front 1 metalbolic pathway | back 1 a specific molecule that is altered in defined steps, resulting in a product. ( always catalyzed by an enzyme ) |
front 2 catabolic pathway | back 2 release energy by breaking down complex molecules to simpler compounds. |
front 3 anabolic pathways | back 3 consume energy to build complicated molecules from simpler ones. |
front 4 photosynthesis | back 4 decrease in energy |
front 5 cellular respiration | back 5 increase in entropy |
front 6 T | back 6 temperature |
front 7 H | back 7 enthalpy |
front 8 S | back 8 entropy |
front 9 first law of thermodynamics | back 9 energy can be transferred and transformed but never created nor destroyed. |
front 10 second law of thermodynamics | back 10 every energy transfer or transformation increases the entropy of the universe. |
front 11 entropy | back 11 randomness |
front 12 enthalpy | back 12 total heat of a system or internal energy |
front 13 free energy | back 13 a systems energy that can preform work when pressure and temperature are constant. measure of systems instability. |
front 14 spontaneous reaction | back 14 a process that leads to an increase in entropy without an input of energy. |
front 15 exergonic | back 15 loss of free energy, increase of entropy, delta G is negative, temperature is increased, enthalpy is decreased. |
front 16 endergonic | back 16 absorbs free energy, decrease of entropy, delta G is positive, temperature is decreased, enthalpy is increased. |
front 17 ATP | back 17 ribose, 3 nitrogenous bases, adenine, and 3 phosphate groups that is a renewable source. |
front 18 ADP | back 18 made by a hydrolysis reaction where terminal phosphate bond is broken and a molecule of inorganic phosphate is left over. |
front 19 energy coupling | back 19 exergonic process to drive an endergonic one. ATP is responsible for this in cells and acts as an intermediate source of energy that powers cellular work. |
front 20 phosphorylated intermediate | back 20 transfer of a phosphate group from ATP to another molecule and that molecule covalently bonds to a phosphate group. |
front 21 hydrolysis of sucrose | back 21 involves breaking bonds between glucose and fructose and one of the bonds of a water molecule which then forms 2 new bonds |
front 22 activation energy/ free energy of activation | back 22 the energy required to contort the reactant molecules so the bonds can break. pushes reactants to top so they can go “downhill”. |
front 23 transition state | back 23 when molecules have absorbed energy for the bonds to break, the reactants are in an unstable condition. |
front 24 formation of bonds | back 24 release energy |
front 25 breaking of bonds | back 25 absorbs energy |
front 26 catalysis | back 26 speed up enzyme reactions |
front 27 substrate | back 27 the reactant an enzyme acts on |
front 28 enzyme- substrate complex | back 28 an enzyme bonded to a substrate when there are 2 or more substrates. |
front 29 active site | back 29 where enzyme binds to substrate |
front 30 to speed up reactions… | back 30 add more enzyme. |
front 31 activity of enzyme | back 31 effected by pH and temperature |
front 32 cofactors | back 32 non protein helpers for catalytic activity. |
front 33 cofactors of enzymes include… | back 33 metal atoms: zinc, iron, and copper. |
front 34 competitive inhibitors | back 34 reduce productivity of enzymes by blocking substrates from entering active site. |
front 35 noncompetitive inhibitors | back 35 do not directly compete with substrate but instead bind to another part of the enzyme, changing its shape. |
front 36 mutation | back 36 permanent change in genes. |
front 37 allosteric regulation | back 37 any case in which proteins function at one site is affected by the binding of a regulatory molecule to a separate site. This changes an enzymes shape and function of active site. |
front 38 activator | back 38 stabilizes the shape of a functioning active site. |
front 39 inhibitor | back 39 stabilizes the inactive form of an enzyme. |
front 40 cooperactivity | back 40 a substrate molecule binding to one active site in its multi subunit enzyme triggers a shape change in all the subunits. This increases the catalytic activity at the other active sites and amplifies the response of enzymes to substrates. |
front 41 equilibrium | back 41 forward and backward reactions occur at the same rate and delta G equals 0. This preforms NO work and has no net change. |
front 42 disequilibrium | back 42 cells maintain this as open systems. |