CHEM351 Fall 2024 Enzymes Catalysis, Enzyme Kinetics, and Protein Function Study Guide PDF

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UnlimitedRadiance3949

Uploaded by UnlimitedRadiance3949

Southern Illinois University Edwardsville

2024

CHEM

Tags

enzymes enzyme kinetics protein function biochemistry

Summary

This study guide is for Exam #3 in CHEM351, Fall 2024, focusing on enzymes, catalysis, enzyme kinetics, and protein function. It covers various topics including enzyme models, reaction mechanisms, kinetics (Michaelis-Menten equation), enzyme inhibitors, and hemoglobin. The guide has numerous questions to aid in preparation for the exam.

Full Transcript

**Study Guide for Exam \#3. Enzymes Catalysis, Enzyme Kinetics and Protein Function** **CHEM351 Fall 2024** I. **Enzymes** What is an enzyme? **Review the models for substrate binding** **How do you calculate the rate of enhancement?** **What are Ribozymes?** **Do you und...

**Study Guide for Exam \#3. Enzymes Catalysis, Enzyme Kinetics and Protein Function** **CHEM351 Fall 2024** I. **Enzymes** What is an enzyme? **Review the models for substrate binding** **How do you calculate the rate of enhancement?** **What are Ribozymes?** **Do you understand the reaction coordinate diagram for an enzymatic reaction?** **How does enzyme achieve rate enhancement? (types of catalysis)** Review mechanisms of serine proteases What are the 6 major classes of enzymes? II. **Enzyme Kinetics** Do you understand saturation curve? Discuss assumptions of enzyme kinetics Do you understand Michaelis Menten equation (you don't need to derive it)? What is steady state assumption? What does the value for Km mean (definition)? What does Km tell you about the enzyme and the substrate? What is kcat? What is catalytic efficiency? What is the turnover number? Calculate Km and Vmax from a Lineweaver-Burke plot and include units. How does a competitive inhibitor affect kinetics (Vmax? Km?)? How does a uncompetitive inhibitor affect kinetics (Vmax? Km?)? How does a non-competitive inhibitor affect kinetics (Vmax? Km?)? Recognize Lineweave-Burke plots of each inhibition type. Discuss enzyme regulations III. **Hemoglobin** **Myoglobin (Mb) and hemoglobin (Hb); proteins structure and differences** **What is the Heme prosthetic group? How does it bind O~2~?** **What does the value for Y~O2~ mean?** **Do you understand the oxygen-binding curve for Hb and Mb?** **What is P~50~? What does it tell you about protein-oxygen binding?** **What happens when the externa P~O2~ or \[O~2~\] concentration varies?** **Do you know how to calculate P~50~ from an oxygen binding curve?** **Discuss Allostery. Understand the concept; How the equilibrium between conformation is shifted.** **Difference between the Tense (doxy) and the Relaxed (oxy) state.** **What is cooperativity?** **How does oxygen get transported from the lungs to the rest of the body?** **What are Allosteric effectors.** **What is the Bohr effect? How does the pH affect O~2~ binding? And under which circumstances?** **How does 2,3-BPG regulates O2 binding to hemoglobin?** **What happens when Hb is mutated? Is this mutation conservative or nonconservative? Why?**

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