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30 Cards in this Set
- Front
- Back
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Metabolism |
•Living Organisms must be able to take energy & raw material in the environment & convert it to energy/material that the organism can use •Chemical reaction occurs w/in an organism |
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Catabolism |
•Breaks Down large molecules into smaller ones •Release Energy (exergonic) •Energy coupled to other reactions (e.g. ATP production, synthesis of organic material) •Energy released as heat |
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Anabolism |
•Energy (endergonic) to make large molecules from smaller ones •Couple High energy reactions to anabolic reactions to provide the required energy |
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Oxidation |
•Loss Of electrons by a molecule, ion or atom •Gain Of oxygen atoms or loss of hydrogen atoms by a molecule |
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Reduction |
•Gain of electrons by a molecule, ion, or atom •Loss Of oxygen atoms or gain of hydrogen atoms by a molecule |
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Enzymes |
Proteins That catalyze reactions w/out being consumed |
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Enzyme Classification: Hydrolase |
Catabolize Molecules by adding water in a decomposition reaction |
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Enzyme Classification: Isomerase |
Rearrange Atoms within the molecule but do not add or remove anything |
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Enzyme Classification: Ligase |
Join two or more molecules together |
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Enzyme Classification: Lyases |
Split large molecules into smaller ones with using water |
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Enzyme Classification: Oxidoreductase |
Remove Or add electrons to substrates |
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Enzyme Classification: Transferase |
Transfer Functional groups between molecules |
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Enzymes: Cofactors |
•Non-protein molecules that aid in the catalytic activity of enzymes •Inorganic molecules (e.g. Iron, Magnesium, Zinc) |
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Enzymes: Coenzymes |
•Organic molecules (Vitamins) |
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Apoenzyme |
A protein that requires cofactors to function, but is not bound to them |
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Holoenzyme |
A apoenzyme w/ cofactors attached & is active |
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Enzyme Activity |
Catalyze Reactions by lowering the activation energy |
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Induced Fit Model |
•Substrate Initially fits loosely to the enzyme •Resulting Compound is the enzyme-substrate complex •Binding Of the substrate induces to change its shape to conform the substrate |
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Enzyme Kinetics |
Rate of enzyme reactions |
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Enzyme Kinetics: Vmax |
Maximum Rate achieved by the system |
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Enzyme Kinetics: Km |
Substrate Concentration at ½ Vmax -a measure of the affinity of the substrate to the enzyme -inverselycorrelated to the affinity |
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Enzyme Inhibitors |
•Activity can be blocked by the binding inhibitors Two Types of Enzyme inhibitors •Competitive Inhibitor •Noncompetitive inhibitors |
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Competitive Inhibitor |
•Binds to the active site of the enzyme •Increasing The concentration of substrate can overcome competitive inhibition |
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Non-Competitive Inhibitor |
•(Allosteric) binds to enzyme on site other than the active site •Conformational change in enzyme & renders it unable to bind to the substrate |
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Carbohydrate Metabolism |
•Glucose Is the primary source of energy for most organisms •The First step is glycolysis |
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Glycolysis |
•Breakdown Of glucose •Does Not require oxygen |
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Pyruvate Decarboxylation |
•1 carbon is removed from pyruvate •Molecule of Coenzyme A binds to the 2 carbon molecule •Acetyl CoA 1 |
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Citric Acid Cycle |
•AKA Tricarboxylic acid cycle/ the Krebs cycle •Acetyl CoA (2C) joins the Citric acid cycle by binding to the 4 carbon oxaloacetate •3 NADH/ FADH2/ 1 GTP |
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1 possible arrangement of Electron Transport Chain |
•Mitochondrian Eukaryotes 2 molecules energy •6:2:2 Glycolysis •2 Pyruvate/ 1 Acetyl CoA •1 glucose 2 Acetyl CoA |
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Fermentation |
•Cannot Undergo oxidative phosphorylation under anaerobic conditions •Cells Require constant source of NAD+ •Pathways provide cells regenerate NAD+ |
