WorksheetsChapter 4.1 Properties and Mechanism of Enzyme
Total questions: 10
Worksheet time: 5mins
What is allosteric site
Specific site on enzyme that bind to specific substrate
Other site than the active site on enzyme
Specific site on enzyme that bind to specific enzyme
Other site for another substrate to bind
Which of the following properties of enzyme is related to small quantity of enzyme required for each reaction?
Reversible
Reusable
Specific
Globular protein
What causes the specificity of each enzyme?
Complementary shape of active site and substrate
The similar shape of active site and enzyme
The different shape of active site and enzyme
The similar shape
Which of the following is a class of enzyme?
Lyase
Transferase
Hydrolase
Decarboxylase
What is the definition Hydrolase class enzyme?
Catalyse the breakdown of chemical bond by adding water molecule
Catalyse the transfer of a functional group from one substrate to another
Catalyse the formation of new bond between two substrate by using energy from ATP.
Catalyse the addition and removal of a group of atom to a substrate
What is an example of enzyme classified as Transferase?
Phosphorylase
RuBP carboxylase
Malate dehydrogenase
Isomerase
How does enzyme lower activation energy?
By bringing substrates closer together
By breaking or forming new bond between enzyme
By providing extra energy to substrate
By binding with substrate at the allosteric site
What is induced fit model?
Binding of substrate induce conformational changes in the active site of enzyme until it fits with substrate
Binding of substrate induce confirmational changes in the active site of enzyme until it is the same with substrate
Binding of substrate induce the enzyme to become activated
Substrate induce the enzyme active site to fit before it binds to the active site
How does pH affects enzyme action?
By altering the acidic/ basic side chain of amino acid in enzyme and break the ionic or hydrogen bond.
By altering the acidic/ basic side chain of amino acid in enzyme and break the ionic or covalent bond.
By breaking the peptide bond between the amino acid in the enzyme.
By altering the acidic/ basic side chain of amino acid in substrate and break the ionic or hydrogen bond.
Why rate of reaction of enzyme remain constant at very high substrate concentration?
All active site are bind with substrate
All substrate are bind with active site
Enzyme become denatured
Enzyme become inactivated
