Name: Peña, Leda Joy B.

Date: October 20, 2022

Course, Year & Section: BSFT 3A-NS

FOOD CHEMISTRY 2
ACTIVITY 2 – ENZYMES
Supply the following information on the table

ENZYME Examples Functions

1. TRANSFERASES Aminotransferases
Apoptosis Catalyze the transfer of a functional group from
Methyl group a donor molecule, often a coenzyme, to an
Glucokinase acceptor molecule.
Phosphofructokinase
Choline acetyltransferase
2. ISOMERASES Phosphoglucose isomerase Responsible for glycolysis
Triosephosphate isomerase Involved in a critical energy-producing process
known as glycolysis
Maleate isomerase Essential enzyme for the last step of metabolic
degradation pathway of nicotinic acid
Beta-carotene isomerase Breaks down beta-carotene
Photo isomerase Activate the photo-pigment isomerization
catalyst in the biochemical procedure. Peptides
in the eyes
Alanine racemase Catalyzes the conversion of L-alanine to D-
alanine
3. OXIDOREDUCTASES Ceruloplasmin Transports and stores copper by transferring it
from the liver to the blood and then to the
bodily organs that require it.
Catalase Responsible for neutralizing hydrogen peroxide
by its breakdown
Choline Oxidase Catalyzes the reaction between choline and
betaine glycine
Alcohol dehydrogenase Metabolizes the majority of the ethanol eaten
as part of the diet.
Aromatase Converts of androgen to estrogen in many
tissues.
Dihydrofolate reductase Reduces dihydrofolate to tetrahydrofolate via
catalysis.
4. HYDROLASES DNA glycosylase Work on DNA bases, removing damaged bases
and replacing them
Invertase Breaks the glycosidic bonds of sucrose
Esterases Breaks an ester molecule into acid and alcohol
Phosphodiesterases Help in the 3′ cyclic phosphate bond
breakdown of cyclic nucleotides.
 Amylase Stimulates the hydrolysis of starch, converting
it into simple sugars
Helicases Stimulates hydrolysis of ATP molecules to
separate nucleic acid strands
5. LIGASES Acetyl—CoA synthetase (C-S Assisting in the thioester bond synthesis
bond) between Coenzyme A and a carboxylic acid.
Propionyl-CoA carboxylase (C-C Catalyzes the carboxylation of propionyl-CoA
bond) to methylmalonyl-CoA
Ubiquitin Ligases (C-N bond) Helps or directly catalyzes the transfer of
ubiquitin from the E2 to the protein substrate
by recruiting an E2 ubiquitin conjugating
enzyme.
DNA ligase (Phosphoric ester Required for the repair, replication, and
bonds) recombination of DNA
Glutamate–cysteine ligase (C-N Catalyzes the first and rate-limiting step in the
bond) production of the cellular antioxidant
glutathione
Pyruvate carboxylase (C-C bond) Catalyze the ATP– dependent carboxylation of
pyruvate to oxaloacetate
6. LYASES Alginate lyase Catalyzes the degradation of alginate by β-
elimination mechanism
Citrate lyase Synthesis of cytosolic acetyl-CoA in many
tissues.
Pectate lyase Involved in the maceration and soft rotting of
plant tissue
Isocitrate lyase Catalyzes the conversion of isocitrate to
succinate and glyoxylate
Hydroxynitrile Catalyze the addition of cyanide to an aldehyde
or a ketone
Phenylalanine ammonialyase Eliminates ammonia from phenylalanine to
form transcinnamic acid

2. Draw the graph and explain the factors affecting the enzymes
 Temperature, substrate concentration, and pH are the three variables that can influence enzyme
activity. So, under temperature, a process is sped up by raising temperature and slowed down by reducing
temperature. Up to a certain degree, increasing the concentration of the substrate also speeds up the
reaction while it is already occurring; but, after all the enzymes have bound, adding more substrates will
have no further effect on the rate of the reaction. Furthermore, pH variations outside of this range will
slow the enzymes' activity.

3. Draw the schematic diagram for both Competitive and Non-competitive enzyme Inhibition. Explain in
3-5 sentences what happens in the reaction.

A competitive inhibitor physically resembles the substrate for a specific enzyme and engages in
binding competition with the substrate at the enzyme's active site. A noncompetitive inhibitor can bind
to either the free enzyme or the enzyme-substrate complex and binds at a location different from the
active site. Using the neuraminidase inhibitor Relenza as a competitive inhibitor in the treatment of
influenza is one example. The utilization of cyanide as a poison is an illustration of how a non-competitive
inhibitor is put to use (prevents aerobic respiration).