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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 = (k-1 + k2)/k1
[S]=substrate concentration
What is Km? Relate it to Vmax.
Michaelis constant
(k-1 +k2)/k1 (all the rate constants below)
k1 k2
E+S <---> ES ---> E+P
k-1
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?
Non-Covalent
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
Vmax decreased
Km is the same
The graph x intercept is the same
Author
Anonymous
ID
164974
Card Set
Enzymes.txt
Description
enzymes from book
Updated
2012-08-04T18:48:45Z
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