In general, with every 10^oC rise in the temperature [in the range 0^oC to 40^oC], the rate of enzyme catalyzed reaction:
1. Becomes half
2. Gets doubled
3. Remains same
4. There is no such correlation in general

Low temperature:
1. Preserves enzyme in a temporary inactive state
2. Denatures the enzyme
3. Makes enzyme more active
4. Does not have any affect on enzyme activity

In non competitive inhibition, an increase in substrate concentration would:
1. Increase the rate of the reaction
2. Decrease the rate of the reaction
3. Not increase the rate of the reaction
4. Nullify the effect of the inhibitor

Most common enzyme inhibition used in control of bacterial pathogens is:

Enzymes that catalyze removal of groups from substrates by mechanisms other than hydrolysis leaving double bonds are:

Transferases do not catalyze the transfer of the following group between a pair of substrates:

The non protein constituent present in many enzymes is called:

Haem in hemoglobin:
1. is loosely bound
2. is the co-enzyme
3. is the prosthetic group
4. has no influence on activity of Hb

What is the co-factor for the proteolytic enzyme, carboxypeptidase?

Most of the coenzymes contain: