Topic 3 - Enzymes Flashcards
How do enzymes affect the rate of a chemical reaction
Catalysts - increase reaction rate, do not alter equilibrium, just alter the rate at which reach equilibrium
They do this by decreasing the activation energy of the reaction - more molecules have the energy for the reaction to occur
What is activation energy
Difference between substrate and transition state
How do enzyme-substrate complexes form
Binding of enzyme to substrate
Specific religion of enzyme - active site
Binding is stabilised by interaction of amino acid residues surrounding
What are the key features of the active site?
Occupies a small part of the enzyme
Formed by amino acids from different parts of the primary sequence
Clefts or crevices - the folds hide active site to prevent water entry to affect reactions
Complementary shape to substrate - lock key or induced
Substrates are bound to enzymes by multiple weak bonds so products can be released
How do you find V0 (initial rate)
Tangent to the curve
What does the rate of reaction depend on
Substrate concentration
What is the michealis-menten equation
V0 = Vmax [S] / Km + [S]
For curve
What is vmax and how do you find it
The theoretical maximum rate when all enzyme molecules are saturated with substrate
Extrapolate tangent until level out = vmax
Measured in ..M/min
What is the Km and how do you find it
The substrate concentration that gives half the maximal rate of reaction
Low - higher enzyme affinity
Find vmax
1/2 that on V0
Across to curve down to substrate concentration
Measure in mM
1 unit
The amount of enzyme that produces 1 micromol of product per min under standard conditions
Rate of enzyme catalysed reaction proportional to concentration of enzyme
What is the lineweaver-burn plot
V0 = vmax [S] / Km + [S]
Y = Mc delta T
Eg: y intercept = -1/km
Slope = km/vmax
Intercept = 1/vmax
Straight line
What is competitive inhibition?
Binds at active site
Reduce proptiln of enzyme molecules able to bind
Adding enough substrate will overcome effect of inhibitor so no effect on vmax whereas Km increases
What is non competitive inhibitor
Bind sat site other than active site
Causes conformational change
Decreases concentration of functional enzyme
Even if add more substarte will not over crime the effect so Km unaffected and vmax decreases
Km is independent of…
The concentration of enzyme
If twice as much enzyme used, and halves
Vmax double, Km unchanged
Vmax halves, Km unchanged