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Enzyme Kinetics

Enzyme Kinetics

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Published by: giridharraju on Dec 07, 2008
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Enzyme Kinetics
Enzymes (which are large protein molecules) are nature's catalysts. The vast majority of chemical reactions that keep living things alive are much too slow (without a catalyst) to sustainlife. (This is so even though some of the reactions are highly thermodynamically favored.) Anexample of this is the oxidation of a sugar - say glucose - to give water, carbon dioxide andenergy. You can leave glucose open to the air for years without any appreciable oxidation, yetthis is one of the reactions that provides the energy to walk and run in daily life. There arediseases caused by the failure of the body to produce a specific enzyme. (For example, phenylketonuria is a disease which arises from the absence of a single enzyme, phenylalaninehydroxylase.)The Michaelis-Menten mechanism for the catalysis of biological chemical reactions is one of themost important chemical reaction mechanisms in biochemistry. (Maud Menten graduated fromthe University of Toronto, but she was unable to obtain a university position in Canada becauseof the exclusion of women from Canadian universities at that time. As a consequence she did her work the United States.)The Michaelis-Menten mechanism for enzyme kinetics is:. (1)E is the enzyme, S is the "substrate" (the molecule on which the enzyme does its work), and ESis an enzyme-substrate complex. (It is presumed that the substrate must somehow bind to theenzyme before the enzyme can do its work.)We analyze this mechanism as usual. First, we define the reaction rate as the rate of formation of  product and write the kinetic equation implied by this mechanism,. (2)The enzyme-substrate complex, ES, is a transient species so we set up an equation for its rate ochange and apply the steady state approximation,. (3)Solve for [ES],, (4)and substitute it into the equation for the rate,
 
. (5)We might think that we are finished, but there is a complication and some new notation tointroduce. First we introduce the Michaelis-Menten constant,
 K 
M
,, (6)so that the rate becomes,. (7) Now we must deal with the difficulty that [E] is the concentration of free (uncomplexed) enzymeand this is usually not known. What is known is the total enzyme concentration, [E]
o
, but(8)from which we obtain,. (9)The rate becomes, then,(10).Define the reaction velocity as
v
= Rate. So,. (11)
 
 Note that the reaction velocity,
v
, is zero when [S] is zero and that the reaction velocity increasesas we increase [S]. The reaction velocity reaches a maximum when [S] becomes very large.Define the maximum velocity,
v
max
, as,, (12)then. (13) Note that the kinetics of the reaction are characterized by two parameters,
v
max
and
 K 
M
. These arethe parameters that are usually given in the literature in studies of the kinetics of biochemicalreactions.In order to deal with experimental data we write,(14)In an experiment one measures
v
as a function of [S]. If we plot 1/
v
against 1/[S] we should get astraight line with slope,
 K 
M
/
v
max
and intercept 1/
v
max
. This gives us both parameters,. (15)
Enzyme With Inhibitor
 Recall the basic Michaelis-Menten mechanism,. (1)There are several possibilities for an inhibitor, I, to interfere with this reaction:. (16)In words, the inhibitor binds with the enzyme to the exclusion of the substrate.. (17)

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