which role can meta ions serve in enzymatic reactions?
Which of the following best describes the function of cofactors?
Which of the following best describes the function of cofactors?
Which property of metas enhances substrate reactivity?
Which property of metas enhances substrate reactivity?
What distinguishes meta ions from other cofactors?
What distinguishes meta ions from other cofactors?
Which enzyme is known to cleave peptide bonds on the carboxy-terminal side of large hydrophobic amino acids?
Which enzyme is known to cleave peptide bonds on the carboxy-terminal side of large hydrophobic amino acids?
What term is used to describe distinct enzyme forms that catalyze the same reaction?
What term is used to describe distinct enzyme forms that catalyze the same reaction?
What concept explains the evolutionary relationship of enzymes based on specific amino acids in relative positions?
What concept explains the evolutionary relationship of enzymes based on specific amino acids in relative positions?
What is commonly observed in higher organisms regarding enzyme forms?
What is commonly observed in higher organisms regarding enzyme forms?
What mechanism is often used in higher eukaryotes to generate various forms of enzymes?
What mechanism is often used in higher eukaryotes to generate various forms of enzymes?
Which of the following statements about enzyme assays is true?
Which of the following statements about enzyme assays is true?
In the context of enzyme evolution, what does the term 'evolutionarily conserved residues' refer to?
In the context of enzyme evolution, what does the term 'evolutionarily conserved residues' refer to?
What does trypsin cleave peptide bonds adjacent to?
What does trypsin cleave peptide bonds adjacent to?
What role do coenzymes play in one-carbon metabolism?
What role do coenzymes play in one-carbon metabolism?
How do enzymes discriminate between their substrates?
How do enzymes discriminate between their substrates?
What is suggested by describing the enzyme's active site as a 'lock'?
What is suggested by describing the enzyme's active site as a 'lock'?
What do FADH2 and NADH stabilize during enzymatic reactions?
What do FADH2 and NADH stabilize during enzymatic reactions?
What is the primary function of coenzymes according to their described properties?
What is the primary function of coenzymes according to their described properties?
What aspect of coenzymes contributes to their ability to serve as substrate shuttles?
What aspect of coenzymes contributes to their ability to serve as substrate shuttles?
What can be inferred about enzymatic active sites from the description provided?
What can be inferred about enzymatic active sites from the description provided?
What is a characteristic feature of several coenzymes mentioned?
What is a characteristic feature of several coenzymes mentioned?
What role does the nucleophile His 392 play in the enzymatic reaction?
What role does the nucleophile His 392 play in the enzymatic reaction?
Which molecule assists in the nucleophilic attack resulting in the formation of inorganic phosphate?
Which molecule assists in the nucleophilic attack resulting in the formation of inorganic phosphate?
What is high-throughput screening (HTS) primarily used for?
What is high-throughput screening (HTS) primarily used for?
In what manner do isozymes differ from one another?
In what manner do isozymes differ from one another?
At which site does the fructose-6-phosphate leave the enzyme in the reaction process?
At which site does the fructose-6-phosphate leave the enzyme in the reaction process?
What is the wavelength at which NAD(P)H absorbs light?
What is the wavelength at which NAD(P)H absorbs light?
What types of methods complement high-throughput screening?
What types of methods complement high-throughput screening?
What happens to absorbance at 340 nm when NAD(P)+ is reduced?
What happens to absorbance at 340 nm when NAD(P)+ is reduced?
Which of the following statements is true regarding the role of arginine residues in the process described?
Which of the following statements is true regarding the role of arginine residues in the process described?
Which enzyme is primarily indicated in the coupled enzyme assay for hexokinase activity?
Which enzyme is primarily indicated in the coupled enzyme assay for hexokinase activity?
How do isozymes enhance survival according to the provided information?
How do isozymes enhance survival according to the provided information?
Which enzyme's analysis plays a central role in diagnosing disease processes, as mentioned?
Which enzyme's analysis plays a central role in diagnosing disease processes, as mentioned?
What is a possible product of the glucose-6-phosphate dehydrogenase reaction?
What is a possible product of the glucose-6-phosphate dehydrogenase reaction?
Which of the following is NOT a function of NAD(P)+?
Which of the following is NOT a function of NAD(P)+?
Which component is necessary for the conversion of glucose into glucose-6-phosphate?
Which component is necessary for the conversion of glucose into glucose-6-phosphate?
In the coupled enzyme assay, what is formed from NAD+ when it undergoes reduction?
In the coupled enzyme assay, what is formed from NAD+ when it undergoes reduction?
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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.
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