WorksheetsEnzyme kinetics
Total questions: 22
Worksheet time: 8mins
A biological catalyst
Enzyme
Coenzyme
Apoenyme
Holoenzyme
Non protein component of an enzyme
Coenzyme
Cofactor
Holoenzyme
Apoenzyme
In to how many groups enzymes are classified as
Four
Six
Five
Eight
Region on enzyme where catalytic reaction occurs
Catalytic site
Active site
Binding site
Interaction site
A common measure of activity is
Permit number
Turnover number
Activity number
Enzyme number
Tight binding interaction of enzyme substrate indicates ......... Km value
Large
Initially large and then small
Initially small and the large
Small
Weak binding interaction of enzyme and substrates indicates ..........Km value
Small
Initially slow
Initially fast
Large
Which type of inhibition has structural resembles of I and E
Non competitive
Competitive
Uncompetitive
Non of the above
In which type of Inhibition inhibitor binds with ES complex
Uncompetitive
Non competitive
Competitive
All of the above
In which type of inhibition inhibitor has the tendency to bind with both E and ES complex
Competitive
Non competitive
Un competitive
Mixed
In competitive inhibition, from lineweaver burk plot Km value
Remains constant
Changes
Changes with addition of inhibitor
None of the above
In which type of inhibition both Km and Vmax changes?
Competitive
Non competitive
Mixed inhibition
Un competitive
Confinement of enzyme movement is known as
Inhibition
Immobilisation
Grouping
All the above
Immobilisation technique that uses semipermeable membrane for entrapment
Matrix entrapment
Microencapsulation
Cross linking
Adsorption
Insoluble support medium for confining enzyme movement is
Absorbent
Matrix
Carrier
All the above
To treat metabolic disorder phenyl ketonuria which type of immobilisation technique is adopted
Covalent bonding
Cross-linking
Micro encapsulation
Matrix entrapment
Sensitivity of enzyme is associated with
Denaturation
Steric hindrance
pH level
None of the above
Growth of micro organism is inhibited at a pressure of
400-700MPa
300-600MPa
300-600Pa
400-700Pa
Optimum pH range for effective enzyme activity is
2-4
5.5-7.5
7-13
5-6
pH of pepsin is ..........
2
4
2.5
3.5
Which is Michaelis Menten equation
V=Vmax S/(Km+S)
V=Vmax S/2(Km+S)
1/V=1/Vmax+Km/Vmax S
V=Vmax-KmV/S
Qualitative features of Michaelis Menten Equation is
The reaction rate if 1st order
As substrate concentration inc reaction order in substrate dec
The rate of reaction is proportional to the total amount of enzyme present
All the above
