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Flashcards in Enzyme Kinetics Deck (7):
1

What is Vmax

Maximum enzyme velocity and it is approached asymptomatically

2

What is Km

Michaelis constant - concentration which rate is exactly half Vmax

3

What is V0

Initial velocity calculated using beer lambert law

4

What is a lineweaver burk plot

Vmax approached asymptomatically as [S] becomes large so reciprocals used to determine
Plot 1/V0 against 1/[S], y intercept is Vmax and x intercept is -1/Km

5

What is the kinetics method

At each concentration of S, measure the absorbance against time during the enzyme reaction and then draw a tangent for t=0 for the initial rate V0

6

What is the affect of competitive inhibition on Vmax and Km

No affect on Vmax because completely outcompeted by geniune substrate. Maximum effect of enzyme unchanged yet Km increased because genuine substrate must compete with inhibitor

7

What is the affect of non-competitive inhibition on Vmax and Km

no effect on Km but decreased Vmax because some active sites denatured by allosteric inhibitor binding