PPT-Enzyme Theory

Biology Do not appreciate the awesomeness of enzymes How do enzymes work Lock and key theory Enzymes have a specific 3D structure They exactly match the shape of a molecule of substrate How do enzymes work. Watch the PowerPoint presentation and copy the notes.. When finished, assemble in a lab group of 2 students and begin planning your experiment.. A rough overview of your experiment is due at the end of class that includes:. Chapter 2: Section 2.5. 1. Objectives. SWBAT explain the effect of a catalyst on activation energy. . SWBAT describe how enzymes regulate chemical reactions. . and maintain homeostasis.. 2. Starter: How can this be possible. C483 Spring 2013. Questions. 1. Enzymes . that join two substrates and require energy of a nucleoside triphosphate (such as ATP) to do so are called. A. ) . isomerases. .. B. ) . lyases. .. C. ) ligases.. Lecturer Dr. . Kamal. E. M. . Elkahlout. Assistant Prof. of . Biotechnology. 1. CHAPTER 3. Immobilized . enzymes and their . uses. 2. Enzyme reactors. An enzyme reactor consists of a vessel, or series of vessels, used to perform a desired conversion by enzymatic means (Figure 5.1). . Inhibition. C483 Spring 2013. Questions. 1. . An inhibitor binds to a site other than the active site of the enzyme. Which statement below correlates with this observation? . A. ) It must be a competitive inhibitor. . Inhibition is a term used to describe the inability of a product being formed due to the presence of another substance (the inhibitor). Enzyme inhibition . can be competitive or noncompetitive. Competitive inhibition is caused when an inhibitor “competes” with the substrate in binding with the enzyme. Pratt & . Cornely. . Ch. 7. Other Factors. Other factors affect enzyme activity. Temperature. pH . pH Optimum. Determined by structural stability. Compartmentalization. Determined by active site residues. Mechanisms. C483 Spring 2013. Questions. 1. . Replacement of the amino acid ________ at or near an active site of an enzyme is more likely to change enzyme activity than the replacement of ________ at or near the active site.. Learning Objectives. Learn how the rate of an enzyme controlled reaction is measured.. Learn how temperature affects the rate of an enzyme controlled reaction.. Learn how pH affects the rate of an enzyme controlled reaction.. Lecturer Dr. . Kamal. E. M. . Elkahlout. Assistant Prof. of . Biotechnology. 1. CHAPTER 4. Recent Advances. 2. Enzymatic reactions in biphasic liquid systems. E. nzyme catalyzed . reactions could be performed in solvents other than . Pratt & . Cornely. . Ch. 7. Enzyme Kinetics. How fast an enzyme catalyzed reaction goes. Why study enzyme kinetics?. Helps us understand mechanism of enzyme (how it works). Investigation of mutations in metabolic pathways. Phosphorylation is a type of covalent modification that activates or deactivates an enzyme.. a. ) A . kinase activates an . inactive enzyme . by phosphorylation. . b. ) A . phosphatase activates . an inactive . Stryer. Short Course. Chapter 6. Enzymes. Biocatalysts. Active site. Substrate and product. Catalyzed rate. Uncatalyzed. rate. Rate Enhancement. Which is a better catalyst, carbonic anhydride. Or OMP decarboxylase? Defend your answer.. Katja. Dove. PhD Candidate, . Department of Biochemistry, University of Washington. Email: Katja.Dove@seattlecolleges.edu. Please turn in your take-home part for midterm 1 BEFORE class. I will hand back in-class exams at the end of class today.