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45 Cards in this Set

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definition. the maximum velocity of reaction that a particular amount of enzymes could possibly give
Vmax
is vmax extensive or intensive?
EXtensive. The more the enzyme the more higher the vmax
is Km extensive or intensive
INtensive. enzyme concentration does not change Km
what is inversely related to the binding affinity of the enzyme for substrate
Km
what does a large Km tell you
rxn only works when substrate conc is very high
what does a low Km tell you
rxn will function toward vmax even at a very low concentration of substrate
what three things could happen to the ES
back to substrates (E+S) or forward to products (E+P)
what is [Etotal]
[ES] +[Efree] which simply considers all forms of enzyme going on in a reaction
state the MM equation
v = vmax[S]/(Km + [S])
state the Lineweaver Burk equation
1/v = km/vmax x 1/[s] + 1/vmax
what is the slope of the lineweaver burk? The y intercept? the x and y axes?
slope = km/vmax
y int = 1/vmax
y axis = 1/v
x axis = 1/[s]
what are the units of Km?
concentration... same units as [S]
what if Km = S
Then v is half velocity of vmax
what are three kinds of inhibitors?
competitive
non competitive
uncompetitive
where do competitive inhibitors bind? non competitive? uncompetitive?
same site
can bind to different site on enzyme OR ES complex
binds exclusively to ES
what changes in the MM or LB with a competitive inhibitor and why?
vmax is the same
km apparent increases because it takes reaction longer to get there
what changes in the MM or LB with non competitive inhibitors?
vmax decreases
Km stays the same
what changes in uncompetitive inhibition?
kM and vmax
BUT slope stays the same!
what reactive groups are typically found in irreversible inhibitors?
ser
cys
Finish the lecture
Finish the lecture!
which inhibitors usually form a covalent bond with some reactive gorup in the enzyme frequently a serine or cys at the active center
irreversible
what was our class example of a irreversible inhibitor
nerve gas DFP
what other type of inhibition do irreversible inhibitors look like
noncompetitive
what happens if you have an irreversilbe inhibitor that gave 50% inhibition and double it again?
100% inactivation
how can you overcome an irreversible inhibitor
high substrate conc
what is a suicide substrate
looks like the normal substrate but when it binds it forms a covalent bond
what three things does the reaction velocity depend on?
catalyc speed
availability of substrate
concentration of product (rate of reverse reaction)
define Km
the [S] at which reaction proceeds at 1/2vmax
what are the units of Km
sames as the substrate concentration units
T or F. Km depends on [enzyme] concentration
FALSE. Km is an intensive constant
Km is inversely relate to the affinity of an enzyme for its substrate, the higher the affinity the _____ the Km
lower
what would .5 units of the enzyme look like?
define Km in terms of k1 k2 k3
Km = (k2+k3)/k1
state the MM equation
State the LB equation
Name two major classes of inhibitors
reversible
irreversible
Name the three subclasses of reversible inhibitors
competitive
non competitive
un competitive
______ inhibitors react only with the free enzyme binding to the active site
competitive
what do the plots for competitive inhibitors look like?
________ inhibitors react with the free enzyme and the enzyme substrate complex. They usually bind to a site on the enzyme surface away from the active site
non competitive
what do plots for noncompetitive inhibitors look like?
_______ inhibitors only react with the substrate bound form of the enzyme
uncompetitive
what do uncompetitive inhibitor plots look like?
fill in the chart
Addition of an irreversible inhibitor will continually lower _____
vmax