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WorksheetsAspartate Transcarbamoylase
Total questions: 20
Worksheet time: 14mins
Where does a non-substrate ,non - competitive regulatory molecule bind an enzyme?
At active site
At allosteric site
Offsite
None of these
Which forms do the relaxed and tensed states takes
Inactive and active
Active and inactive
None of these
Which of these is an allosteric enzyme?
Glutamine synthetase
ATCase
All of the above
None of these
Cooperativity means
Two substrates binding to same active site
Binding to one site affects the binding affinity of other sites
Binding to one site donot affects other sites
None of the above
Cooperative behaviour implies that ATC ase must consist of
Multiple subunit
Multiple activesite
Single subunit
Single active site
Inorder to probe the active site of ATCase, which of the following was used?
Ciprofloxacin
Cimetidin
PALA
Isoniazid
Which are the two types of multi- subunit structure in ATCase?
Catalytic trimers and regulatory dimer
Catalytic dimer and regulatory trimer
Catalytic tetramer and regulatory dimer
None of the above
Plotting the rate of N - Carbamoyl aspartate formation verses aspartate gives a
Closed curve
Sigmoidal curve
Hyperbolic
Transcendental curve
At low concentration of CTP, ATCase activity and rate of N-carbamoyl aspartate formation is
Low
High
Constant
Average
ATCase exist in two confirmations
Tense state and relaxed state
Taut state and relaxed state
Tense state and released state
Taut state and released state
In T state, the Enzyme has
Low affinity for substrate
High affinity for substrate
According to concerted model, the activity of ATCase is all or nothing ; which means
It can only exist in T state
It can either exist in T state or R state
It can only exist in R state
It cannot exist in both T and R state
If all the active sites are occupied , this will shifts the equilibrium from
R state to T state
T state to R state
Do ATCase follow MM Kinetics?
Donot follows
Strictly follows
Sometimes follows
None of these
Binding of CTP to the regulatory subunit results in an equilibrium shift towards the
R state
T state
Tensed state
Relaxed state
The site to which the effector binds is termed as
Allosteric site
Regulatory site
Catalytic site
None of these
Enzyme allosterically regulated often have two states known as
The R and R state
The T and R state
The R and P state
The P and T state
Which of these is not a property of allosteric enzyme?
There can be more than one allosteric site present in an enzyme molecule
They have an ability to respond to multiple condition, that influence the biological reaction
Velocity verses concentration of substrate graph of allosteric enzyme is hyperbolic
Allosteric enzyme have a additional site other than active site
Which of the following is a allosteric inhibitor of ATCase ?
ATP
CTP
UTP
Malonate
As the concentration of CTP increases ,then the rate of N-carbamoyl aspartate will get
Doubled
Decreased
Constant
First increases and then decreases
