chapter 8 Flashcards
catabolic process
energy yielded
anabolic process
energy used for cellular work
what is required to synthesize ATP
ADP and phosphate
what is ATP used for
most cellular work that requires energy
what is chemical potential energy stored in
ATP
what do enzymes do?
speed up a metabolic reaction by lowering the energy barrier
how are enzymes and catalysts similar
an enzyme acts as a catalyst, as it speeds up a reaction without being consumed within it
How can the activation energy be found on an energy graph
From the height of the reactants to the top of the highest point curve
What do enzymes not change on an energy graph?
delta G
changing an endogonic to an endergonic reaction
what indicates spontaneity
- delta G
why is it inappropriate to speed up these reactions by applying heat
heat denatures the protein and kills cells and speeds up reactions
substrate
reactants that enzymes react on
why are enzymes able to recognize molecular differences
enzymes have specific shapes that dictate their unique functions
active site
where an enzyme binds to its substrate
what do R-groups of amino acids interact with on substrates
chemical groups on the active active site of the substrate
induced fit
enzyme changing shapes slightly to the active site fits more snug on the substrate
induced fit increases what ability of an enzyme
catalytic
how efficient an enzyme is depends on :
temp
pH
specific chemicals
what is the optimal pH for each enzyme
most in between 6-8 pH
what is the optimal temperature for each enzyme
human enzyme– 35-40 C
thermophilic enzyme – 70-80 C
why do reaction rates drop quickly at temps greater than the optimal temperaure
higher temps will disrupt the hydrogen, ionic, and hydrophobic interactions that stabilize the active state
how can you determine which direction a reaction is going
positive or negative delta G
how does the active site environment impact a reaction
favorable micro-environment (can be more acidic than a neutral cell)
cofactors
some enzymes require a non-protein molecules to aid catalytic activity (binds either loosely or tightly)
what are two types of cofactors
organic molecules
inorganic molecules
what are examples of inorganic ions
magnesium
zinc
iron
copper
what are examples of organic molecules
(aka co-enzyme)
most vitamins
NAD+
irreversible inhibitions
when inhibitors bind covalently to the enzyme and block activity
reversible inhibition
when inhibitors bind to enzyme via weak interaction and block activity
what are the two types of reversible inhibition
competitive inhibitors
noncompetitive inhibitors
competitive inhibitors
block substrates from binding to the active site
noncompetitive inhibitors
impede enzyme activity by binding to another part of the enzyme. changes shape so active site is less catalytic