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27 Cards in this Set
- Front
- Back
Catabolism |
Releases energy by oxidation of molecules |
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Anabolism |
Uses energy to synthesize macromolecules that make up the cell |
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Metabolism |
- Catabolism - Glucose --> CO2 + H2O - Energy = released by hydrolysis of ATP - Energy is stored in molecules of ATP - Amino Acids --> Proteins - Anabolism |
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Enzymes |
1. Are biological catalysts 2. Increase rate of reaction by decreasing the activation energy of a reaction 3. Chemical reactions require activation energy |
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Activation Energy |
Energy required to alter reactants so that product can form |
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Proteins: Enzymatic Reaction |
1. Substrate binds to active site 2. Enzyme-substrate complex 3. Products leave 4. Becomes Enzyme again |
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Components of a holoenzyme |
1. Apoenzyme (protein portion), inactive + 2. Cofactor (nonprotein), activator = 3. Holoenzyme (whole enzyme), active |
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Factors Influencing Enzyme Activity |
1. Temperature 2. pH (most active @ 5.0) 3. Substrate concentration |
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Temperature affecting enzyme activity |
- Temperature increases rate of chemical reactions; increases kinetic energy of atoms - Too low temp: reduces freq. with enzyme and reactants collide - Too high temp: enzyme (protein) denatures = looses activity Optimal temp for human (bacteria): 35-37 C Thermophile Archaea: 100-120 C |
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Substate concentration affecting enzyme activity |
- Increase in substrate concentration increases rate of enzymatic reaction - High substrate concentration results in saturation (active site of enzyme is at all times occupied with substrate). - Increase of substrate concentration doesn't increase reaction rate |
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pH affecting enzyme activity |
- Precise pH req. for folding of protein - Too high or low pH denatures enzymes, then = inactive |
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Inhibitors |
1. Competitive inhibitor 2. Noncompetitive 3. Feedback Inhibition |
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Competitive Inhibition |
- Inhibitor competes with substrate for binding to the active site - Increase in substrate concentration reverses inhibition - Some competitive inhibitors bind covalently to amino acid(s) in active site and inactivate enzyme permanently |
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Noncompetitive Inhibitors |
- Do not bind to active site but other regions in enzyme (allosteric inhibition) - Inhibitor binds allosteric site - Cyanide binds iron-containing enzymes |
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Feedback Inhibition |
- Product of metabolic pathway binds and inhibits first enzyme of metabolic pathway - Feedback inhibition prevents the synthesis of excess product |
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Oxidation |
Loss of electrons |
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Reduction |
Gain of electrons |
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Oxidation reaction = ? |
Dehydrogenation reaction |
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NAD+ serves as? |
- Electron (Hydrogen) acceptor - NADH contains more energy |
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Glucose redox reaction |
glucose C6H12O6 + 6O2 ---> 6CO2 + 6 H2O + ATP (cellular energy) |
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ATP (Adenosine Triphosphate) |
- ATP serves as energy currency in cells - Primary energy-harvesting and transferring molecule - Energy released during chemical rxns is harvested and stored in form of ATP, cell uses ATP as energy source to drive biochemical rxn, generated primarily during cellular respiration |
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Phosphorylation |
Enzymes transfer terminal phosphate-group of ATP to other compounds and thereby prime (activate) the molecules for further reactions |
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Dephosphorylation |
Enzymes remove phosphate group from molecule and deactivate molecule |
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Generation of ATP |
1. Substrate level phosphorylation 2. Oxidative phosphorylation 3. Photophosphorylation |
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Substrate level phosphorylation |
ATP is generated when enzyme transfers high-energy Pi from phosphorylated substrate directly to ADP |
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Oxidative Phosphorylation |
- Electrons are transferred from organic substrate to electron carrier (NAD+; FAD+) - Electrons are transferred to terminal electron acceptor oxygen via an electron transport chain (ETC) - Energy released during electron transport is used to generate ATP |
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Photophosphorylation |
- Occurs in photosynthetic cells - Light energy is converted into ATP and NADPH - ATP and NADPH are used to produce organic molecules from CO2 and H2O |