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BSC114 Ch8 Notes- Intro to Metabolism

by: Lauren Dutch

BSC114 Ch8 Notes- Intro to Metabolism BSC 114

Marketplace > University of Alabama - Tuscaloosa > Biology > BSC 114 > BSC114 Ch8 Notes Intro to Metabolism
Lauren Dutch
GPA 4.0

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combination of book and lecture notes
The Principles of Biology 1
Dr. Stephenson
Class Notes
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This 6 page Class Notes was uploaded by Lauren Dutch on Saturday September 24, 2016. The Class Notes belongs to BSC 114 at University of Alabama - Tuscaloosa taught by Dr. Stephenson in Fall 2016. Since its upload, it has received 8 views. For similar materials see The Principles of Biology 1 in Biology at University of Alabama - Tuscaloosa.


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Date Created: 09/24/16
Chapter 8 Introduction to Metabolism I. An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics A. Two metabolic pathways 1. Catabolic pathways release energy by breaking down complex molecules into simpler compounds 2. Anabolic pathways consume energy to build complicated molecules from simpler ones 3. Energy released from catabolic pathways can be used to drive anabolic pathways B. Types of energy 1. Chemical energy is energy stored in chemical reactions 2. Kinetic energy is the energy associated with movement 3. Potential energy is the energy possessed due to location or position 4. Thermal energy is energy due to random movement of atoms or molecules and is transferred as heat C. Law of Thermodynamics 1. Thermodynamics are the principles that govern energy transformations 2. First law of thermodynamics states that energy is not created or destroyed but it can be converted between forms 3. Second law of thermodynamics states that every energy transformation increases the entropy of the system  Some energy is inevitably lost as heat to the system II. Why do certain things react or bind? A. Enzymes regulate biochemical reactions B. Enzymes can stop or divert reactions III. The free energy change of a reaction tells us whether or not the reaction occurs spontaneously A. Free energy (G) is the energy in a molecule that is available for conversion to some other form 1. All molecules have an inherent free energy that also includes state and position, e.g. water at the top of the hill has more free energy than water at the bottom of the hill B. Free energy change is the difference between the free energy in 2 molecules or states ΔG = G(final state) – G(initial state) C. Free energy changes for reversible reactions have opposite signs 1. Example: glucose + fructose = sucrose + H2O…. ΔG = +7 kcal/mol sucrose + H2O = glucose + fructose… ΔG = -7 kcal/mol D. Exergonic reactions have a ΔG of less than 0 1. Spontaneous 2. Release energy E. Endergonic reactions have a ΔG of greater than 0 1. Require an input of energy 2. Cannot occur unless energy from some other source is added IV. ATP powers cellular work by coupling exergonic reactions to endergonic reactions A. Cells carry out endergonic reactions by coupling them to exergonic reactions B. Most common exergonic reaction coupled to endergonic reactions is ATP hydrolysis 1. ATP = adenosine triphosphate  Typical nucleotide with a nitrogenous base, a pentose sugar, and 3 phosphates 2. ATP hydrolysis occurs when the terminal phosphate is removed to produce ADP and an inorganic phosphate ATP + H2O = ADP + P … ΔG = -7.3 kcal/mol  ATP is produced from ADP and PO4 … ΔG = +7.3 kcal/mol… but because it is an endergonic reaction, it needs to be coupled with an exergonic reaction 3. Example: When glutamic acid combines with ammonia, the reaction is endergonic, meaning it cannot occur spontaneously. For this reason, ATP hydrolyzes, adds a phosphate molecule to the glutamic acid, ammonia replaces the phosphate, and the overall ΔG of the glutamic acid conversion and ATP hydrolysis is negative, making the entire process exergonic  In this example, the glutamic acid is the phosphorylated intermediate because the phosphate binds to it V. Enzymes speed up metabolic reactions by lowering energy barriers A. Activation energy 1. Starting an exergonic reaction requires overcoming a barrier called the activation energy 2. Energy must be added to break bonds before others are formed B. Enzymes are catalysts that accelerate a chemical reaction without being changed by it 1. Lower the activation energy of a reaction C. Accelerate rates of exergonic reactions by lowering activation energy 1. Cannot catalyze endergonic reactions D. Regulation 1. Enzymes can be regulated- turned off and on, rate of action adjusted 2. All biochemical reactions are exergonic  Some are inherently exergonic  Some are endergonic but couple with an exergonic reaction 3. Most exergonic reactions require a catalyst to overcome activation energy 4. A substrate binds to the active site of an enzyme to create a product  Enzymes are semi-specific for substrates and products 5. Competitive inhibitors are molecules that are similar in shape to the substrate and bind to the active site, blocking the substrate from binding to the active site 6. Allosteric regulation is noncompetitive regulation in which a molecule binds to a site other than the active site and inhibits or promotes catalysis  Can be activating or inhibiting  Molecule binds to allosteric site, not active site  Proteins exist in 2 or more alternative, slightly different shapes or conformations - When a molecule binds to the allosteric site, it produces a change in conformation which changes the shape of the active site  Cooperativity occurs in enzymes with more than one subunit where the binding of one substrate increases the stability of the active conformation and allows additional substrates to combine more readily - The allosteric activator stabilizes active form 7. Feedback inhibition occurs when a downstream product inhibits an earlier step in the biochemical pathway  End product binds to allosteric site on first enzyme and changes the active site  Not competitive because the end product is not similar enough in shape to the substrate to fit in the active site E. Structures 1. Enzymes are usually proteins  Globular proteins  Substrates fit tightly into the active site, the cavity in which the reaction occurs - Substrates held in active site by hydrogen bonds, Van der Waals reactions, and ionic bonds  Induced fit occurs when the protein tightens around the substrate after bonding 2. Cofactors are non-protein molecules required for catalysis  Metal ions, e.g. zine  Coenzymes are organic molecules that act as cofactors, e.g. vitamins F. Mechanisms 1. Catalytic cycle  Substrate binds in active site  Enzyme undergoes slight change in 3D structure (induced fit)  Chemical reaction occurs  Products are released 2. Enzyme lower activation energy by:  Acting as a template to bring reactive groups into close proximity  Straining bonds and stabilizing transition states  Providing a microenvironment for the chemical reaction  Participating directly in the reaction 3. Each enzyme has an optimal temperature, pH, salt concentration, etc.  Stability of protein folding (too high of a temperature will negatively impact folding)  Stability of weak bonds in active site  Thermal motion of substrate(s)


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