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.