Republic of the Philippines

Leyte Normal University

Tacloban City

BIOCHEMISTRY
WRITTEN REPORT
(VITAMINS & COFACTOR; ENZYMES)

Group 5
Almerol, Iris Margarette
Basiano, Mark Angelo
Cagoyong, Daryll T.
Jaway, Jill Marie
Llosa, Theresa Mae
Salvacion, Ma. Cassandra June

Prof. Leslie Radaza

BioChem Teacher
VITAMINS & COFACTOR
Objectives:
1. Define the following terms:
a) vitamins and
b) cofactors
2. Describe the function of vitamins and cofactors.
3. Identify the dietary supplement information.
4. Provide sources and examples of each group.

ENZYMES
Objectives:
1. Define the following terms:
a) Enzyme
b) Coenzyme
c) Enzyme kinetics
d) Enzyme Inhibition
e) Michaelis – Menten Enzyme
f) Allosteric enzymes
2. Explain the relation between enzyme and coenzyme.
3. Describe the six classes of enzymes.
4. Explain the specialty of enzymes.
5. Explain the difference between Michaelis – Menten and allosteric
enzymes.

Reporter: Daryll Cagoyong (Vitamins and Cofactors)

Objectives to report:
 Define the following terms:
a. vitamins and
b. cofactors
 Describe the function of vitamins and cofactors.

Content:

The word "vitamin" was coined in 1911 by the Warsaw-born biochemist Casimir
Funk (1884-1967). At the Lister Institute in London, Funk isolated a substance that
prevented nerve inflammation (neuritis) in chickens raised on a diet deficient in that
substance. He named the substance "vitamine" because he believed it was necessary to
life and it was a chemical amine. The "e" at the end was later removed when it was
recognized that vitamins need not be amines. The letters (A, B, C and so on) were
assigned to the vitamins in the order of their discovery. The one exception was vitamin K
which was assigned its "K" from "Koagulation" by the Danish researcher Henrik Dam.
A vitamin is an organic molecule (or related set of molecules) that is an essential
micronutrient that an organism needs in small quantities for the proper functioning of
its metabolism. Essential nutrients cannot be synthesized in the organism, either at all or
not in sufficient quantities, and therefore must be obtained through the diet. Vitamin C can
be synthesized by some species but not by others; it is not a vitamin in the first instance
but is in the second. The term vitamin does not include the three other groups of essential
nutrients: minerals, essential fatty acids, and essential amino acids.
Cofactor is a non-protein chemical compound or metallic ion that is required for
an enzyme's activity. Cofactors can be considered "helper molecules" that assist
in biochemical transformations. The rates at which these happen are characterized
by enzyme kinetics. A cofactor is a non-protein chemical that assists with a biological
chemical reaction. Co-factors may be metal ions, organic compounds, or other chemicals
that have helpful properties not usually found in amino acids. Some cofactors can be
made inside the body, such as ATP, while others must be consumed in food. Minerals,
for example, come from the environment, and cannot be made from scratch by any
living cell. The organic compounds we refer to as “vitamins” are cofactors that our own
bodies cannot make, so we must consume them from food in order for our cells to be able
to perform essential life functions. At the biochemical level, cofactors are important in
understanding how biological reactions proceed. The presence or absence of cofactors
may determine how quickly reactions proceed from their reactant to their product.
At the biological level, understanding cofactors is important to understanding health.
Without the proper cofactors, humans and other animals can develop serious diseases
and even death.

Functions:

Vitamins:
Vitamins have diverse biochemical functions. Some forms of vitamin A function
as regulators of cell and tissue growth and differentiation. The B complex vitamins
function as enzyme cofactors (coenzymes) or the precursors for them. Vitamin D has a
hormone-like function as a regulator of mineral metabolism for bones and other organs.
Vitamins C and E function as antioxidants. Both deficient and excess intake of a vitamin
can potentially cause clinically significant illness, although excess intake of water-
soluble vitamins is less likely to do so.

Cofactor:
Cofactors generally serve the purpose of supplying chemical groups or properties
that are not found in other chemical groups.
ATP, for example, is a cofactor with a unique ability to transfer energy to drive chemical
processes such as the activity of enzymes and transport proteins.
Heme, on the other hand, is a chemical complex that contains iron, which allows heme to
bond to oxygen molecules in a unique way. Heme is necessary for our blood cells to carry
oxygen through our bodies.
There are dozens of known cofactors, each of which may be necessary for multiple
biochemical reactions, as illustrated below.

As a result, the functions of cofactors may be as diverse as their chemical structures

and properties.
The wide-ranging effects of cofactors can be seen by studying vitamin deficiencies:
deficiencies of different vitamins, many of which are cofactors, have many different
negative effects on human health.

Reporter: Theresa Mae Llosa (Vitamins and Cofactors)

Objectives to report:
 Identify the dietary supplement information.
 Provide sources and examples of each group.

Content:
Vitamins and Minerals

2 Types of Vitamins:
  Water-soluble Vitamins – can be  Fat-soluble Vitamins – can be
dissolved in water dissolved in lipids

o Vitamin B1 o Vitamin A
o Vitamin B2 o Vitamin D
o Vitamin B3 o Vitamin E
o Vitamin B5 o Vitamin K
o Vitamin B6
o Vitamin B7
o Vitamin B9
o Vitamin B12
o Vitamin C

(9) Water-soluble Vitamins

1. Vitamin B1 (Thiamine)
Thiamine is a sulfur-containing vitamin that participates in energy metabolism,
converting carbohydrates, lipids and proteins into energy. Thiamine also plays a key role
in nerve and muscle activity.
The primary sources of vitamin B1: Offal (liver, kidneys, heart), fish, meat (pork), whole
grain cereals, leafy green vegetables, asparagus, eggplant, fruits, legumes (beans and
lentils), nuts, soymilk, squash, brewer’s yeast.
Risks related to inadequate or excess intake of vitamin B1: Beriberi- there is damage
to the nervous system characterized by muscle weakness in the arms and legs, or
damage to the cardiovascular system which is characterized by dilated blood vessels,
causing the heart to work harder and the kidneys to retain salt and water, resulting in
edema. No adverse effects have been associated with excessive thiamine intakes.
2. Vitamin B2 (Riboflavin)
Vitamin B2 participates in oxidation-reduction reactions, by accepting and then
donating two hydrogen molecules, which are necessary for releasing energy from
carbohydrates, fats and proteins.

The primary sources of vitamin B2 : Vitamin B2 is found in offal (liver, kidneys, heart),
eggs, meat, milk, yogurt, cheeses, whole grain cereals, dark green leafy vegetables, and
brewer’s yeast.
Risks related to inadequate or excess intake of vitamin B1: Vitamin B2 deficiency co-
occurs with other nutrient deficiencies and it may precipitate deficiencies in vitamin B6
and niacin. People with cardiovascular disease, diabetes or cancer are at risk for vitamin
B2 deficiency.
3. Vitamin B3 (Niacin)
Niacin acts as coenzyme in energy-transfer reactions, especially the metabolism of
glucose, fat, and alcohol. Niacin is similar to the riboflavin coenzymes in that it carries
hydrogen molecules (and their electrons) during metabolic reactions. It also protects
against neurological degeneration. Niacin is unique in that it can also be synthesized from
the amino acid tryptophan. It occurs in two forms: niacinamide and nicotinic acid.
The primary sources of vitamin B3: offal (liver), fish, meat, milk, eggs, whole grain
cereals, legumes, fruit (avocados, figs, dates, prunes), and nuts.
Risks related to inadequate or excess intake of vitamin B3: Pellagra- severe niacin
deficiency and its symptoms are dermatitis, diarrhea, dementia and eventually death.
Risk of excessive intake is unlikely if niacin is consumed from food sources. However
consumption of niacin in the form of nicotinic acid from multiple sources at high levels,
including dietary supplements, pharmaceutical doses, and fortified foods, may result in
adverse effects such as flushing, nausea and vomiting, liver toxicity, blurred vision and
impaired glucose tolerance.
4. Vitamin B5 (Pantothenic Acid)
Vitamin B5 is part of the structure of coenzyme A, the “crossroads” compound in
several metabolic pathways, and is involved in more than 100 different steps in the
synthesis of lipids, neurotransmitters, steroid hormones, and hemoglobin. Vitamin B5 is
important for maintenance and repair of tissues and cells of the skin and hair, helps in
healing of wounds and lesions, and pantethine, which is a form of vitamin B5, normalizes
blood lipid profiles.
The primary sources of vitamin B5: offal (liver, kidneys), meat (chicken, beef), egg yolk,
milk, fish,whole grain cereals, potatoes, tomatoes, broccoli, mushrooms.
Risks related to inadequate or excess intake of vitamin B5 Vitamin B5 deficiency is
very rare and symptoms involve a general failure of all the body’s systems. Symptoms
include fatigue, nausea, vomiting, headaches, tingling sensations (“burning feet”
syndrome). No adverse effects have been reported with high intakes of vitamin B5.
5. Vitamin B6 (Pyridoxine)
Vitamin B6 is required for the majority of biological reactions (i.e., amino acid metabolism,
neurotransmitter synthesis, red blood cell formation). It occurs in three forms: pyridoxal,
pyridoxine, and pyridoxamine.
The primary sources of vitamin B6: There are many good sources of vitamin B6,
including chicken, liver (cattle, pig), fish (salmon, tuna), nuts (walnut, peanut), chickpeas,
maize and whole grain cereals, and vegetables (especially green leafy vegetables),
bananas, potatoes and other
Risks related to inadequate or excess intake of vitamin B6: Deficiency of vitamin B6
alone is uncommon; usually it occurs in combination with a deficit in other B-vitamins.
Individuals at risk for poor intakes are alcoholics and those taking tuberculosis
medication. Signs of vitamin B6 deficiency include microcytic anemia due to inadequate
synthesis of hemoglobin, depression, nerve problems, and irritability. No adverse events
have been observed with high intakes of vitamin B6 (from food or supplements).
6. Vitamin B7
Biotin plays an important role in metabolism as a coenzyme that transfers carbon
dioxide. This role is critical in the breakdown of food (carbohydrates, fats and proteins)
into energy. Biotin is involved in many cellular reactions, particularly in fat and protein
metabolism of hair roots, finger nails, and skin.
The primary sources of vitamin B7: Eggs, milk, vegetables, cereals, nuts (almonds,
walnuts, peanuts), liver, kidney, yeast, soybeans.
Risks related to inadequate or excess intake of vitamin B7 Experts have yet to
quantify the amount of biotin in natural foods. Deficiency due to lack of dietary intake is
rare in healthy populations. Symptoms of deficiency include general fatigue, nausea,
neurological problems, poor skin and hair quality. No adverse effects have been reported
with excessive intakes of biotin.
7. Vitamin B9 (Folate)
Folate refers to the naturally occurring forms (pteroylglutamic acid) as well as the forms
found in fortified foods and supplements (folic acid). Folic acid is the most stable form of
folate.
The primary sources of folate: Dark green leafy vegetables, beans, lentils, asparagus,
wheat germ, yeast, peanuts, oranges, strawberries.
Risks related to inadequate intake of folate: Individuals with diets that lack sufficient
quantity and variety of green leafy vegetables and legumes are at risk for inadequate
folate intake. Folate requirements are increased during pregnancy, especially in the first
couple of weeks of gestation. Folate deficiency is highly associated with the risk for neural
tube defects in the growing fetus. Thus, women of child-bearing age and pregnant women
are advised to meet folate requirements using a combination of natural foods (folate
forms) and fortified foods or supplements (folic acid).
8. Vitamin B12 (Cobalamin)
Vitamin B12 functions as a coenzyme in the conversion of homocysteine to methionine,
in the metabolism of fatty acids and amino acids, and in the production of
neurotransmitters. It also maintains a special lining that surrounds and protects nerve
fibers, and bone cell activity depends on vitamin B12.
The primary sources of vitamin B12: Vitamin B12 is found only in foods of animal origin,
except where plant-based foods have been fortified. Rich sources of vitamin B12 include
shellfish, liver, game meat (venison and rabbit), some fish (herring, sardines, salmon,
trout), milk and milk
Risks related to inadequate or excess intake of vitamin B12: About 10–30% of older
adults are estimated to have chronic inflammation of the stomach, a condition that impairs
the absorption of vitamin B12. It is advised that older adults consume fortified foods or
supplements to meet their vitamin B12 requirements. Vegans (individuals who do not
consume animal-source foods), who do not take fortified foods or supplements, will
develop vitamin B12 deficiency.
9. Vitamin C (Ascorbic Acid)
Vitamin C parts company with the B-vitamins in its mode of action. It acts as an antioxidant
or as a cofactor, helping a specific enzyme perform its job. High levels of vitamin C are
found in pituitary and adrenal glands, eyes, white blood cells, and the brain. Vitamin C
has multiple roles - in the synthesis of collagen, absorption of iron, free radical
scavenging, and defense against infections and inflammation
The primary sources of vitamin C: Fruits (especially citrus fruits), cabbage-type
vegetables, green leafy vegetables, lettuce, tomatoes, potatoes, and liver (ox /calf).
Risks related to inadequate intake of vitamin C: Individuals who do not consume
sufficient quantities of fruits and vegetables are at risk for inadequate intakes of vitamin
C. Because smoking generates free radicals, individuals who smoke have elevated
requirements for vitamin C. Vitamin C deficiency can cause scurvy; signs of scurvy are
bleeding gums, small hemorrhages below the skin, fatigue, loss of appetite and weight,
and lowered resistance to infections.
(4) Fat-soluble Vitamins

1. Vitamin A: Retinol/Carotenoids
Vitamin A plays a central role in our vision, skin, genes, growth, and immune
system. It is especially important during the early stages of pregnancy in supporting the
developing embryo. Infections and fevers increase the requirement for vitamin A.
The primary sources of vitamin A: Retinol is found in liver, egg yolk, butter, whole milk,
and cheese. Carotenoids are found in orange-flesh sweet potatoes, orange-flesh fruits
(i.e., melon, mangoes, and persimmons), green leafy vegetables (i.e., spinach, broccoli),
carrots, pumpkins, and red palm oil.
Risks related to inadequate or excess intake of vitamin A: About 90% of vitamin A is
stored in the liver. Vegetarians can meet their vitamin A requirement with sufficient intakes
of deeply colored fruits and vegetables, with fortified foods, or both. Vitamin A deficiency
is a major problem when diets consist of starchy staples, which are not good sources of
retinol or β-carotene, and when the consumption of deeply colored fruits and vegetables,
animal-source foods, or fortified foods is low. Vitamin A plays a role in mobilizing iron from
liver stores, so vitamin A deficiency may also compromise iron status. Excessive intakes
of pre-formed vitamin A can result in high levels of the vitamin in the liver – a condition
known as hypervitaminosis A. No such risk has been observed with high β-carotene
intakes.
 2. Vitamin D: (Calciferol)
With the help of sunlight, vitamin D is synthesized by the body from a precursor
derived from cholesterol. Vitamin D is therefore not an essential micronutrient, given the
right season and enough time in the sun.
The primary sources of vitamin D: Sunlight – exposure to ultraviolet B (UVB) rays is
necessary for the body to synthesize vitamin D from the precursor in the skin. There are
a few foods that are natural sources of vitamin D. These sources are oily fish, egg yolk,
veal, beef, and mushrooms.
Risks related to inadequate or excess intake of vitamin D: Inadequate exposure to
sunlight is the primary risk factor for poor vitamin D status. One of the main roles of
vitamin D is to facilitate the absorption of calcium and phosphorus. Consequently, a
vitamin D deficiency creates a calcium deficiency, with significant consequences to bone
health. Among children and adolescents, it may cause rickets and adversely affect peak
bone mass. In adults, vitamin D deficiency increases the risk of osteomalacia and
osteoporosis.
3. Vitamin E: (α-Tocopherol)
The most active form of vitamin E is α-tocopherol, which acts as an antioxidant (i.e., stops
the chain reaction of free radicals producing more free radicals). Vitamin E protects cell
membranes, proteins, and DNA from oxidation and thereby contributes to cellular health.
It prevents oxidation of the polyunsaturated fatty acids and lipids in the cells. Vitamin E is
stored in the liver and is safe even at high intakes.
The primary sources of vitamin E: Vitamin E in the α-tocopherol form is found in edible
vegetable oils, especially wheat germ, and sunflower and rapeseed oil. Other good
sources of vitamin E are leafy green vegetables (i.e., spinach, chard), nuts (almonds,
peanuts) and nut spreads, avocados, sunflower seeds, mango and kiwifruit.
Risks related to inadequate or excess intake of vitamin E: Individuals whose diets
consist mostly of starchy staples – with inconsistent intake of edible oils or other vegetable
sources of vitamin E – are at a higher risk of inadequate vitamin E intake. Vitamin E
deficiency leads to red blood cell breakage and nerve damage. Recent studies from
Bangladesh link low vitamin E blood levels to an increased risk of miscarriage. In other
studies, vitamin E supplementation has been successfully used for the treatment of non-
alcoholic fatty liver disease, a condition widespread in overweight and obese people.
Excessive intake of vitamin E from food is very rare.
4. Vitamin K: (Phylloquinone | Menaquinones)
Vitamin K acts primarily in blood clotting, where its presence can make the difference
between life and death. More than a dozen different proteins and the mineral calcium are
involved in making a blood clot. Vitamin K is essential for the activation of several of these
proteins. When any of the blood clotting factors is lacking, hemorrhagic disease
(uncontrolled bleeding) results. Vitamin K also participates in the metabolism of bone
proteins, most notably osteocalcin. Without vitamin K, osteocalcin cannot bind to the
minerals that normally form bones, resulting in poor bone mineralization. Vitamin K is
stored in the liver.
The primary sources of vitamin K: Vitamin K is found in plant foods as phylloquinone
(K1). Bacteria in the lower intestine can synthesize vitamin K as menaquinone (K2), which
is absorbed by the body. Sources of phylloquinone are green leafy vegetables (i.e.,
parsley, spinach, collard greens, and salad greens), cabbage, and vegetables oils
(soybean, canola, olive). Menaquinones are also found in fermented foods such as
fermented cheese, curds, and natto (fermented soybeans).
Risks related to inadequate or excess intake of vitamin K
Vitamin K is poorly transferred via the placenta and is not found in significant quantities
in breast milk, so newborn infants are especially at risk for bleeding. This innate vitamin
K deficiency is treated with intramuscular injection or oral administration of phylloquinone.
Supplementation with vitamin K has been found to be beneficial for improving bone
density among adults with osteoporosis because it drives synthesis of a special protein
called matrix Gla protein.
Minerals
 Essential inorganic nutrients, required in small amounts.
 As many as 20 minerals may be required!
 Required for growth, maintenance, reproduction and lactation.
The Macrominerals
• Calcium (Ca)
 Function: major component of bones and teeth and essential in blood
coagulation, nerve and muscle function and milk and egg production.
 Deficiency signs: retarded growth, deformed bones in young animals
(rickets), and soft shelled eggs and osteoporosis in older animals.
 Sources: milk, oyster shells and limestone.
 Sodium chloride (NaCl)
 Considered together because of a close biochemical relationship and are
provided as common salt (NaCl)
 Function: required for the formation and retention, concentration and pH of
body fluids, such as protoplasm, blood. Important in the formation of
digestive juices and functions in nerve and muscle activity.
 Deficiency signs: poor condition and depressed appetite. Most farm
produced feeds are deficient in these two minerals.
 Sources: salt supplements and injectable products.
 Phosphorus (P)
 Function: essential for the formation of bones, teeth, and body fluids.
Required for metabolism, cell respiration and normal reproduction.
  Deficiency signs: similar to calcium deficiency, lack of appetite, poor
reproduction and unthrifty appearance.
 Sources: dicalcium phosphate, bone meal, and low fluorine phosphates.
 Potassium (K)
 Function: retention and formation of body fluids, pH concentration of body
fluid and rumen digestion.
 Deficiency signs: nonspecific and unlikely under most conditions but may
have decreased feed consumption and efficiency.
 Sources: roughages. Grains are less than roughages
 Manganese (Mn)
 Function: Fetal development, udder development, milk production and
skeleton development.
 Deficiency signs: Abortions, reduced fertility, deformed young and poor
growth.
 Sources: Most use trace mineralized salt.

Microminerals
 Copper (Cu)
 Function: should be present in animal tissues for iron to be properly utilized,
hemoglobin formation and synthesis of keratin for fair and wool growth.
 Deficiency signs: poor pigmentation of feathers, stringy wool, sway back
lambs, lack of muscle coordination and anemia.
 Sources: forages and copper salts.
 Iron (Fe):
 Function: essential for the function of every organ and tissue of the body
(Hemoglobin).
 Deficiency signs: seldom occurs in older animals, nutritional anemia,
labored breathing and pale eyelids, ears and nose.
 Sources: forages and copper or trace mineral salts.
 Cobalt (Co)
 Function: required as a nutrient for the microorganisms in ruminants and
thereby aids in rumen synthesis of Vitamin B12. Because swine cannot
manufacture B12 from cobalt, the diets are supplemental with vitamin B12
instead.
 Deficiency signs: lack of appetite, loss of weight, rough hair coat, anemia,
decreased milk and wool production and death in extreme cases.
 Sources: legume forages and salt containing cobalt.
 Magnesium (Mg)
 Function: similar to calcium and phosphorus.
 Deficiency signs: Animals are irritable, their heart beat is irregular and there
is severe kidney damage.
 Sources: mineral supplements and ordinary feeds.

Vocabulary Review
  Nutrients: chemical substances in food that are used by the body to produce
energy and tissues.
 Vitamins: essential organic nutrients, required in small amounts that cannot be
synthesized by the body. Required for growth, maintenance, reproduction and
lactation.
 Vitamin deficiency: decline in health due to the lack of a vitamin in a ration.
 Fat soluble vitamin: a vitamin that can be stored and accumulated in the liver and
other fatty tissues.
 Water soluble vitamin: a vitamin that cannot be stored in the tissues. Must be
provided regularly as deficiencies can develop in a short time.
 Minerals: essential inorganic compounds, required in small amounts. Required
for growth, maintenance, reproduction and lactation.
 Macrominerals: required in large amounts.
 Microminerals: required in small amounts.

Reporter: Ma. Cassandra June Salvacion (Enzymes)

Objectives to report:
 Define the following terms:
a. Enzyme
b. Coenzyme
c. Enzyme kinetics
d. Enzyme Inhibition
e. Michaelis – Menten Enzyme
f. Allosteric enzymes
Content:
Enzymes
Enzymes are proteins that catalyse biochemical reactions. In general, a protein is
a chain of amino acids (aa) covalently linked (when the chain is short ~ 5-10 aa, the
protein is often called oligopeptide/polypeptide or simply peptide). Thousands of different
proteins are built with the same ubiquitous set of 20 amino acids (the protein “alphabet”).
Some proteins have structural roles (e.g. actin in the muscles), other have catalytic
(chemical-reaction-making) activity and are called enzymes. Most enzymes are globular
proteins wherein a few are made of RNA that catalyse biochemical reactions involving
nucleic acids.
Enzymes are biological molecules (typically proteins) that significantly speed up
the rate of virtually all of the chemical reactions that take place within cells. They are vital
for life and serve a wide range of important functions in the body, such as aiding in
digestion and metabolism. They are high molecular weight compounds made up
principally of chains of amino acids linked together by peptide bonds. They accelerate the
rate of chemical reactions without permanent alterations to themselves. The reaction
takes place in a small part of the enzyme called the active site, while the rest of the
protein acts as "scaffolding". The substance acted on by an enzyme is called the
substrate.
Each organism contains thousands of enzymes and some are simple proteins
consisting only of amino acid units. Others are conjugated and consist of a protein part,
or apoenzyme, and a nonprotein part, or coenzyme or cofactor. Both parts are
essential, and a functioning or biochemically active enzyme that consists of both the
protein and nonprotein parts is called a holoenzyme: Apoenzyme + Coenzyme =
Holoenzyme
There are parts to enzyme catalysis and these different aspects of the same
process are: Reaction Mechanism (Enzyme-Substrate Complex) and Molecular
Geometry (Lock and Key Model) with the latter’s modification the Induced-Fit Theory.
The Enzyme-Substrate Complex is formed after the substrate first binds to the active site
of the enzyme and then it is converted into product while attached to the enzyme, finally
releasing the product and allowing the enzyme to start all over again. Meanwhile, the
substrate molecule is complementary in shape to that of the active site and is thought to
exactly fit into the active site of the enzyme molecule like a key fitting into a lock thus the
Lock and Key Model. On the other hand, Induced-fit theory proposes that enzymes have
flexible conformations where they change shape adapting to incoming substrates in order
to accept and accommodate for them to bind.

Coenzymes
Coenzymes are non-protein organic substances which are essential to the efficient
functioning of some enzymes, but are not themselves bound to the enzyme. Many
coenzymes are derived from vitamins.

Coenzymes play a role in the function of cells. Reactions within the cells work to
either break down nutrients or combine molecules for cellular activities that keep the cells
alive. Enzymes speed up these reactions. Without enzymes, these reactions may not
occur. Coenzymes, in turn, support the functions of enzymes. They loosely bind to
enzymes to help them complete their activities. Coenzymes are non-protein, organic
molecules that facilitate the catalysis, or reaction of its enzyme.

Enzyme Kinetics
Enzyme kinetics is the study of the binding affinities of substrates and inhibitors
and the maximal catalytic rates that can be achieved. Much of the nature of enzymes was
learned from the Michaelis-Menten plots (Leonor Michaelis and Maud Menten).
A living system controls its activity through enzymes. An enzyme is a protein
molecule that is a biological catalyst with three characteristics. First, the basic function of
an enzyme is to increase the rate of a reaction. Most cellular reactions occur about a
million times faster than they would in the absence of an enzyme. Second, most enzymes
act specifically with only one reactant (called a substrate) to produce products. The third
and most remarkable characteristic is that enzymes are regulated from a state of low
activity to high activity and vice-versa.
The enzyme activity, the measure of the rate at which an enzyme converts
substrate to products in a biochemical reaction and is usually measured as turnover
number which is the number of molecules of substrate acted on by one molecule of the
enzyme per minute. The activity is affected by four factors namely: temperature, pH,
substrate concentration, and enzyme concentration.
Enzymes work fastest when they have an optimum temperature wherein the
enzyme and substrate molecules both have more kinetic energy and so collide more often
and also more molecules have sufficient energy to overcome the activation energy.
Enzymes also exhibit maximum activity at optimum pH where for most enzymes it’s
about pH 7-8 (normal body pH) but a few can work at extreme pH like gastric protease
(pepsin) in our stomach that has an optimum of pH 1. Small changes in pH can result in
enzyme denaturation and loss of function. An enzyme is also working at its maximum
capacity as the substrate concentration increases until a saturation point, substrate
molecules are bound to all available active sites of the enzyme molecules, is met where
the reaction rate stays the same even if the number of substrate is increased. Also as the
enzyme concentration increases, the rate of the reaction also increases due to more
enzyme molecules therefore more active sites that are available to catalyse the reaction
and thus more enzyme-substrate complex forms.
The individuality of a living cell is due in large part to the unique set of some 3,000
enzymes that it is genetically programmed to produce. Even if one enzyme is missing or
defective, the results can be disastrous.
Enzyme Inhibition
Enzyme inhibition means the decreasing or cessation in the enzyme activity.
Enzyme inhibitors are substances that bind to enzymes which alter its catalytic action and
consequently slow down, or in some cases, stop catalysis. They are a variety of small
molecules which can reduce the rate of an enzyme-controlled reaction that are found
naturally but are also used artificially as drugs, pesticides and research tools. Inhibition
may be reversible or irreversible.
I. Reversible inhibition
The inhibitor binds reversibly to an enzyme, establishing an equilibrium between
the bound and unbound inhibitor can be easily removed from the enzyme and cause no
permanent damage by shifting the equilibrium. Once it combines with the enzyme, the
active site is blocked and no further catalysis takes place. There are two types:
a) Competitive inhibitors
- compete with the substrates for the active sites of by binding to the
enzyme molecules as they are structurally similar to the substrate and so
the reaction is slower.
- while remain in the active sites, they prevent access of the true
substrate.
 - is a reversible process where either increasing the concentration of
the substrate or decreasing the concentration of the enzyme will
outcompete the competitive inhibitor. If the substrate concentration is
increased, it will restore reaction rate.
b) Non-competitive inhibitors
- this molecule is quite different in structure from the substrate and
does not fit into the active site. It binds to another part of the enzyme
molecule other than the active site, changing the shape of the whole
enzyme, including the active site, so that it can no longer bind substrate
molecules.
- Non-competitive inhibitors therefore simply reduce the amount of
active enzyme where increasing the substrate concentration does not affect
the inhibition since it can’t bind to the site occupied by the inhibitor. The
process can be reversed only by lowering the non-competitive inhibitor.
II. Irreversible inhibition
The inhibitor combines with the enzyme permanently and so the enzyme unable
to carry out its catalytic function forever. Heavy metal ions such as mercury and silver
cause disulphide bonds to break. These bonds help to maintain the shape of the enzyme
molecule. Once broken the enzyme molecule’s structure becomes irreversibly altered
with the permanent loss of its catalytic properties.

Michaelis – Menten Enzyme

The Michaelis-Menten model is the one of the simplest and best-known
approaches to enzyme kinetics.
It takes the form of an equation relating reaction velocity to substrate concentration
for a system where a substrate S binds reversibly to an enzyme E to form an enzyme-
substrate complex ES, which then reacts irreversibly to generate a product P and to
regenerate the free enzyme E.
This system can be represented schematically as follows:

The Michaelis-Menten equation for this system is:

 Here, Vmax represents the maximum velocity achieved by the system, at maximum
(saturating) substrate concentrations. KM (the Michaelis constant; sometimes
represented as KS instead) is the substrate concentration at which the reaction velocity is
50% of the Vmax. [S] is the concentration of the substrate S.

Allosteric Enzymes
An allosteric enzyme is an enzyme that contains a region to which small, regulatory
molecules ("effectors") may bind in addition to and separate from the substrate binding
site and thereby affect the catalytic activity.
Allosteric enzymes are those modulated by agents that bind to them at a site
different to the active center.
Enzymes are biological catalysts. They accelerate the rates of reactions in cells
without being changed themselves during the process of reaction. Allosteric enzymes are
a subset of enzymes that are involved in the control and regulation of biological
processes. The control of processes is essential to biological systems: A cell that divides
out of control has undergone a kind of transformation (cancerous or precancerous) that
can threaten an entire organism. There are many processes occurring inside the cell at
any one time, and they must coexist in proper balance. This balance is where allosteric
enzymes come into play.
Allosteric enzymes have the ability to respond to several different conditions in
their environments. Every enzyme contains an active site, the location on the enzyme
where it catalyzes its specific reaction. Allosteric enzymes contain a second type of site,
called an allosteric site. The allosteric site, through its binding of a non-substrate
molecule, influences (enhances or impairs) the activity of the enzyme. The word
"allosteric" is derived from two Greek words: allos, meaning other, and stereos, meaning
site. Another important feature of allosteric enzymes is that they consist of multiple
polypeptide chains, with multiple active and allosteric sites.

Reporter: Jill Marie Jaway (Enzymes)

Objectives to report:
 Explain the relation between enzyme and coenzyme.
 Describe the six classes of enzymes.

Content:
 Catalyst
o A substance that increases the rate of a chemical reaction without being
changed or consumed in the reaction.
 Enzymes
o biological catalysts, nearly all of them are proteins.
 o it is neither consumed nor changed in the reaction.
o commonly known as biocatalysts.

 Coenzyme
o a substance that enhances the action of an enzyme
o vitamins B1, B2, B6 serves as coenzymes.
The relationship between the enzyme and coenzyme is that the enzyme is a protein
which catalyzes a particular biochemical reaction inside the cell whereas
the coenzyme is a non-protein molecule which carries chemical groups between
enzymes.
SIX CLASSES OF ENZYMES

Reporter: Iris Margarette Almerol (Enzymes)

Objectives to report:
 Explain the specificity of enzymes.

Content:
 One of the properties of enzymes that makes them so important as diagnostic and
research tools is the specificity they exhibit relative to the reactions they catalyze. A few
enzymes exhibit absolute specificity; that is, they will catalyze only one particular reaction.
Other enzymes will be specific for a particular type of chemical bond or functional group.
In general, there are four distinct types of specificity:
 Absolute specificity - the enzyme will catalyze only one reaction.
 Group specificity - the enzyme will act only on molecules that have specific
functional groups, such as amino, phosphate and methyl groups.
 Linkage specificity - the enzyme will act on a particular type of chemical bond
regardless of the rest of the molecular structure.
 Stereo chemical specificity - the enzyme will act on a particular steric or optical
isomer.

Reporter: Mark Angelo Basiano (Enzymes)

Objectives to report:
 Explain the difference between Michaelis – Menten and allosteric enzymes.
Content:
The difference between Michaelis-Menten and Allosteric enzyme
ALLOSTERIC REGULATION
Allosteric enzyme:

Oligomeric organization (more than one active site and

more than one effector-binding site)
The regulatory effects exerted on the enzyme’s activity are
achieved by conformational changes occurring in the
protein when effector metabolites bind

Conformational states for a protein (monomer):

Taut state (T): Low substrate affinity

Relaxed state (R): High substrate affinity

Homotropic effect: The ligand-induced conformational

change in one subunit can affect the adjoining subunit:
Cooperativity

Usually, it is positive regulation

No Michaelis-Menten kinetics

Sigmoidal curves

STEADY-STATE ASSUMPTION AND MICHAELIS-MENTEN EQUATION

Michaelis-Menten equation describes a curve known as a rectangular hyperbola
The velocity of the product formation is:
[ES] depends on:
the velocity of ES formation from E + S
the velocity of its dissociation to regenerate E+S or to form E + P.
Under experimental conditions [S]>>>[E]. The [ES] quickly reaches a constant value in
such dynamic, and remains constant until complete P formation: Steady State
assumption
Maximal velocity is obtained when the enzyme is saturated: [E]T=[ES]

REFERENCES:
D.C. DeLuca, J. Lyndal York, in Encyclopedia of Genetics, 2001
https://sciencing.com/role-coenzymes-5164918.html
http://www.math.pitt.edu-~bard/bardware/classes/mth3380/enzyme_inhib.pdf
https://www.livescience.com/45145-how-do-enzymes-work.html
http://www.chemistryexplained.com/A-Ar/Allosteric-Enzymes.html
https://depts.washington.edu/wmatkins/kinetics/michaelis-menten.html