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Enzymology QnA

Short Questions and answers

1. What is the principle of catalysis in enzymology?
  • Enzymes act as biological catalysts, increasing the rate of chemical reactions by lowering the activation energy required for the reaction to occur. They do this by providing an alternative reaction pathway with a lower energy barrier.

2. What are enzymes, and how do they function?
  • Enzymes are biological macromolecules, usually proteins, that speed up chemical reactions by binding to reactants (substrates) and facilitating their conversion into products. Enzymes are highly specific to their substrates.

3. What is enzyme kinetics?
  • Enzyme kinetics is the study of the rates of enzyme-catalyzed reactions. It involves measuring parameters like reaction rate, substrate concentration, and enzyme activity to understand the enzyme's performance.

4. Explain the Michaelis-Menten equation and its significance in enzyme kinetics.
  • The Michaelis-Menten equation describes the relationship between substrate concentration and the initial reaction rate. It's essential for determining the enzyme's maximum reaction rate (Vmax) and the substrate concentration at which the enzyme is half-saturated (Km).

5. How are enzymes regulated in biological systems?
  • Enzymes are regulated through mechanisms such as allosteric regulation, competitive and non-competitive inhibition, covalent modification, and feedback inhibition. These processes control the rate of enzymatic reactions in response to the cell's needs.

6. What is the mechanism of enzyme catalysis, and what are some common catalytic mechanisms used by enzymes?
  • Enzymes catalyze reactions through several mechanisms, including acid-base catalysis, covalent catalysis, and metal ion catalysis. These mechanisms involve interactions with substrates to lower activation energy.

7. How are enzymes important in the field of diagnosis and therapy?
  • Enzymes are crucial in diagnostic tests, as they can be used as biomarkers to detect specific diseases or conditions. Enzyme-linked assays, such as ELISA, are widely used for diagnostic purposes. Enzyme-based therapies, like enzyme replacement therapy, are employed to treat enzyme deficiencies or related disorders.

8. Give an example of how enzymes are used in clinical diagnosis.
  • Enzyme markers like creatine kinase (CK) and troponin are used in diagnosing heart conditions, while amylase and lipase levels help diagnose pancreatitis. Elevated or lowered levels of these enzymes can indicate specific medical conditions.

9. How do enzyme inhibitors play a role in drug development and therapy?
  • Enzyme inhibitors are often used to design drugs that target specific enzymes involved in disease pathways. For example, protease inhibitors are used to treat HIV, and acetylcholinesterase inhibitors are employed in Alzheimer's disease therapy.

10. What are the challenges and considerations in using enzymes for therapy and diagnostics?
  • Enzyme stability, specificity, and potential immunogenicity are important considerations when using enzymes in therapy and diagnostics. Ensuring proper storage and delivery of enzymes is also crucial.

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