1st Flashcards
A competitive inhibitor of an enzyme is usually
structurally similar to the substrate
Linear inhibition is sometimes called as
complete inhibition
The types of inhibition pattern based on
Michaelis Menten equation are
competitive
non-competitive
uncompetitive
The effect of non-competitive inhibition on a
Lineweaver-Burk Plot is that
it can change the y-intercept
The rate-determining step of Michaelis Menten
kinetics is
the complex dissociation step to produce
product
In competitive inhibition a factor is obtained
from the measurement of
KM
Which of these proteases is not a cysteine active
site protease?
Cathepsin D
Given an enzyme with a Km = 10m M and Vmax = 100 m mol/min. If [S] = 100 m M, which of the following will be true?
A 10-fold increase in Vmax would increase
velocity 10-fold y
The conformational change in an enzyme after the substrate is bound that allows the chemical reaction to proceed, can be explained by
induced fit
The active site of an enzyme remains
a. at the center of globular proteins
b. rigid and does not change shape
c. complementary to the rest of the molecule
d. none of the above
Which category of enzymes belongs to class two in the international classification?
Transferases
The reciprocal equation for non-competitive inhibition can be arranged to the equation for the
Dixon plot
The Woolf-Augusteinsson-Hofstee plot of ν versus ν/[S] and the Eadie-Scatchard plot of ν/[S] versus ν do not involve reciprocals of ν therefore are considered to be more reliable when the error in v is
significant
The relationship between Keq, Km and Vmax is
known as
Haldane equation
Which of the following statements is true for enzymatically catalyzed reaction
The activation energy of the reaction is lowered so that a larger proportion of the substrate qualifies to overcome it
