Sulfanilamide that resembles substrate of an enzyme inhibits the
enzyme when added to the reaction mix. What type of inhibition is
this
A) allosteric inhibition
B) competitive inhibition
C) excitatory allosteric control
D) noncompetitive inhibition
E) feedback inhibition
An enzyme (select all that apply)
1) is not altered by reaction with a substrate
2) is changed by reaction with a substrateis
3) made of carbohydrate
4) can be reused if not damaged
5) is made of protein
6) slows the rate of chemical reactions
7) increases the rate of chemical reaction
Select all that apply. An enzyme
1) is a carbohydrate
2) is a protein
3) is a biological catalyst
4) is changed by reaction with a substrate...
50. The table represents the
rates of reaction at specific substrate concentrations for an
enzyme that displays classical Michaelis-Menten kinetics. Two sets
of inhibitor data are also included. Determine the Km and Vmax for
the uninhibited enzyme.
[s](mM) Without
inhibitor Vo (µM/s) With inhibitor A
With Inhibitor B
1.3
2.50
1.17
0.62
2.6
4.00
2.10
1.42
6.5
6.30
4.00
2.65
13.0
7.60
5.70
3.12
26.0
9.00
7.20
3.58
Please Please Please....show
detailed steps so...
If the substrate concentration is limiting, how does increasing
enzyme concentration affect reaction rate?
A.Increasing enzyme concentration has no effect on reaction
rate.
B.Increasing enzyme concentration results in an increase in
reaction rate.
C.Increasing enzyme concentration decreases reaction rate.
1. (3%) You measure the initial rate of an enzyme reaction as a
function of substrate concentration in the presence and absence of
an inhibitor. The following data are obtained: [S] V0 –Inhibitor
+Inhibitor 0.0001 33 17 0.0002 50 29 0.0005 71 50 0.001 83 67 0.002
91 80 0.005 96 91 0.01 98 95 0.02 99 98 0.05 100 99 0.1 100 100 0.2
100 100
a) What is the Vmax in the absence of inhibitor?
b) What is...
3. What happens to the enzyme and the substrate during a
chemical reaction? What does it mean by enzymes being “specific”?
Why is the active site specific for only one type of
substrate?
Please type the answer. Thanks
2) The initial rate for an enzyme-catalyzed reaction has been
determined at a number of substrate concentrations. Data are given
below. [S](mu*M) 5 10 20 50 100 200 500 vo (mu*Mmin-1) 21 62 92 126
185 210 217 a) Estimate Vmax and Km from a direct graph of vo vs
[S] (Michaelis-Menton plot). b) Use a Lineweaver-Burk plot to
analyze the same data. What are the values of Vmax and Km? c) If
the total enzyme concentration is 100 pM,...
What has to occur for an enzyme to catalyze a reaction? Select
all correct.
A.
The enzyme and substrate cannot interact with each other
B.
The enzyme and substrate have to undergo a chemical with each
other
C.
The enzyme and an inhibitor have to come into contact at the
active site
D.
The enzyme needs to become denatured prior to contact
E.
The enzyme and substrate have to undergo temporary non-covalent
interactions with each other
F.
The enzyme and...
1a) what is the relationship between substrate
concentration and reaction rate?
b) Describe how the enzyme structure is
effected:
i) below the optimal
temperature
ii)above the optimal
temperature?
c)Why is enzyme activity reduced at pH values above or
below the optimum? How does the enzyme structure change at
non-optimum pH?
You have added an irreversible inhibitor to a sample of enzyme and substrate. At this point, the reaction has stopped completely. What can you do to regain the activity of the enzyme?
Removing the irreversible inhibitor should get the reaction working again.
Adding more substrate will increase the rate of reaction.
Adding more inhibitor should get the reaction up to speed again.
The enzyme is inactive at this point. New enzyme must be added to regain enzyme activity.