PPT-Enzyme

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. 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. immobilised enzyme enzyme 21. An enzyme specifically through a this respect, lipoamide dehydrogenase particularly useful enzyme comprises two polypeptide chains each binding binding and containing 10 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. . 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. Lab Presentation. By May, Nam T., . Por. , . Parn. , . Mook. , Mix (10-9). Objective . To study how pH, temperature, ionic conditions, substrate concentration affects enzyme activity. Something you should know before :. 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 . 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?. Objectives. To monitor the progress of an enzyme catalyzed reaction (Acid phosphatase).. To determine the initial rate of the reaction (. V. i. ).. Important terms and points:. Enzyme kinetics. The central approach for studying the mechanism of an enzyme-catalyzed reaction is to study enzyme kinetics. . Introduction:. All . enzyme assays measure either the. consumption of substrate or production of product over time. . Different enzymes require different estimation methods . dependingon. the type of . 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.