Course Code & Description: Sci Ed 114.

1 Cell & Molecular Biology (Laboratory)

Group 4 Members: AGYOD, Redford | DOLO, Jan Kaiser | DOQUEY, Dream | DUMALNOG, Geryl Mae |
SALEY, Joylyn | TANGONAN, Ana Marie
Degree & Section: BSED 3D

QUESTIONS FOR RESEARCH

1. What biomolecules make up enzymes?
The biomolecules that make up enzymes are proteins comprised of amino acids linked together in one
or more polypeptide chains. They act as catalysts when bonded upon substrate molecules decreasing the
activation energy necessary for a chemical reaction to occur. The lower the activation energy, the faster the
rate of a reaction. Thus, enzymes speed up reactions by lowering activation energy.
2. Describe the influence of the following factors on the rate of enzyme activity:
a. Temperature - As the temperature increases, the rate of enzyme activity increases as well. Hence, as
the temperature lowers, the reaction also slows down. The enzyme’s optimum activity is reached at its
optimum temperature. However, as there is continuous increase of temperature at extreme levels, there
is a sharp decrease in enzyme activity as the enzyme's active site changes shape and is already being
denatured.

b. pH - Each enzyme work bests at a specific pH value. The optimum pH for an enzyme depends on
where it normally works. As the pH increases so does the rate of enzyme activity until it reaches its
optimum activity at its optimum pH. Same with temperature, a continued increase and decrease in pH
at extreme levels results in a sharp decrease in activity as the enzyme’s active site changes shape and
is now being denatured.

c. Substrate concentration - As the enzyme molecules become saturated with substrate, this increases
reaction rate levels. Which, an optimum rate is reached at the enzyme’s optimum substrate
concentration. A continued increase in substrate concentration results in the same enzyme activity as
there are not enough enzyme molecules available to break down the excess substrate molecules.

d. Enzyme concentration - Increased enzyme concentration speed up the enzyme reaction, as long as
there is substrate available to bind it, once all of the enzymes have been bonded, any substrate
increase will have no effect on the rate of reaction, as the available enzymes will be saturated and
working at their maximum rate. This is simply because more substrate molecules will be colliding with
enzyme molecules, so more product will be formed.

e. Inhibitors - The influence of the inhibitors is that it reduces the compatibility of substrate and enzyme
that leads to the inhibition of enzyme substrate complexes formation, preventing the catalysis of
reactions and decreasing at times to zero, the amount of product produced by a reaction. Thus,
Inhibitors alter the catalytic action of the enzyme and consequently slow down or in some cases stop
catalysis.
3. Describe the major classes of enzymes based on their function and give one specific example for each. Give the substrates, specific
reaction and products of each example given.

Major Classes of Function Example Substrate Specific Reaction Products

Enzyme
1) Oxidoreductase Catalyze the transfer Dehydrogenase Glyoxylate Catalyze the reversible Lactate to Pyruvate:
of electrons from one conversion of lactate to  Pyruvic acid
molecule to another (ex:. Lactate pyruvate with the  NADH, H+
molecule. Dehydrogenase) reduction of NAD+ to
NADH and vice versa. Pyruvate to Lactate:
 Lactic Acid
 NAD+
2) Transferase Catalyze the transfer Transaldolase Fructose-6- In the Pentose  erythrose-4-phosphate
of a group of atoms phosphate Phosphate Pathway, the
(ex: amine, carboxyl, enzyme Transaldolase  fructose-6-phosphate.
carbonyl, methyl, transfers a
etc.)l from a donor dihydroxyacetone group
substrate to an from donor compounds
acceptor compound. (fructose 6-phosphate
or sedoheptulose 7-
phosphate) to aldehyde
acceptor compounds.
3) Hydrolase Catalyze the Lipase Triglycerides Catalyzes the hydrolysis  Fatty acid
cleavage of a of triglycerides.
covalent bond using  glycerol
water (Hydrolysis).
4) Lyase Catalyze splitting of Aldolase Fructose1, 6- In the Glycolysis  Dihydroxyacetone
chemicals into bisphosphate metabolic pathway, phosphate (DHAP)
smaller parts without Aldolase catalyzes the
the use of water. conversion of fructose  glyceraldehyde - 3 -
1-6-diphosphate to phosphate.
glyceraldehyde 3-
phosphate and
dihydroxy-acetone
phosphate.
5) Isomerase Catalyze Epimerase DP-glucose UDP-galactose 4- UDP-galactose to UDP-
rearrangement of epimerase catalyzes the glucose:
atoms within a (ex: UDP- interconversion of UDP-
molecule galactose 4 galactose and UDP-  UDP-glucose
epimerase) glucose during normal UDP-glucose to UDP-
galactose metabolism. galactose:
 UDP-galactose

6) Ligase Catalyze the Carboxylase Biotin Catalyzes the  Oxaloacetate

reaction of joining anaplerotic
(ex: Pyruvate
two large carboxylation of
Carboxylase)
molecules by pyruvate to
establishing a new oxaloacetate
chemical bond
7) Translocase Catalyze the Ornithine Ornithine Transports ornithine  Mitochondrial
movement of ions translocase into the mitochondria ornithine
or molecules for use in the urea
across membranes cycle.
or their separation
within membranes

4. Describe one tool/ procedure in molecular biology used in studying enzyme activity.
One tool/ procedure in molecular biology used in studying enzyme activity are enzyme assays
Enzyme assays are used to characterize an enzyme by measuring its activity. The decrease in substrate or the increase in product during a
specific time interval are used to determine measurement techniques. From the measured parameters, the necessary value may be determined.
Because assays can only be assessed if all reaction conditions are the same, factors such as a sufficient pH, buffer, and temperature must be
specified and maintained constant all across the reaction.