Enzymes.txt
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 author "Joshua Ellis"
 tags "HUCM"
 description ""
 fileName "Enzymes"
 freezingBlueDBID 1.0
 What is the Michaelis Menten Equation
 Vo= Vmax[S]/(Km+[S]

Vo= initial velocity
 Vmax= maximal velocity
 Km= Michaelis constant = (k1 + k2)/k1
 [S]=substrate concentration

What is Km? Relate it to Vmax.
 Michaelis constant
 (k1 +k2)/k1 (all the rate constants below)
 k1 k2
 E+S <> ES > E+P
 k1
 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 enzymereach 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 LineweaverBurke 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?
NonCovalent

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 noncompetitive inhibition? What is the effects on Vmax, Km, and Lineweaver Burke Plot
non active site binding
 Vmax decreased
 Km is the same
The graph x intercept is the same