PPT-20.4 Regulation of Enzyme Activity

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 . Lecture 3. Objective. To understand . Specificity of enzymes. Specificity means:. Ability of an enzyme to . catalyse. a specific reaction and NO others. The active site. The . active site, . is. . 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 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. 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 :. 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. Presented by: Paula Freeman, CSC. Self-Regulation. Self-regulation. makes it possible for us to know and manage our emotions, recognize emotions in others, and make use of these abilities in relationships. With adequate self regulation, we are able to control immediate responses to stimuli in order to make behavioral choices (Tollison, Synatschk, & Logan, 2011).. 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 . 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 . In this experiment, we will continue to study acid phosphatase kinetics.. Objective:. To establish the relationship between enzyme concentration and the rate of an enzyme catalyzed reaction.. The reaction rate will increase as the concentration of enzymes is increased but there must be a . 322 BCH. . . Exp. (6). In this experiment, we will continue to study . acid phosphatase . kinetics.. Objectives. To establish the relationship between pH and the rate of an enzyme catalyzed reaction.. 2- ISOENZYMES:. Some . of the enzymes are present in more than one form having the same molecular weight and differ in conformational structures called isoenzymes, e.g. Trypsinogen isoenzymes . are present . Drill:. . What background knowledge do you have on enzymes?. Enzyme Structure and Function. Enzymes are . protein catalysts. They speed up the rate at which reactions occur. Lower the activation energy by creating a microenvironment that is energetically more favorable for a reaction. Enzyme Inhibition. Regulation of Enzyme Activity. Clinical Applications of . Enzymes. Enzymes. Factors . A. ffecting Enzymatic . A. ctivity. Enzymes are . most active at an optimum temperature (usually 37°C in humans)..