AP Biology
For test on October 23
Terms : Hide Images
| 507490481 | Metabolism | Totality of an organism's chemical reactions | |
| 507490482 | Catabolic | Reactions release energy; break down molecules; i.e. cellular respiration | |
| 507490483 | Anabolic | Reactions consume energy; build up larger molecules; considered "uphill"; i.e. photosynthesis | |
| 507490484 | Enzymes | Required to catalyze both catabolic and anabolic reactions | |
| 507490485 | Kinetic energy | Associated with relative motion of objects | |
| 507490486 | Potential energy | Because of location or structure | |
| 507490487 | Free Energy | (∆G) Portion of a system's energy that can perform work when temperature and pressure are uniform throughout the system | |
| 507490488 | Exergonic | Cellular respiration is an ... reaction. | |
| 507490489 | Endergonic | Photosynthesis is an ... reaction. | |
| 507490490 | Electromagnetic | In photosynthesis, plants capture ... energy from the sun to fuel the reaction; light is converted then to chemical energy | |
| 507490491 | Exergonic | Reaction type: Spontaneous | |
| 507490492 | Exergonic | Reaction type: -∆G | |
| 507490493 | Exergonic | Reaction type: Less stable | |
| 507490494 | Exergonic | Reaction type: More free energy in reactants | |
| 507490495 | Endergonic | Reaction type: Not spontaneous | |
| 507490496 | Endergonic | Reaction type: +∆G | |
| 507490497 | Endergonic | Reaction type: More stable | |
| 507490498 | Endergonic | Reaction type: Less free energy in reactants | |
| 507490499 | Chemical work | Synthesis of polymers from monomers | |
| 507490500 | Transport work | Movement across a membrane against the concentration gradient | |
| 507490501 | Mechanical work | Physical movement of objects/items within the body (i.e. chromosomes during cell reproduction) | |
| 507490502 | ATP structure | Three phosphate groups connected to a ribose connected to an adenine | |
| 507490503 | Phosphate | The last ... group in ATP is most likely to be broken off to produce energy | |
| 507490504 | Hydrolysis | Breaking down complex molecules by the chemical addition of water; process through which the final phosphate group is broken off from the ATP | |
| 507490505 | Adenosine triphosphate | Full name of ATP | |
| 507490506 | released | ATP: When the terminal phosphate bond is broken, a molecule of inorganic phosphate is formed and energy is ... | |
| 507490507 | Negative | Is ∆G positive or negative in the following reaction? ATP --> ADP + Pi | |
| 507490508 | Exergonic | Reaction type for ATP --> ADP + Pi | |
| 507490509 | Energy coupling | Ability to use energy released by ATP hydrolysis directly to drive reactions that are, by themselves, endergonic; use of an exergonic reaction to drive an endergonic one | |
| 507490510 | phosphorylated | In many cellular reactions, a phosphate group is transferred from ATP to some other molecule in order to make the second molecule less stable. The second molecule is said to be ... | |
| 507490511 | Catalyst | Chemical agent that speeds up a reaction without being consumed by the reaction | |
| 507490512 | Activation energy | Energy required to contort the reactant molecules so the bonds can break; the initial amount of energy needed to start the reaction | |
| 507490513 | lowers | An enzyme ... the activation energy barrier enabling the reactants to absorb enough energy to reach the transition state | |
| 507490514 | not affected | The ∆G value of a reaction is ... by the introduction of an enzyme. | |
| 507490515 | Enzyme | Macromolecule that acts as a catalyst | |
| 507490516 | Substrate | Reactant that an enzyme acts on | |
| 507490517 | Active site | Restricted region (pocket or groove) of the enzyme molecule that actually binds to the substrate | |
| 507490518 | Products | New molecules that exit the enzyme after the reaction | |
| 507490519 | First law of thermodynamics | Energy is neither created nor destroyed; it is only transferred from one form to another. | |
| 507490520 | Second law of thermodynamics | An energy transfer is never 100% efficient ('Law of entropy'); For all the ecologists out there: this law gives rise to the 10% rule :) | |
| 507490521 | Induced fit | Amino acids that form the active site change shape slightly to better hold the substrate snuggly; enzyme will wrap around the substrate | |
| 507490522 | Enzyme specificity | Enzyme only bonds to one substrate due to the shape of active site | |
| 507490523 | orient | Enzyme mechanism to lower activation energy: For two or more reactants, the enzyme can be shaped appropriately to ... the molecules to allow a reaction to occur. | |
| 507490524 | bonds | Enzyme mechanism to lower activation energy: The enzyme can stretch and bend the substrates to help break key ... that must be broken. | |
| 507490525 | micro-site | Enzyme mechanism to lower activation energy: The enzyme can provide a ... is more conducive to the reaction. | |
| 507490526 | participation | Enzyme mechanism to lower activation energy: Direct ... of the active site in the reaction. | |
| 507490527 | Concentration | Affects rate of enzyme action because more substrate molecules, the more frequently they access the active sites of the enzyme | |
| 507490528 | denature | If the pH and temperature are not correct, protein-based enzymes can ... | |
| 507490529 | Cofactors | Require nonprotein helpers for activity in enzyme | |
| 507490530 | Coenzymes | Organic cofactor molecules | |
| 507490531 | Competitive inhibitors | Some reversible inhibitors resemble the normal substrate molecule and compete for active site; they reduce productivity of enzyme by blocking active sites; easy to overcome by increasing substrate concentration | |
| 507490532 | Non-competitive inhibitors | They do not directly compete with substrate; they bind to another part of the enzyme that causes the enzyme to change shape in such a way that the active site is less effective | |
| 507490533 | Allosteric regulation | Protein's function at one site is affected by the binding of a regulatory molecule to a separate site | |
| 507490534 | Allosteric activator | Binds to the enzyme and induces the enzyme's active form | |
| 507490535 | Allosteric inhibitor | Substance that binds to an allosteric site on an enzyme and stabilizes the inactive form of the enzyme | |
| 507490536 | Cooperativity | A kind of allosteric regulation whereby a shape change in one subunit of a protein caused by substrate binding is transmitted to all the others, facilitating binding of subsequent substrate molecules | |
| 507490537 | Feedback inhibition | A method of metabolic control in which the end product of a metabolic pathway acts as an inhibitor of an enzyme within that pathway. |
