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Chapter 8 teacher notes Bio

by: Marla Notetaker

Chapter 8 teacher notes Bio BSC 2010

Marketplace > University of South Florida > Biology > BSC 2010 > Chapter 8 teacher notes Bio
Marla Notetaker
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About this Document

As usual....... notes for this chapter courtesy of the lesson
Biology I Cellular Processes
Dr. Eric M. Sikorski
Class Notes
Energy, Cell, ATP, Enzymes, regeneration, Inhibition, allosteric




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This 2 page Class Notes was uploaded by Marla Notetaker on Monday October 3, 2016. The Class Notes belongs to BSC 2010 at University of South Florida taught by Dr. Eric M. Sikorski in Fall 2016. Since its upload, it has received 25 views. For similar materials see Biology I Cellular Processes in Biology at University of South Florida.


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Date Created: 10/03/16
Chapter 8 Concept 8.1  Metabolism= catabolic + anabolic processes  Catabolic: break down  Anabolic: synthesize I. Organization of the Chemistry of Life into Metabolic Pathways  Pathways: series of reactions producing a product  Most pathways are NOT terminal, meaning that their product end up being for something else.  All these reactions require catalysis – enzymes  Cellular respiration: breakdown of glucose (or other monomer carb) using O2  Fermentation: without O2  Catabolic: release energy  Bioenergetics: study of metabolism II. Forms of Energy  Energy: capacity to do work  Kinetic: energy of motion o Heat (thermal)  Potential: stored energy o Chemical III. Thermodynamics  Thermodynamics: study of energy transformations  Laws o 1 : energy is not created nor destroyed, just transformed o 2 : Entropy, creating waste, mostly heat Concept 8.2 I. Free Energy Change  ∆???? = ∆???? − ????∆????  ???????? ∆???? ???????? ???????????????????????????????? –???????????????????????????????????????????? – Exergonic – exothermic  If ∆???? ???????? ???????????????????????????????? + − ???????????? − ???????????????????????????????????????????? – Endergonic – endothermic  If ∆???? = 0 ????ℎ???????????? ???????? ????????????????????????????????????????  If cells reach equilibrium they die because they have no energy to do work (active transport)  Coupling: catabolic reaction of the ATP (to ADP) take it to the anabolic reaction of the new reaction that NEEDS energy (non-spontaneous) Concept 8.3 I. Adenosine Triphosphate (ATP)  composed of Adenine, a 5C sugar and 3 phosphates  Usually from ATP-> ADP + P i  Sometimes ATP -> AMP + PP i i  P plays as intermediate phosphate while making a reaction because it breaks off from i the ATP and links to the reactant and when the other molecule comes to link with the reactant the phosphate is released and the 2 molecules link  Ca be used to make the protein change in its structure II. The Regeneration of ATP  Creatine: used to build up muscle o Its stored phosphate o Muscle uses immediate energy Concept 8.4  Catalysts: enzymes mostly to reach chemical equilibrium faster however the rae of the enery conversion is the same  Enzymes “push over the edge” of the top of the curve faster.  How do enzymes do it?  Water needs to hit the bond of the molecule with enough force to break it…. Enzyme can grab the 2 reactants forming the bond and make it more accessible (bending it or else)  Enzymes do not affect free energy because the anabolism and catabolism is the same just easier  ATPase – specific to break down of ATP  Induced Fit: the enzyme grips the substrate when it comes into the enzyme o Substrate o Active site o Microenvironment (pH, ionic) o If it has LESS affinity the substrate will get out of there o Enzymes kinetics: how fast can the reaction take place thanks to this enzyme I. Effects of Local Conditions on Enzyme Activity  pH  Temperature o An INCREASE in temperature could affect non-covalent bonds (hydrogen, Van) o A DECREASE in temperature will solidifies the bonds and the “shift” (of enzyme’s shape) necessary for the product happens slower or not at all  There are some ions that are necessary but cell doesn’t like it in high concentrations (Na) o Perturbing substance: aggravating, disrupt normal protein function + o Na would mess up the shame of some enzymes if the concentration of it inside the cell is too high.  Co-factors: substances required by many enzymes for functionality 2+ 2+ 2+ 2+ 2+ o Metal ions: Mg , Mn , Zn , Cu , Fe o Organic based (coenzymes): Vitamins. AMP, ATP, FAD, NAD o Coenzyme: these factors (^) combine with enzyme, typically a “loose” interaction o Prosthetic groups: “strong” interaction that provides structure, thus function 2+  Hemoglobin: heme (enzyme) needs Fe to allow oxygen to bind II. Enzyme inhibition  Direct competition: directly binding to the active site… the inhibitor binds INTO the AS  Indirect (noncompetitive): molecule binds somewhere else and changes the shape o Like poisons  Arsenic: change shape and inhibits the ability to interact III. Evolution of Enzymes  Beta galactoside – lactose  galactose and glues  E. coli - the change of 6 amino acids and now the enzyme has affinity fir sucrose Concept 8.5  Gene regulation: make and destroy the enzyme when needed  Regulate enzyme itself: turn on and off the enzyme if needed I. Allosteric regulation:  Molecule will bind to the enzyme in OTHER than the active site, affecting its activity (non-competitive inhibition)  Most of these enzymes are made of Polypeptide subunits (quarterly - 4 structure)  Interactions are NON-covalent so they can be EASILY reversible o PO cannot be because it’s a COVALENT (so NOT allosteric) 4  Cooperativity: enzyme can bind multiple substrates when 1 binds, and it enhances binding of next o Involves the active site or binding site if NOT an enzyme o Every Hemoglobin (Hb) can bind up to 4 O 2  As you increase the number of O2binding to the Hb the faster the other O 2 will bind II. Feedback Inhibition  The end product of a pathway inhibits the pa pathways\  Threonine produces Isoleucine for protein synthesis, but if it is not needed anymore Isoleucine can bind to the enzyme and stops the production o The cell looks for the concentration of Threonine and if the concentration is high enough then it will make the Isoleucine. o This also happens with ATP and ATPase III. Localization of Enzymes within the cell  Enzyme associated with cytoskeleton all in the same place for the same process  Enzyme placed in organelle  Glycolysis (10 step process) o All the enzymes necessary for glycolysis are right next to the other to facilitate to the other in the cytoskeleton


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