Lecture 2 Flashcards
(115 cards)
What are enzymes
biological catalysts
- all proteins except some RNAHo
By how much can a catalyst increase the rate of a reation
10^20
Rate of reaction depends on what
activation energy (delta G)
What is activation energy
amount of energy required to start the rxn
- puts reactant in same transition state
- lower for enzyme catalyzed rxn
active site in enzyme catalyzed rxn
small portion of enzyme surface where substrate is bound
substrate in enzyme catalyzed reaction
reactant binds to active site of enzyme
enzyme substrate complex
held together by hydrogen bonding, electrostatic attractions, and van der waal interactions
Lock and key model
substrate binds to portion of enzyme w complementary shape
Induced fit model
binding of substrate induced change in conformation of enzyme that results in complementary fit
How do enzymes work
- concentration of enyzme usually lower than concentration of substrate
- rate of catalyzed rxn depends on substrate concentration
when are enzymes working at max rate
at saturation when all enzymes are bound to the substrate
What factors affect rate of reaction
- temp
- pH
- enzyme concentration
- substrate concentration
- presence of controlling molecules
how doe pH affect rate or rxn
- every enzyme is most active at particular pH
- pH influences ionization of functional group
How does temp affect rate of rxn
- every enzyme has optimal temp
- increase temp = increase rate of rxn
what happens to enzymes @ high temps
noncovalent bonds begin to break which affects enzyme structure and function
at what temp do noncovalent bonds begin to break
50 - 55º c
enzyme concentration and rate of rxn
- directly proportional
- if enough substrate, enzymes will double with wil cause Vm to double
substrate concentration and rate of rxn
rate of enzyme depends on substrate concentration
- @ low substrate concentration, adding more substrate increases rate f reaction
- constant rate (vmax) is reached when enzyme is completely saturates with substrate
the higher the Km value..
the lower the affinity for substrate
the lower the Km value…
the higher the affinity for substrate
Reversible inhibitor
substance that binds to enzyme to inhibit it, but can be released
competitive inhibitor
- reversible
- binds to active site and blocks access by substrate
noncompetitive inhibitor
binds to site other than active site, inhibits enzyme by chaging conformation
irreversible inhibitor
substance that causes inhibition that cannot be reversed