The plot represents the relationship between
substrate concentration and velocity for a
single enzyme in the absence (curve x) and
presence (curve y) of a compound that binds
allosterically to the enzyme. The allosteric
compound is:

1. a competitive inhibitor.
2. a noncompetitive inhibitor.
3. an irreversible inhibitor.
4. an activator.

The metal ion that acts as a co-factor for both alcohol dehydrogenase and carbonic anhydrase is:

The living state can be best described as a:
1. non equilibrium steady state
2. non equilibrium non steady state
3. equilibrium non steady state
4. equilibrium steady state

The blood concentration of glucose in a normal healthy individual is:

All the following assumptions apply to Michaelis-Menten kinetic analyses of enzyme action EXCEPT:
1. the total enzyme concentration studied at each substrate concentration is fixed in analysis of enzyme kinetics.
2. formation of enzyme-substrate complex does not appreciably decrease the concentration of substrate.
3. Km decreases with competitive inhibition.
4. maximal velocity is reached when the enzyme-substrate complex is equal to the total concentration of enzyme present.

The conversion of glucose into lactic acid in
our muscles takes place in:
1. 9 metabolic steps
2. 10 metabolic steps
3. 11 metabolic steps
4. 12 metabolic steps

The living state is synonymous with:
1. Cellular organization
2. Metabolism
3. Consciousness
4. Reproduction

Consider the following two statements regarding enzyme action:

Of the above statements:
1. Both I and II are correct and II explains I
2. Both I and II are correct but II does not explain I
3. I is correct but II is incorrect
4. I is incorrect but II is correct

Enzymes, vitamins and hormones are common in :
1. Being proteinaceous
2. Being synthesized in the body of organisms
3. Enhancing oxidative metabolism
4. Regulating metabolism

The four elements making 99 % of living system are :
1. CHOS
2. CHOP
3. CHON
4. CNOP