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Mol and cell ch. 6
| Question | Answer |
|---|---|
| Kenetic energy | associated with movement |
| Potential energy | due to structure or location |
| First law of thermodynamics | law if conservation of energy. Energy canot be created or destroyed. Can be transformed from one type to another |
| Second Law of Thermodynamics | Transfur or transformation of energy from one form to another increases entropy or degree of disorder or system. |
| Entropy energy transformation | Energy transforms involeve an increase in entropy. |
| Entropy | A measure of the disorder that cannot be harnessed to do work. |
| Exergonic reactions | Delta G= the change in free energy. |
| Endergonic reactions | Invest energy in the form of ATPin our bodies. ie: Na/K pump, proton pump |
| Phosphorylation | transferring a phosphate group to some other molecule. The addition of one or more phosphate groups to another molecule makes that molecule of more reactive |
| Kinases | Are a family of enzymes that catalyze the phophorylation of various molecules |
| Phosphatases | Catalyze the removal of phosphate from molecules |
| Catalyst Enzyme Ribozyme | -agent that speeds up the rate of a chemical reaction without being consumed during the reaction -protein catlysts in living cells -RNA molecules with catalytic properties |
| Activation Energy | -initial input of energy to start reaction -allows molecules to get close enough to cause bond rearrangement -Can now achieve transition state where bonds are stretched |
| How do you overcome activation energy? | 2 ways: 1)large amounts of heat (chem lab) 2)using enzymes to lower activation energy |
| How do you lower activation? | 1)straining bonds-in reactants to make it easier to achieve transition state 2)positioning reactants-together to facilitate bonding 3)changing local enivronment |
| Active Site Substrate Enzyme-substrate complex products | -Location where reaction takes place -reactants that bind to active site -formed when enzyme and substrate bind -released at end of reaction |
| Substrate binding | -enzymes have a high degree of specificity -Induced fit-interaction also involves conformational changes |
| Prosthetic Groups Cofactor Coenzyme | -small molecules permanently attched to the enzyme -usually inorganic ion that temporarily binds to enzyme -organic molecule that participates in reaction but left unchanged afterward |
| Saturation | plateau where nearly all active sites occupied by substrate |
| K sub m | substrate concentration at which velocity is half max value |
| Competitive Inhibitor Noncompetitive Inhibitor | -bind to the active site of an enzyme, competing w the substrate -bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective |
| Regulation of enzyme activity is achieved by | 1)switching on or off the genes that encode specific enzymes 2)reulating the activity of existing enzymes by: -phosporylation -allosteric activation of inhibion -feedback inhibition |
| Allosteric regulation | -may either inhibit or stimulate an enzyme's activity -occurs when a regulatory mol. binds to a protein at one site and affects the proteins function at another site |
| Feedback inhibition | -the end product of a metabolic pathway shuts down the pathway -prevents a cell from wasting chem resources by synthesizing more product than is needed |
| Catabolic Pathways | -release energy (exergonic) by breaking down complex molecules into simpler compounds |
| Anabolic pathways | -consume energy (endergonic) to build complex molecules from simpler ones |