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Questions and Answers
How do sulfa drugs inhibit bacterial growth?
How do sulfa drugs inhibit bacterial growth?
Sulfa drugs inhibit bacterial growth by competitively inhibiting the enzymes that normally react with PABA, preventing the synthesis of folic acid.
What is the main structural difference that allows penicillin to target bacteria but not human cells?
What is the main structural difference that allows penicillin to target bacteria but not human cells?
The main structural difference is that bacteria possess a cell wall, while human cells do not.
What role does the enzyme transpeptidase play in bacterial cell wall synthesis?
What role does the enzyme transpeptidase play in bacterial cell wall synthesis?
Transpeptidase cleaves terminal d-alanine and facilitates the cross-linking of peptidoglycan layers in the bacterial cell wall.
How do penicillins act as inhibitory substrates for transpeptidase?
How do penicillins act as inhibitory substrates for transpeptidase?
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Explain why sulfa drugs are ineffective in humans.
Explain why sulfa drugs are ineffective in humans.
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What does Km represent in enzyme kinetics?
What does Km represent in enzyme kinetics?
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How is Km related to the binding affinity of the substrate to the enzyme?
How is Km related to the binding affinity of the substrate to the enzyme?
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Explain the significance of the Lineweaver-Burke plot in determining Km.
Explain the significance of the Lineweaver-Burke plot in determining Km.
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What happens to Km when the substrate concentration, S, is very low?
What happens to Km when the substrate concentration, S, is very low?
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How does the value of vmax relate to the turnover number of an enzyme?
How does the value of vmax relate to the turnover number of an enzyme?
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What type of reaction does an oxidase catalyze?
What type of reaction does an oxidase catalyze?
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Name one substrate and its corresponding enzyme from the hydrolases class.
Name one substrate and its corresponding enzyme from the hydrolases class.
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What do transferases specifically facilitate in biochemical reactions?
What do transferases specifically facilitate in biochemical reactions?
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Describe the action of lyases and provide an example.
Describe the action of lyases and provide an example.
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Identify and define one type of enzyme that belongs to the isomerases class.
Identify and define one type of enzyme that belongs to the isomerases class.
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What is the primary action of hydrolases in biochemical reactions?
What is the primary action of hydrolases in biochemical reactions?
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Explain how dehydrogenases function in enzymatic reactions.
Explain how dehydrogenases function in enzymatic reactions.
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How are enzyme names typically structured based on their function and substrates?
How are enzyme names typically structured based on their function and substrates?
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What is the role of protein modification in enzyme activity?
What is the role of protein modification in enzyme activity?
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How do irreversible inhibitors affect enzyme activity?
How do irreversible inhibitors affect enzyme activity?
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Describe competitive inhibition.
Describe competitive inhibition.
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What distinguishes noncompetitive inhibition from competitive inhibition?
What distinguishes noncompetitive inhibition from competitive inhibition?
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What is the role of kinases and phosphatases in protein modification?
What is the role of kinases and phosphatases in protein modification?
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What is a structural analog in the context of enzyme inhibition?
What is a structural analog in the context of enzyme inhibition?
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Explain how chemotherapy relates to enzyme activity.
Explain how chemotherapy relates to enzyme activity.
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Give an example of an irreversible inhibitor and its effect.
Give an example of an irreversible inhibitor and its effect.
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What is the significance of the slope and intercept in the plot of 1/υ vs. 1/(S)?
What is the significance of the slope and intercept in the plot of 1/υ vs. 1/(S)?
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List the vitamin that acts as a coenzyme in decarboxylation reactions and its deficiency symptoms.
List the vitamin that acts as a coenzyme in decarboxylation reactions and its deficiency symptoms.
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What coenzyme is associated with riboflavin (B2) and what are some symptoms of its deficiency?
What coenzyme is associated with riboflavin (B2) and what are some symptoms of its deficiency?
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Which vitamin is known for its role in numerous redox reactions and name the deficiency it causes?
Which vitamin is known for its role in numerous redox reactions and name the deficiency it causes?
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What is the function of coenzyme A, and is there a known deficiency syndrome for pantothenic acid (B5)?
What is the function of coenzyme A, and is there a known deficiency syndrome for pantothenic acid (B5)?
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Which coenzyme is linked to amino acid reactions involving transamination and what are the potential deficiency symptoms?
Which coenzyme is linked to amino acid reactions involving transamination and what are the potential deficiency symptoms?
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Identify the coenzyme for CO2 fixation reactions and its associated deficiency symptoms.
Identify the coenzyme for CO2 fixation reactions and its associated deficiency symptoms.
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What role does tetrahydrofolic acid play and what are the consequences of its deficiency?
What role does tetrahydrofolic acid play and what are the consequences of its deficiency?
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Cyanocobalamine is known for which specific biochemical processes, and what deficiency does it cause?
Cyanocobalamine is known for which specific biochemical processes, and what deficiency does it cause?
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What is the primary function of ascorbic acid (Vitamin C) and what deficiency symptoms may arise?
What is the primary function of ascorbic acid (Vitamin C) and what deficiency symptoms may arise?
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Study Notes
Enzyme Reactions and Nomenclature
- Enzymes are categorized by their reaction type, indicated by prefixes; examples include oxidase for oxidation and hydrolase for hydrolysis.
- Substrates can also be included in enzyme names, e.g., glucose oxidase and pyruvate carboxylase.
- Enzymes are classified into six major classes by the International Union of Biochemistry.
Classification of Enzymes
-
Oxidoreductases: Catalyze oxidation-reduction reactions.
- Oxidases: Facilitate oxidation.
- Reductases: Facilitate reduction.
- Dehydrogenases: Introduce double bonds by removing H₂, transferring hydrogen to coenzymes.
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Transferases: Aid in transferring functional groups.
- Kinases: Transfer phosphate groups.
- Transaminases: Transfer amino groups.
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Hydrolases: Add water to break bonds.
- Proteases: Hydrolyze peptide bonds in proteins.
- Carbohydrases: Hydrolyze glycosidic bonds (including sucrase and lactase).
- Lipases: Hydrolyze ester bonds in lipids.
- Nucleases: Hydrolyze sugar phosphate bonds in nucleic acids.
- Phosphatases: Hydrolyze phosphate ester bonds.
-
Lyases: Remove/add groups to form double bonds without hydrolysis.
- Dehydratases: Remove water.
- Decarboxylases: Remove carbon dioxide.
- Deaminases: Remove ammonia.
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Isomerases: Convert substrates into isomers.
- Racemases: Convert D to L isomers.
Enzyme Activation and Regulation
- Protein modification, particularly phosphorylation, can activate or inactivate enzymes.
- Kinases phosphorylate proteins, while phosphatases dephosphorylate them.
Inhibition of Enzyme Activity
-
Irreversible Inhibitors: Form covalent bonds with enzymes, blocking activity permanently (e.g., diisopropylphosphofluoridate).
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Reversible Inhibitors: Bind non-covalently and can be released.
- Competitive Inhibition: Inhibitor competes with substrate for active sites; can be overcome by increasing substrate.
- Noncompetitive Inhibition: Inhibitor binds elsewhere, altering enzyme activity without blocking substrate binding.
Chemotherapy and Antibiotics
- Chemotherapy: Uses chemicals to target infectious microorganisms.
- Antimetabolites: Act through competitive inhibition (e.g., sulfa drugs mimic PABA).
- Antibiotics: Target bacterial-specific structures like cell walls (e.g., penicillin inhibits cell wall synthesis enzymes).
Michaelis-Menten Kinetics
- Vmax: Maximum reaction rate; influenced by substrate concentration.
- Km (Michaelis constant): Substrate concentration at which reaction velocity is half of Vmax; indicative of substrate affinity.
Lineweaver-Burke Plots
- Linear transformation of Michaelis-Menten equation allows for easier determination of Km and Vmax.
- Slope represents Km/Vmax; intercepts provide Vmax and -1/Km.
Coenzymes and Vitamins
- Water-soluble vitamins play crucial roles as coenzymes in metabolic reactions.
- Thiamine (B1): Decarboxylation; deficiency leads to beriberi.
- Riboflavin (B2): Redox reactions; deficiency causes dermatitis and glossitis.
- Niacin (B3): Redox reactions; deficiency leads to pellagra.
- Pantothenic Acid (B5): Transfers acetyl groups; no known deficiency.
- Pyridoxine (B6): Key for amino acid reactions; deficiency can cause dermatitis and anemia.
- Biotin: CO2 fixation; deficiency leads to dermatitis and fatigue.
- Folic Acid: Involved in C-compound reactions; deficiency results in abnormal blood counts.
- Cyanocobalamin (Vitamin B12): Isomerization and methyl transfers; deficiency leads to pernicious anemia.
- Ascorbic Acid (Vitamin C): Necessary for collagen formation; deficiency leads to scurvy.
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Description
This quiz focuses on the nomenclature and classification of enzymes based on the reactions they catalyze and their substrates. You'll explore common enzyme suffixes and prefixes, and how specific enzymes are named. Test your knowledge on important terms in biochemistry!