PPT-Enzyme Regulation Control by

Allostery Glycogen Phosphorylase Control by Allostery amp Phosphorylation Glycogen n P i Glycogen n1 more active Enzyme Regulation Control by Allostery Glycogen Phosphorylase. 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 6. . Overproduction of Metabolites of Industrial Microorganisms. 2. The . organism’s genetic apparatus determines in . 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. . Competitive & Non-Competitive. Learning Objectives. To learn about what enzyme inhibition is.. To learn how competitive and non-competitive inhibitors affect the active site.. To understand the implications of inhibition of rates of reaction.. 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 . 10-1 :. Munich, Anne, Fluke, and Yu. Factors Affecting . Enzyme Activity. We are doing this experiment in order to test and find out the factors that has affects on the enzyme. . The indicator tells the substance’s chemical characteristic(pH). For red cabbage indicator. 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 . Lecturer Dr. . Kamal. E. M. . Elkahlout. Assistant Prof. of . Biotechnology. 1. CHAPTER 1. Fundamentals of Enzymes. 2. Fundamentals of enzymes. Why enzymes?. Enzyme nomenclature. Enzyme . units. Sources of . . Informal document . GRPE-74-13. 74th . GRPE. , . 9. -13 . January 2017,. A. genda . item . 6(a). UNECE Regulation . 96. on. Uniform . provisions concerning the approval of compression ignition (C.I.) engines . Therapy of enzyme defects: general considerations. How many organs are affected by the enzyme defect: One organ, a few, or all organs?. How severe is the defect?. Can the defect be adequately controlled by conventional treatment?.