AP Biology - Energy & Enzymes Flashcards
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9783160040 | catabolic pathways | Series of reactions that release energy by breaking down complex molecules into simpler compounds. | ![]() | 0 |
9783160041 | anabolic pathways | Series of reactions that consume energy to build complicated molecules from simpler ones. | ![]() | 1 |
9783160045 | potential energy | Stored energy. | ![]() | 2 |
9783160050 | endergonic reaction | Reaction that absorbs free energy from its surroundings. | ![]() | 3 |
9783160051 | exergonic reaction | Reaction that proceeds with a net release of free energy. | ![]() | 4 |
9783160054 | phosphorylation | The metabolic process of introducing a phosphate group into an organic molecule. | ![]() | 5 |
9783160056 | enzyme | Protein that speeds up reactions. Typically end in "ase" (ex. Peroxidase, Lipase) | ![]() | 6 |
9783160057 | activation energy | The amount of energy needed to push the reactants over an energy barrier. | ![]() | 7 |
9783160058 | enzyme-substrate complex | When an enzyme binds to its substrate, it forms: | ![]() | 8 |
9783160059 | active site | A pocket or groove on the surface of the enzyme where a substrate can bind. | ![]() | 9 |
9783160060 | induced fit model | States that the enzyme and substrate undergo conformational changes to interact fully with one another (as opposed to "Lock & Key" | ![]() | 10 |
9783160061 | cofactor | Inorganic metal ion helpers that may be bound tightly to the enzyme as a permanent resident, or may bind loosely and reversibly along with the substrate. Iron is an example. | ![]() | 11 |
9783160062 | coenzyme | Non-protein Organic helpers that may be bound tightly to the enzyme as a permanent resident, or may bind loosely and reversibly along with the substrate. Most vitamins function this way. | ![]() | 12 |
9783160065 | feedback inhibition/negative feedback | A metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway. | ![]() | 13 |
9783160066 | saturated enzyme | Describes an enzyme's maximum activity when every active site is being used. | 14 | |
9783160067 | Chemical Energy | Potential energy trapped in molecular bonds. | ![]() | 15 |
9783160072 | Competitive inhibition | substance that resembles the normal substrate competes with the substrate for the active site which can be overcome by adding more substrate | ![]() | 16 |
9783160073 | Noncompetitive inhibitor | a chemical that binds to an enzyme but not in the active site. This chemical will change the shape of the enzyme so substrate can no longer fit active site | ![]() | 17 |
9783160074 | substrate | the substance an enzyme catalyzes, changes. | ![]() | 18 |
9783160075 | exothermic reaction | a chemical reaction where energy is given off, so that the products have less energy than the reactants. | ![]() | 19 |
9783160076 | endothermic reaction | a chemical reaction where energy is taken in, so that the products have more energy than the reactants. | ![]() | 20 |
9783160086 | Denature | Characteristic of proteins; a change in shape that stops the protein from functioning. | ![]() | 21 |
9783160087 | Allosteric | __________ regulation of enzyme occurs when a molecule binds to an enzyme changing the protein's shape | ![]() | 22 |
9783160097 | Protein Kinases | enzymes that reversibly activate or inactivate other proteins by adding phosphate groups to (phosphorylating) them | 23 | |
9783160098 | pH | After looking at the graph the enzyme activity of the the three different enzymes is being regulated by what variable | ![]() | 24 |
9783160099 | Temperature | After looking at the shape of graph the enzyme activity of this enzymes is being regulated by what variable: | ![]() | 25 |
9783160101 | Metabolism | The totality of an organism's chemical reaction | 26 |