Automatically remove your image background. Try it now!
author "Joshua Ellis"
What is the Michaelis -Menten Equation
Vo= initial velocity
Vmax= maximal velocity
Km= Michaelis constant = (k-1 + k2)/k1
What is Km? Relate it to Vmax.
(k-1 +k2)/k1 (all the rate constants below)
E+S <---> ES ---> E+P
Does not change with concentration of enzyme. Basically equal to reaction velocity = 1/2 Vmax
What does a low and high Michaelis constant mean?
Small Km = high affinity of the enzyme for substrate. (low concentration of substrate need to half saturate the enzyme--reach v=1/2vmax)
Large Km = low affinity. Cuz a high concentration is required.
What is the relationship to enzyme concentration and velocity of reaction?
ALWAYS directly proportional. If you half [E] then the Vo and Vmax will also be halved
How can you determine the order of the reaction?
When [S] is much less than Km velocity is proportional to [S]-----FIRST ORDER
When [S] is much greater than Km velocity is constant and equal to Vmax (independent of [S])----- ZERO ORDER
How do you make the Lineweaver-Burke Plot? What does it tell you? What is the equation?
Its the reciprocal of the Michaelis Menten equation
It can tell you the Km and Vmax (as x and y intercepts)
1/vo= Km/(Vmax[S]) + 1/Vmax
Reversible inhibitors have what type of bond?
What is competitive inhibition? What is the effects on Vmax, Km, and Lineweaver Burke Plot
Binds to active site
Vmax is the same
Increased Km because need more [S]
Graph y intersect is same but x intercept is increased (obvious slope change)
What is non-competitive inhibition? What is the effects on Vmax, Km, and Lineweaver Burke Plot
non active site binding
Km is the same
The graph x intercept is the same
enzymes from book