PPT-Enzyme Regulation

Author : briana-ranney | Published Date : 2015-10-27

C483 Spring 2013 Questions 1 Which statement is false about allosteric regulation A It is usually the mode of regulation for the last step in reaction pathways

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Enzyme Regulation: Transcript


C483 Spring 2013 Questions 1 Which statement is false about allosteric regulation A It is usually the mode of regulation for the last step in reaction pathways since this step produces the final product . 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:. 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 . 1. Dr. Nikhat Siddiqi. The most responsive regulation of amino acid . synthesis takes . place through feedback inhibition of the first . reaction in . a sequence by the end product of the pathway.. This first reaction is usually irreversible and . Chapter 17 . Stryer. Short Course. Glucose Metabolism Overview. Gluconeogenesis. Glycogen . metabolism. Pentose Phosphate Pathway. Precursors for Gluconeogenesis. Names of compounds?. Type of reaction?. 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. 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 . http://. courses.ucsd.edu. /. rhampton. /bibc102/. Randy. ’. s bipartite office hours. . Wed . 3-4 pm. . Thr. . 3-4 pm . 2130 Pacific Hall. BIBC 102 Web Site. Activation energy and reaction rate. 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?. Objectives. -Understand how Restriction Enzymes digest DNA.. -Know how to construct a . pAMP. . (plasmid) or gel.. -Given the size of fragments, gel, know how to construct a restriction map.. -Given a restriction map know how to construct a gel.. BC 2.5 Microbiology and Genetics 12 2 6 85 BC 2.6 Quantitative Analysis and Molecular Biology 12 2 6 85 BC 2.7 Viva-Voce -- 1 25 ----- Total marks Allostery. :. Glycogen Phosphorylase:. Control by . Allostery. & Phosphorylation. Glycogen. (n). +. P. i. +. Glycogen. (n-1). . (more active). Enzyme Regulation. Control by . Allostery. :. Glycogen Phosphorylase:. -. The SSERC Team. Effect of competitive and non. –. competitive inhibitors on . . ‑galactosidase. Paul Beaumont / Kate Andrews /. Margaret Louis. b. -galactosidase. b. -galactosidase. Competitive inhibition. By- . Shubhani. . singh. thakur. department of biochemistry. Contents. Introduction. History. Properties. Modulators. Types of . Allosteric. Regulation. Models of . Allosteric. Regulation. Allosteric.

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