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.
(Increase km but the Vmax remains constant)
4) The non- competitive inhibitors decrease the Vmax/km but the Vmax/km remains constant.
(Decrease Vmax but the 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/Non competitive.
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.
(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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