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Biology Chapter 8
Introduction to Metabolism
| Term | Definition |
|---|---|
| Metabolism | Sum total of all energy exchanges that occur in cells |
| Metabolic Pathways | Sequence of chemical reactions(steps) each catalyzed by a particular enzyme that has a very specific shape |
| Intermediate Products(I.P.) | The products of one step in the metabolic pathway, they become the reactants for the next step |
| Final or End Product | The last product produced in a metabolic pathway |
| Anabolic Pathway | "Build up"; Consume or store energy to build larger, more complex molecules from simpler ones; can be called biosynthetic pathways. Bonds will form and energy stored(absorbed) from surroundings. "Uphill Pathways". Ex; photosynthesis |
| Catabolic Pathway | "Break down"; Release energy by breaking down more complex molecules to simpler ones. "Downwhill Pathways". Bonds break; energy released. Ex: Aerobic cellular respiration |
| Energy | The capacity to do work or to cause change |
| Forms of Energy | 1. Kinetic Energy.. Heat or Thermal Energy.. 2. Potential Energy.. Chemical Energy.. 3. Free Energy |
| Kinetic Energy | The energy of motion(movement) |
| Heat or Thermal Energy | Kinetic energy associated with the random movement of atoms or molecules. As temperature increases by the addition of heat, there is an increase in kinetic energy(K.E) |
| Potential Energy | Energy of position; energy that matter has because of its location or structure. "Has the potential to do work" |
| Chemical Energy | "Bond energy". The potential energy that is available for release in a chemical reaction. The energy that is stored in the bonds between molecules |
| Free Energy | Is the portion of a system's total energy that is available to do work. Symbolized "G" (Gibb). (Delta)/\G = change in free energy |
| Delta G Equation | Delta G = G(of final product) - G(of initial product) |
| Laws of Thermodynamics | Energy rules |
| First Law of Thermodynamics(Quantity of Energy) | Called the Principle of Conservation of Energy. Energy cannot be created or destroyed, it can be transferred and transformed. The amount of energy in the universe is constant. |
| Second Law of Thermodynamics(Quality of Energy) | Every energy transfer or transformation (changing forms) increases the entropy of a system |
| Entropy | Measure of disorder. "Chaos, randomness". Adding energy reduces entropy and reducing energy increases entropy |
| Exergonic Reactions | Proceeds with a a net release of free energy; spontaneous reactions(likelihood of it happening is high). "Downhill reactions". Products have less free energy than the reactants. Delta G is negative(less than zero)because energy was lost |
| Endergonic Reactions | A reaction that absorbs free energy from its surroundings; non-spontaneous reactions(likelihood of it happening is low). "Uphill reactions". Products have more free energy than reactants. Delta G is positive or more than zero because gain of energy |
| Energy Coupling | The use of an exergonic process to drive(push) an endergonic one. ATP is used for energy coupling |
| ATP(Adenosine Triphosphate) | Energy currency of cells. Energy form that cells do work with. |
| Functions of ATP | Responsible for mediating most energy coupling in cells; in most cases acts as the immediate source of energy that powers cellular work. |
| How does ATP Power Things | The exergonic(downhill) process of ATP Hydrolysis drives(pushes) the endergonic(uphill) reactions by transfer of a phosphate group to specific reactants. The bonds between the second and last phosphate group contains 7 calories of energy |
| Structure of ATP | A nucleotide that has been phosphorylated. Contains the pentose sugar ribose, the nitrogenous base adenine which is a purine, and and a chain of three phosphate groups bonded to it. |
| Inorganic Phosphate Group | When a phosphate group is not attached to an organic compound. Symbolized as Pi |
| Adensosine Diphosphate(ADP) | An ATP with only two phosphate groups |
| Adenosine Monphosphate(AMP) | An ATP molecule with only one phosphate group |
| Pyrophosphate Bonds | "High energy" bonds |
| Pyrophosphate Bond Phosphoryation | The addition of a Pi to an ADP to form a ATP by ADP bonding with a Pi group by a pyrophosphate bond(Endergonic) |
| Pyrophosphate Bond Hydrolysis | The release of a Pi from ATP to form ADP breaking pyrophosphate bond(Exergonic) |
| Phosphorylated Intermediate | Formed from ATP transferring a phosphate group to a specific reactant, makes the reactant more reactive(less stable), raises its energy level |
| ATP Exergonic Reaction | ATP ----->(Hydrolysis)----> ADP + Pi + release energy. Powers any cell activity where energy is required |
| ATP Endergonic Reaction | ADP + Pi + abosrb energy --->(Phosphorylation)---> ATP |
| Enzymes | A macromolecule, usually a protein with very specific globular 3-D shape. Functions as biological catalyst and lowers the amount of activation energy(EA) required |
| Catalyst | A chemical agent that speeds up a reaction without being consumed by the reaction and can be used over and over again |
| Activation Energy Barrier(EA - Energy of Activation) | Amount of energy needed to push the reactants to the top of an energy barrier(combine the reactants), or uphill, so the downhill part of the reaction can occur(products formed). ***Thermodynamic Barrier |
| Transition State | The moment in a reaction when the reactants are changing into products |
| Enzyme Structure | Enzymes are globular proteins that have a highly folded very specific 3-D shape of a protein, at least the tertiary level. |
| Active Site | Typically a pocket or groove on the surface of the enzyme where catalysis occurs |
| Substrate | The reactant of an enzyme catalyzed reaction |
| Enzyme-Substrate Complex | Formed when a enzyme binds to its substrate(s) |
| Induced Fit | The enzyme changes shape slightly due to interactions between the substrates and the enzymes. Produces optimum fit |
| Factors That Effect Enzyme Activity | 1. Temperature.. 2. pH.. 3. Cofactors(inorganic).. 4. Coenzymes(organic).. 5. Inhitors.. A. Competitive inhibitors.. B. Non-Competitive inhibitors.. 6. Limiting Factors.. A. Substrate Concentration.. B. Enzyme Concentration.. C. Saturation |
| Temperature Effect on Enzyme Activity | Increase in temperature breaks h-bonds that hold together any protein and denature it. Decrease in temperature does not denature the protein but slows down molecular activity collisions or makes molecules move slower. |
| pH Effect on Enzyme Activity | An increase or decrease in pH can break H-bonds and break R-group interactions denaturing the protein. Buffers maintain pH |
| Cofactors | Any non protein molecule or ion that is required for the proper functioning of an enzyme. Small and attaches to enzyme or near the active site. "Assist in functions. "Ex: Fe+2, Mg+2 |
| Coenzymes | Small, organic molecule serving as a cofactor. Ex: NAD and FAD(carry H+ and electrons), CoA(Coenzyme), CoQ, and cytochromes(function in electron transport). Most are vitamins - B-Complex |
| Inhibitors | Anything that reduces the activity of enzymes. Some are reversible, others are irreversible. Two types... A. Competitive inhibitors.. B. Non-Competitive inhibitors |
| Competitive Inhibitors | Objects that reduce the activity of enzymes by entering enzyme active site and thereby blocking substrates from entering active sites. The components that will win the competition are the ones that there are more of. |
| Non-Competitive Inhibitors | Do not directly compete with the substrate to bind to the enzyme at active site. It binds to another part of the enzyme and denatures it. This denaturation can be irreversible if inhibitor covalently bonds with enzyme, but otherwise is usually reversible |
| Limiting Factors | The factor in the shortest supply determines the overall rate of the reaction |
| Substrate Concentration | Low amounts of substrate concentration can limit the rate of the reaction |
| Enzyme Concentration | Low amounts of the enzyme concentration can limit the rate of the reaction |
| Enzyme Saturation | Every enzyme is occupied |
| Regulation of Enzymes | Enzymes need feedback to know whether to do more or less work. |
| Allosteric Regulation | Used to describe any case in which a protein's function at one site(active site) is affected by the binding of a regulatory molecule at its allosteric(other) site |
| Activators | Stabilizes the shape of the enzyme so that the acive site is functional or active |
| Inhibitors | Stabilizes the shape of the enzyme so that the active site is nonfunctional or inactive |
| Feedback Inhibition | A metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway |
| Oxidation | Loss of electrons and H+ |
| Reduction | Gain of electrons and H+ |
| Oxidizing Agent | The substance that causes another molecules oxidation(the one who was reduced) |
| Reducing Agent | The substance that causes another molecules reduction(the one who was oxidized) |
Created by:
TimBiology1
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