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Choose the correct answer-

1) The enzyme that catalyzes the change in location of the functional group from one position to another within a compound is called Isomerase/Mutase.

2) The enzyme having low affinity for the substrate will have low/high km.

3) The competitive inhibitors increase the Vmax/km but the Vmax/km remains constant.

4) The non competitive inhibitors decrease the Vmax/km but the Vmax/km remains constant.

5) The process of induction of an enzyme is a coarse/fine control for regulation of enzyme activity.

6) Arsenate binds to SH group of the enzyme to inhibit its activity and this mode of inhibition is competitive/Noncompetitive.

7) In normal health LDH-1/LDH-2 is in greater concentration in plasma.

8) Transferases are the enzymes which catalyze the transfer of reducing equivalents/groups other than reducing equivalents.

9) The enzyme activity increases 2/4 fold with every ten degree rise of temperature.

10) The reaction rate is zero/first order when the enzyme activity is directly proportional to substrate concentration.

11) The reaction rate is zero/first order when the enzyme activity is independent of substrate concentration.

12) When the substrate concentration is equal to km the reaction velocity is equal to Vmax/Half Vmax.

13) Pepsin/Trypsin has an optimum p H of 2.0.

14) Hexokinase/ Glucokinase is inducible.

15) Hexokinase/ Glucokinase is inhibited by feed back inhibition.

16) Alkaline Phosphatase/Acid phosphatase rises in malignancy of prostate  gland.

17) LDH/SGOT rises in hemolytic anemias.

18) Methotrexate inhibits dihydrofolate reductase by competitive/Non competitive inhibition.

19) Streptokinase/tPA  causes intravascular bleeding as a side effect.

20) All the Proteolytic/ Lipolytic enzymes are zymases in nature.

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