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Questions and Answers
Which coenzymes are involved in the generation of ATP from the oxidation of fuels?
Which compounds act as antioxidants and protect against oxygen free-radical injury?
Which category of enzymes is involved in the transfer of hydrogen from the substrate to an electron-accepting coenzyme?
Which coenzymes work with metals to transfer single electrons to oxygen?
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Which coenzyme is covalently attached to a lysine residue in the carboxylase enzyme for carboxylation reactions?
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Which coenzyme has a reactive aldehyde that forms a covalent intermediate with amino acids, acting as an electron-withdrawing group for electrophilic catalysis?
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Which coenzymes have unique functional groups for electron transfer and require enzyme participation?
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In oxidation reactions, which coenzyme accepts a hydride ion from lactate, leading to the reduction of NADH?
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How is NAD+ synthesized?
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Which metal ion is involved in the oxidation of ethanol to acetaldehyde by alcohol dehydrogenase (ADH) in the liver?
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What role do metal ions like Mg2+ play in catalysis?
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How is ethanol in serum analyzed?
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What role do metal ions play in enzymes like alcohol dehydrogenase?
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Apart from catalytic roles, what other function can cofactors play in enzymes?
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Which type of enzyme catalyzes the cleavage of carbon–carbon bond, such as fructose 1,6-bisphosphate aldolase in glycolysis?
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What type of enzyme removes water from carbon–carbon bonds to form a double bond?
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Which enzyme type creates isomers of the starting material by rearranging the existing atoms of a molecule?
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What type of enzyme synthesizes C–C, C–S, C–O, and C–N bonds in reactions coupled to the cleavage of a high-energy phosphate bond in ATP or another nucleotide?
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Which enzyme type cleaves C–O, C–N, or C–S bonds through hydrolysis reactions?
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What type of enzyme catalyzes carbon–carbon bond cleavage by means other than hydrolysis or oxidation?
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Which enzyme type catalyzes the transfer of a group that exists as a good leaving group on the donor molecule?
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What type of enzyme is involved in the donation of a nitrogen group from an amino acid to an α-keto acid, forming a new amino acid and the corresponding donor α-keto acid?
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Which enzyme type requires the coenzyme pyridoxal phosphate?
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What type of enzyme may be called synthases when the physiologically important aspect is the compound synthesized?
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How do enzymes accelerate reaction rates?
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What is the mechanism of action of penicillin as an enzyme inhibitor?
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How does allopurinol function as an inhibitor?
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What is the consequence of mercury binding to reactive sulfhydryl groups in enzyme active sites?
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How does lead contribute to toxicity?
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What is the primary effect of ethanol oxidation in the liver?
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What is the role of xanthine oxidase in purine metabolism?
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How does acetylcholine accumulation affect the autonomic nervous system?
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What type of reactions do transferases catalyze?
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How does heavy-metal toxicity occur?
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What is the consequence of allopurinol's inhibition of xanthine oxidase?
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How does ethanol oxidation in the liver contribute to tissue damage?
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Study Notes
Enzyme Inhibitors and Toxicity
- Acetylcholine accumulation overstimulates the autonomic nervous system, causing vomiting, cramps, salivation, and sweating.
- Penicillin is a transition-state analog that binds tightly to glycopeptidyl transferase, inhibiting bacterial cell wall synthesis.
- Penicillin is a suicide inhibitor that irreversibly binds to the enzyme's active site, inactivating it.
- Allopurinol is a suicide inhibitor of xanthine oxidase, decreasing urate production and treating gout.
- Heavy-metal toxicity occurs when metals like mercury, lead, aluminum, or iron bind tightly to enzyme functional groups.
- Mercury binds to reactive sulfhydryl groups in enzyme active sites, causing toxicity.
- Lead replaces normal functional metals in enzymes, such as calcium, iron, or zinc, causing developmental and neurologic toxicity.
- Xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and uric acid, and is inhibited by allopurinol.
- Allopurinol prevents the generation of uric acid, treating gout by inhibiting xanthine oxidase.
- Ethanol oxidation in the liver produces acetaldehyde, which can damage the liver, heart, and other tissues.
- At low ethanol intakes, acetaldehyde is safely oxidized to acetate in the liver by aldehyde dehydrogenases.
- Transferases catalyze group transfer reactions, such as the transfer of high-energy phosphates, carbohydrates, or fatty acyl groups.
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Description
Test your knowledge of enzyme inhibitors and toxicity with this quiz. Explore the effects of acetylcholine accumulation, penicillin as a transition-state analog, allopurinol as a suicide inhibitor, and the impact of heavy-metal toxicity. Learn about the inhibition of xanthine oxidase by allopurinol and ethanol oxidation in the liver.
