AP BIO Unit 2: Enzymes

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AP AP BIO Mindmap am AP BIO Unit 2: Enzymes, erstellt von Meredith W am 30/09/2017.
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Zusammenfassung der Ressource

AP BIO Unit 2: Enzymes
  1. The Energy of Life
    1. metabolic pathways
      1. metabolism: all of the chemical reactions that take place within an organism
      2. forms of energy
        1. kinetic

          Anmerkungen:

          • energy not in motion
          1. thermal energy: heat

            Anmerkungen:

            • the combination of all the movement of the particles in a substance
            1. the energy most difficult to use for doing work
          2. potential

            Anmerkungen:

            • the energy of motion
            1. chemical energy

              Anmerkungen:

              • the potential energy stored within the bonds (chemical makeup) of a substance-- the potential of energy available for release in a chemical reaction
          3. The laws of energy transformation
            1. 1st law of thermodynamics

              Anmerkungen:

              • energy cannot be created or destroyed, only transferred or transformed
              1. 2nd law of thermodynamics

                Anmerkungen:

                • every energy transfer or transformation increases the entropy of the universe
              2. biological order and disorder
                1. even when the entropy of a certain system is reduced, the overall energy of the universe may be increased due to the production of heat energy
              3. the free energy changes of a reaction tell us whether or not it occurs spontaneously
                1. free energy change (ΔG), stability, and equilibrium
                  1. ΔG= energy of reactants - energy of products
                    1. reactions with a negative ΔG are spontaneous, exergonic
                      1. reactions with a positive ΔG are non-spontaneous, endergonic
                      2. things are naturally moving towards equilibrium?
                      3. free energy and metabolism
                      4. ATP powers cellular work by coupling exergonic reactions to endergonic reactions
                        1. the structure and hydrolysis of atp
                          1. ATP= adenosine TRI phosphate
                            1. tends to lose one phosphate group, becomes ADP: adenosine DIphosphate

                              Anmerkungen:

                              • phosphate groups tend to detach because of their negative charge (negatives next to each other--> like charges repel)
                          2. how the hydrolysis of ATP performs work
                            1. the regeneration of ATP
                              1. from ADP?
                            2. Enzymes speed up metabolic reactions by lowering energy barriers
                              1. the activation energy barrier
                                1. EsubA: activation energy
                                  1. the input energy required for an endergonic reaction to begin
                                  2. how enzymes speed up reactions
                                    1. substrate specificity of enzymes
                                      1. structure of enzymes specific to fit enzymes: proteins (3, 4 structures)

                                        Anmerkungen:

                                        • some enzymes are nucleic acids
                                        1. induced fit

                                          Anmerkungen:

                                          • when a substrate enters an enzyme's active site, the enzyme's structure changes slightly to grip more tightly around the substrate
                                          1. substrate: what is catalyzed by the enzyme
                                            1. enzyme: a biological catalyst
                                            2. catalysis in an enzyme's active site
                                              1. substrate enters an enzyme's active site, it catalyzed
                                              2. effects of local conditions on enzyme activity
                                                1. effects of temperature and pH
                                                  1. enzyme has an optimal pH and temp where catalysis is most efficient
                                                    1. temp
                                                      1. temp: below optimal point, as temp increases efficiency increases...

                                                        Anmerkungen:

                                                        • temp= average heat energy, heat energy= average motion of particles in a substance... more temp=more motion of molecules= substrates will enter enzymes faster
                                                        1. past optimal point, as temp increases efficiency decreases

                                                          Anmerkungen:

                                                          • too much heat (too much motion of particles) can cause protein denaturation-- weak bonds holding together a protein's 3°/4° structures (what creates its function) are broken
                                                        2. pH
                                                          1. either more acidic or more basic than optimal point= less efficient

                                                            Anmerkungen:

                                                            • can cause protein denaturation... 
                                                            • ex: enzymes in stomach made specifically to function at pH of 2 (pH of stomach acid)... other enzymes would denature in that state
                                                      2. cofactors

                                                        Anmerkungen:

                                                        • molecules needed for/that aid in an enzyme's catalysis
                                                        1. conenzymes: organic (molecule) cofactors
                                                        2. enzyme inhibitors

                                                          Anmerkungen:

                                                          • needed for when enough of end product has been catalyzed
                                                          1. competitive inhibitors

                                                            Anmerkungen:

                                                            • fit directly into an enzyme's active site, blocking substrates from doing so
                                                            1. noncompetitive inhibitors

                                                              Anmerkungen:

                                                              • fit into a site on the enzyme other than the active site, change the enzyme's structure so the enzyme will no longer fit
                                                          2. the evolution of enzymes
                                                          3. regulation of enzyme activity helps control metabolism
                                                            1. allosteric regulation of enzymes

                                                              Anmerkungen:

                                                              • can be both 
                                                              1. allosteric site

                                                                Anmerkungen:

                                                                • site on an enzyme where allosteric regulators attach-- not the active site
                                                              2. allosteric activators and inhibitors
                                                                1. feedback inhibition
                                                                2. specific localization of enzymes within the cell

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