BIOCHEMICAL ENGINEERING Flashcards
(472 cards)
A competitive inhibitor of an enzyme is usually
structurally similar to the substrate.
Linear inhibition is sometimes called as
complete inhibition
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
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
Which category of enzymes belongs to class two in the international classification?
Transferases
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
The reciprocal equation for non-competitive inhibition can be arranged to the equation for the
Dixon plot
Which of the following common drugs is not a specific enzyme inhibitor?
Iodine
In a Lineweaver-Burk Plot, competitive inhibitor shows which of the following effect?
It changes the x-intercept
An enzyme and a reactant molecule maintain relationship as
a temporary association
An enzyme is assayed at an initial substrate concentration of 2 x 10-5 M. In 6-minute, half of the substrate is used. The Km for the substrate is 2 x 10- 3 M. The value of k in minute is
0.115
Quasi steady state is also known as
Pseudo steady state
A noncompetitive inhibitor of an enzyme-catalyzed reaction
increases KM and reduces Vmax
An allosteric inhibitor of an enzyme usually
participates in feedback regulation
A classical uncompetitive inhibitor is a compound that binds
reversibly to the enzyme substrate complex yielding an inactive ESI complex
Which graphical method is used to determine an enzyme degree of cooperativity?
Hill plot
The ratio of the amount of a protein present in a sample, which is used as a measure of purification, is known as
specific activity
If a reaction occurs in the absence of inhibitor with rate ν0 and in the presence of inhibitor with rate νi, the degree of inhibition is defined as
(ν0 - νi)/ν0
The rate equation in competitive inhibition based on Michaelis Menten equation is given by
rmaxS/(Km(1+I/Ki) +S))
Classical noncompetitive inhibition is obtained only under
rapid equilibrium conditions