Enzymes and Vitamins
enzymes.
General Characteristics of Enzyme
❑ An enzyme is a compound,
usually protein, that acts as a
catalyst for a bio-chemical
reaction.
❑ Each cell in the human body
contains thousands of different
enzymes because almost every
reaction in a cell requires its
own specific enzyme. Enzymes
cause cellular reactions to
occur millions of times faster
than corresponding
uncatalyzed reactions.
❑ Enzymes are not consumed
during the reaction but merely
help the reaction occur more
rapidly. The word enzyme
comes from the Greek words
en which means ‘in’ and zyme
which means ‘yeast’
❑ Most enzymes are globular
proteins. It was thought that all
enzymes are proteins in 1980’s
A few enzymes are that are
now know are made up of
ribonucleic acid (RNA).
Enzymes undergo all reactions
of proteins, including
denaturation. Slight
alterations in pH or
temperature can affect
enzyme activity drastically. The
biochemist must exercise
extreme caution in handling
enzymes to avoid loss of their
activity.
Enzyme Structure
✓ Enzyme Structure can be
divided into two general
structural classes: simple
enzymes and conjugated
1.) A simple enzyme is an
enzyme composed only of protein
(amino acid chains).
2.) A conjugated enzyme is an
enzyme that has a nonprotein part in
addition to a protein part.
✓ An apoenzyme is the protein
part of a conjugated enzyme. A
cofactor is the nonprotein part
of a conjugated enzyme.
✓ A holoenzyme is the
biochemically active
conjugated enzyme produced
from an apoenzyme and a
cofactor. Apoenzyme + cofactor
= holoenzyme
Why do apoenzymes need cofactors?
 Cofactors provide additional
chemically reactive functional
groups besides those present
in the amino acid side chains of
apoenzymes.
 It is generally either a small
organic molecule or an
inorganic ion (usually a metal
ion).
 Coenzyme is a small organic
molecule that serves as a
cofactor in a conjugated
enzyme. Typical inorganic ion
cofactors include Zn^2 +
Mg^2+, Mn^2+, and Fe^2+. The
nonmetallic CI° ion
occasionally acts as a cofactor.
Dietary minerals are an
important source of inorganic
ion cofactors.
Nomenclature and Classification of Enzymes are grouped into six major
Enzyme classes on the basis of the types of
reactions they catalyze.
➢ Enzymes are most commonly
named by using a system that 1. An oxidoreductase is an
attempts to provide enzyme that catalyzes an oxidation–
information about the function reduction reaction. Because oxidation
(rather than the structure) of and reduction are not independent
the enzyme. Type of reaction processes but linked processes that
catalyzed and substrate must occur together, an
identity are focal points for the oxidoreductase requires a coenzyme
nomenclature. A substrate is that is oxidized or reduced as the
the reactant in an enzyme- substrate is reduced or oxidized.
catalyzed reaction. The Lactate dehydrogenase is an
substrate is the substance oxidoreductase that removes
upon which the enzyme hydrogen atoms from a molecule.
“acts.”

Three important aspects of the

enzyme-naming process are the
following:

1. The suffix -ase identifies a

substance as an enzyme. Thus urease,
sucrase, and lipase are all enzyme
designations. The suffix -in is still
2. A transferase is an enzyme that
found in the names of some of the
catalyzes the transfer of a functional
first enzymes studied, many of which
group from one molecule to another.
are digestive enzymes. Such names
Two major subtypes of transferases
include trypsin, chymotrypsin, and
are transaminases and kinases. A
pepsin.
transaminase catalyzes the transfer of
2. The type of reaction catalyzed an amino group from one molecule to
by an enzyme is often noted with a another. Kinases, which play a major
prefix. An oxidase enzyme catalyzes role in metabolic energy-production
an oxidation reaction, and a hydrolase reactions catalyze the transfer of a
enzyme catalyzes a hydrolysis phosphate group from adenosine
reaction. triphosphate (ATP) to give adenosine
diphosphate (ADP) and a
3. The identity of the substrate is often phosphorylated product (a product
noted in addition to the type of containing an additional phosphate
reaction. Enzyme names of this type group).
include glucose oxidase, pyruvate
carboxylase, and succinate
dehydrogenase. Infrequently, the
substrate but not the reaction type is
given, as in the names urease and
lactase.
3. A hydrolase is an enzyme that product in reactions where
catalyzes a hydrolysis reaction in isomerases are operative.
which the addition of a water
molecule to a bond causes the bond
to break. Hydrolysis reactions are
central to the process of digestion.
Carbohydrases effect the breaking of
glycosidic bonds in oligo and
polysaccharides, proteases effect the
breaking of peptide linkages in
proteins, and lipases effect the
6. A ligase is an enzyme that catalyzes
breaking of ester linkages in
the bonding together of two
triacylglycerols.
molecules into one with the
participation of ATP. ATP involvement
is required because such reactions are
generally energetically unfavorable
and they require the simultaneous
input of energy obtained by a
hydrolysis reaction in which ATP is
4. A lyase is an enzyme that catalyzes converted to ADP.
the addition of a group to a double
bond or the removal of a group to
form a double bond in a manner that
does not involve hydrolysis or
oxidation. A dehydratase effects the
removal of the components of water
from a double bond and a hydratase
effects the addition of the
components of water to a double
bond.
Enzyme Active Site

❑ Studies show that only a small

5. An isomerase is an enzyme that
catalyzes the isomerization
(rearrangement of atoms) of a
substrate in a reaction, converting it
into a molecule isomeric with itself.
There is only one reactant and one
portion of an enzyme molecule
called the active site
participates in the interaction
with a substrate or substrates
during a reaction. The active
site is the relatively small part of
an enzyme’s structure that is
actually involved in catalysis.
The active site in an enzyme is
a three-dimensional entity
formed by groups that come
from different parts of the
protein chain(s); these groups
are brought together by the
folding and bending
 (secondary and tertiary
structure of the protein. The
active site is usually a
“crevicelike” location in the
enzyme
Enzyme–Substrate Complex
❑ Catalysts offer an alternative
pathway with lower activation
energy through which a
reaction
can occur. In enzyme-controlled
reactions, this alternative pathway
involves the formation of an enzyme–
substrate complex as an intermediate
species in the reaction. An enzyme–
substrate complex is the intermediate
reaction species that is formed when
a substrate binds to the active site of
an enzyme. Within the enzyme–
substrate complex, the substrate
encounters more favorable reaction
conditions than if it were free. The
result is faster formation of product.
Lock-and-Key Model
To account for the highly specific way
an enzyme recognizes a substrate
and binds it to the active site,
researchers have proposed several
models. The simplest of these models
is the lock-and-key model.
Induced-Fit Model
The lock-and-key model explains the
action of numerous enzymes. It is,
however, too restrictive for the action
of many other enzymes. Experimental
evidence indicates that many
enzymes have flexibility in their
shapes. They are not rigid and static;
there is constant change in their
shape.
The forces that draw the substrate
into the active site are many of the
same forces that maintain tertiary
structure in the folding of peptide
chains. Electrostatic interactions,
hydrogen bonds, and hydrophobic
interactions all help attract and bind
substrate molecules.
Enzyme Specificity
Enzymes exhibit different levels of
selectivity, or specificity, for
substrates. The degree of enzyme
specificity is determined by the
active site. Some active sites
accommodate only one particular
compound, whereas others can
accommodate a “family” of closely
related compounds. Types of enzyme
specificity include
1. Absolute Specificity. Such
specificity means an enzyme will
catalyze a particular reaction for only
one substrate. This most restrictive of
all specificities is not common. Urease
is an enzyme with absolute specificity.
2. Stereochemical Specificity. Such
specificity means an enzyme can
distinguish between stereoisomers.
Chirality is inherent in an active site,
because amino acids are chiral
compounds. L-Amino-acid oxidase
will catalyze reactions of L-amino
acids but not of D-amino acids.
3. Group Specificity. Such specificity
involves structurally similar
compounds that have same
functional groups. Carboxypeptidase
is group-specific; it cleaves amino
acids, one at a time, from the carboxyl
end of the peptide chain.

4. Linkage Specificity. Such

specificity involves a particular type of
bond, irrespective of the structural
features in the vicinity of the bond.
Phosphatases hydrolyze phosphate–
ester bonds in all types of phosphate
esters. Linkage specificity is the most
general of the specificities considered.

Factors that Affect Enzyme

 Enzyme activity is a measure of

the rate at which an enzyme
converts substrate to products Ph
in biochemical reaction. Four
✓ The pH of an enzyme’s
factors affect enzyme activity:
environment can affect its
temperature, pH, substrat
activity. This is not surprising
concentration, and enzyme
because the charge on acidic
concentration.
and basic amino acids (Section
Temperature 20.2) located at the active site
depends on pH.
 Temperature is a measure of
the kinetic energy (energy of ✓ Optimum pH is the pH at
motion) of molecules. Higher which an enzyme exhibits
temperatures mean molecules maximum activity.
are moving faster and colliding Biochemical buffers help
more frequently. This concept maintain the optimum pH for
applies to collisions between an enzyme.
substrate molecules and
✓ Each enzyme has a
enzymes. As the temperature
characteristic optimum pH,
of an enzymatically catalyzed
which usually falls within the
reaction increases, so does the
physiological pH range of 7.0–
rate (velocity) of the reaction.
7.5.
 The temperature that
✓ A variation from normal pH can
produces maximum activity for
also affect substrates, causing
an enzyme is known as the
either protonation or
optimum temperature for that
deprotonation of groups on the
enzyme. Optimum
substrate. The interaction
temperature is the
between the altered substrate
temperature at which an
and the enzyme active site may
enzyme exhibits maximum
be less efficient than normal—
activity.
or even impossible.

Substrate Concentration
When the concentration of an
enzyme is kept constant and the
concentration of substrate is
increased, the enzyme activity pattern
shown in picture (Figure 21.8). This
activity pattern is called a saturation
curve. Enzyme activity increases up to
a certain substrate concentration and
thereafter remains constant.
What limits enzymatic activity to a
certain maximum value?
As substrate concentration increases,
the point is eventually reached where
enzyme capabilities are used to their
maximum extent. The rate remains
constant from this point on (Figure
21.8). Each substrate must occupy an
enzyme active site for a finite amount
of time, and the products must leave
the site before the cycle can be
repeated. When each enzyme
molecule is working at full capacity,
the incoming substrate molecules
must “wait their turn” for an empty
active site. At this point, the enzyme is
said to be under saturation
conditions.
 The rate at which an enzyme
accepts substrate molecules
and releases product
molecules at substrate
saturation is given by its
turnover number. An enzyme’s
turn over number is the
number of substrate molecules
transformed per minute by one
molecule of enzyme under
optimum conditions of
temperature, pH, and
saturation. The table below
gives turnover numbers for
selected enzymes. Some
enzymes have a much faster
mode of operation than others.
Enzyme Concentration
Because enzymes are not consumed
in the reactions they catalyze, the cell
usually keeps the number of enzymes
low compared with the number of
substrate molecules. This is efficient;
the cell avoids paying the energy
costs of synthesizing and maintaining
a large work force of enzyme
molecules. Thus, in general, the
concentration of substrate in a
reaction is much higher than that of
the enzyme.
If the amount of substrate present is
kept constant and the enzyme
concentration is increased, the
reaction rate increases because more
substrate molecules can be
accommodated in a given amount of
time. A plot of enzyme activity versus
enzyme concentration, at a constant
substrate concentration that is high
relative to enzyme concentration, is
shown in the picture (Figure 21.9). The
greater the enzyme concentration,
the greater the reaction rate.
Extremozymes
An extremozyme is a microorganism
that thrives in extreme environments,
environments in which humans and
most other forms of life could not
survive.
It was not until the 1970s that the
existence of extremophiles was
recognized. Research during the
1980s and 1990s resulted in the
identification of numerous diverse
types of extremophiles found in many
different locations.
The enzymes present in
extremophiles are called
extremozymes. An extremozymes is a
microbial enzyme active at conditions
that would inactive human enzymes
as well as enzymes present in other
types of higher organisms.
The development of commercially
useful enzymes using extremophile
sources involves the following general
approach:
1. Samples containing the
extremophile are gathered
from the extreme environment
where it is found.
2. DNA material is extracted from
the extremophile and
processed.
3. Macroscopic amounts of the
DNA are produced using the
polymerase chain reaction.
4. The macroscopic amount of
DNA is analyzed to identify the
genes present that re involved
in extremozyme production.
5. Genetic engineering
techniques are used to insert
the extremozyme gene into
bacteria, which then produce
the extremozyme.
6. The process is then
commercialized.
Enzyme Inhibition
The rates of enzyme-catalyzed
reactions can be decreased by a
group of substances called
inhibitors. An enzyme inhibitor is a
substance that slows or stops the
normal catalytic
function of an enzyme by binding to
it. In this section, we consider three
modes by which
inhibition takes place: reversible
competitive inhibition, reversible
noncompetitive inhibition, and ❑ Unlike the situation in
irreversible inhibition. competitive inhibition,
increasing the concentration of
A competitive enzyme inhibitor is a
substrate does not completely
molecule that sufficiently resembles
overcome the inhibitory effect
an enzyme substrate in shape and
in this case. However, lowering
charge distribution that it can
the concentration of a
compete with the substrate for
noncompetitive inhibitor
occupancy of the enzyme’s active site.
sufficiently does free up many
enzymes, which then return to
normal activity.

Irreversible Inhibition

Figure 21.10 compares the binding of a
normal substrate and that of a
competitive inhibitor at an enzyme’s
active site. Note that the portions of
these two molecules that bind to the
active site have the same shape but
that the two molecules differ in overall
shape. It is because of this overall
difference in shape that the substrate
reacts at the active site but the
inhibitor does not.
Reversible Noncompetitive
Inhibition
❑ A noncompetitive enzyme
inhibitor is a molecule that
decreases enzyme activity by
binding to a site on an enzyme
other than the active site. The
substrate can still occupy the
active site, but the presence of
the inhibitor causes a change
in the structure of the enzyme
sufficient to prevent the
catalytic groups at the active
site from properly effecting
their catalyzing action.
❑ An irreversible enzyme
inhibitor is a molecule that
inactivates enzymes by
forming a strong covalent
bond to an amino acid side-
chain group at the enzyme’s
active site. In general, such
inhibitors do not have
structures similar to that of the
enzyme’s normal substrate.
The inhibitor–active site bond is
sufficiently strong that addition of
excess substrate does not reverse
the inhibition process. Thus the
enzyme is permanently
deactivated. The actions of
chemical warfare agents (nerve
gases) and organophosphate
insecticides are based on
irreversible inhibition.
The difference between a
 reversible competitive inhibitor
and a reversible noncompetitive
inhibitor.
REGULATION OF ENZYME ACTIVITY
➢ Regulation or enzyme activity
within a cell is necessity for
many reasons. Illustrative of
this need are the following two
situations, both of which
involve the concept of energy
conservation.
1. A cell that continually produces
large amounts of an enzyme
for which substrate
concentration is always very
low is wasting energy. The
production of enzyme needs to
be “turned off”.
2. A product of an enzyme-
catalyzed reaction that is
present in plentiful (more than
needed) amounts in a cell, is a
waste of energy if the enzymes
continues to catalyze the
reaction that produces the
product. The enzyme needs to
be “turned off”.
➢ Many mechanism exist by
which enzymes within a cell
can be “turned on” and “turned
off”. In this section we consider,
in general terms, three such
mechanisms:
1) Feedback control associated
with allosteric enzymes,
2) Proteolytic enzymes and
zymogens, and
3) Covalent modification
Allosteric Enzymes
An allosteric enzyme is an enzyme
with two or more protein chains
(quaternary structure) and two kinds
of binding sites (substrate and
regulator). Many, but not all, of the
enzymes responsible for regulating
cellular processes are allosteric
enzymes. Characteristics of allosteric
enzymes are as follows:
1.) All allosteric enzymes have
quaternary structure; that is, they are
composed of two or more protein
chains.
2.) All allosteric enzymes have two
kinds of binding sites: those for
substrate and those for regulators.
3.) Active and regulatory binding sites
are distinct from each other in both
location and shape. Often the
regulatory site is on one protein chain
and the active site is on another.
4.) Binding of a molecule at the
regulatory site causes changes in the
overall three- dimensional structure
of the enzyme, including structural
changes at the active site.
Substances that bind at regulatory
sites of allosteric enzymes are called
regulators. The binding of a positive
regulator increases enzyme activity;
the shape of the active site is changed
such that it can more readily accept
substrate. The binding of a negative
regulator (a noncompetitive inhibitor)
decreases enzyme activity; changes
to the active site are such that
substrate is less readily accepted.
 Proteolytic Enzymes and Zymogens
Feedback Control
❑ A proteolytic enzyme is an
➢ Feedback control is a process enzyme that catalyzes the
in which activation or inhibition breaking of peptide bonds
of the first reaction in a reaction that maintain the primary
sequence is controlled by a structure of a protein.
product of the reaction Because they would other-
sequence. wise destroy the tissues that
produce them, proteolytic
To illustrate the feedback control
enzymes are generated in an
mechanism, let us consider a
inactive form and then later,
biochemical process within a cell that
when they are needed, are
occurs in several steps, each step
converted to their active form.
catalyzed by a different enzyme.
Most digestive and blood-
To illustrate the feedback control clotting enzymes are
mechanism, let us consider a proteolytic enzymes.
biochemical process
❑ The inactive forms of
within a cell that occurs in several proteolytic enzymes are called
steps, each step catalyzed by a zymogens. A zymogen is the
different enzyme. inactive precursor of a
proteolytic enzyme. (An
alternative, but less often used,
name for a zymogen is
Feedback control is not the only proenzyme.)
mechanism by which an allosteric
enzyme can be regulated; it is just
one of the more common ways.

Regulators of a particular allosteric

enzyme may be products of entirely
different pathways of reaction within
the cell, or they may even be
compounds produced outside the cell
(hormones). Activation of a zymogen requires an
enzyme-controlled reaction that
removes some part of the zymogen
structure. Such modification changes
the three-dimensional structure
(secondary and tertiary structure) of
the zymogen, which affects active site
conformation.

Covalent Modification of Enzymes

✓ A third mechanism for

regulation of enzyme activity
within a cell, called covalent
modification, involves adding
 or removing a group from an
enzyme through the forming
or breaking of a covalent bond.
Covalent modification is a
process in which enzyme
activity is altered by covalently
modifying the structure of the
enzyme through attachment
of a chemical group to or
removal of a chemical group
from a particular amino acid
within the enzyme’s structure.
✓ The most commonly
encountered type of covalent
modification involves the
processes by which a bacteriologist
phosphate group is added to or
removed from an enzyme. The
source of the added phosphate
group is often an ATP molecule.
The process of addition of the
phosphate group to the
enzyme is called
phosphorylation and the
removal of the phosphate
group from the enzyme is
called dephosphorylation. This
phosphorylation/dephosphoryl
ation process is the off/on or
on/off switch for the enzyme.
For some enzymes the active
(“turned-on” form) is the
phosphorylated version of the
enzyme; however, for other
enzymes it is the
dephosphorylated version that
is active.
✓ Glycogen phosphorylase, an
enzyme involved in the
breakdown of glycogen to
glucose is activated by the
addition of a phosphate group.
Glycogen synthase, an enzyme
involved in the synthesis of
glycogen is deactivated by
phosphorylation.
Prescription Drugs That Inhibit
Enzyme Activity
ACE Inhibitors
The acronym ACE stands for
angiotensin-converting enzyme.
Angiotensin is an octapeptide
hormone involved in blood pressure
regulation. It increases blood pressure
by narrowing blood vessels.
Sulfa Drugs
The 1932 discovery of the antibacterial
activity of the compound
sulfanilamide by the German
Gerhard Domagk
(1895–1964) led to the characterization
of a whole family of sulfanilamide
derivatives collectively called sulfa
drugs—the first “antibiotics” in the
medical field.
An antibiotic is a substance that kills
bacteria or inhibits their growth.
Antibiotics exert their action
selectively on bacteria and do not
affect the normal metabolism of the
host organism. Antibiotics usually
inhibit specific enzymes essential to
the life processes of bacteria
Penicillins
✓ Penicillin, one of the most
widely used antibiotics, was
accidentally discovered by
Alexander Fleming in 1928
while he was working with
cultures of an infectious
staphylococcus bacterium. A
decade later, the scientists
Howard Flory and Ernst Chain
isolated penicillin in pure form
and proved its effectiveness as
an antibiotic.
✓ Penicillin’s unique action
depends on two aspects of
enzyme deactivation that we
 have discussed before:
structural similarity to the
enzyme’s natural substrate and
irreversible inhibition. Penicillin
is highly specific in binding to
the active site of
transpeptidase. In this sense, it
acts as a very selective
competitive inhibitor. However,
unlike a normal competitive
inhibitor, once bound to the
active site, the b-lactam ring
opens as the highly reactive
amide bond forms a covalent
bond to a critical serine residue
required for normal catalytic
action. The result is an
irreversibly inhibited
transpeptidase enzyme
Vitamins
Medical Uses of Enzymes
General Characteristics of Vitamins
➢ Enzymes can be used to
diagnose certain diseases.
Although blood serum
contains many enzymes, some
enzymes are not normally
found in the blood but are
produced only inside cells of
certain organs and tissues. The
appearance of these enzymes
in the blood often indicates
that there is tissue damage in
an organ and that cellular
contents are spilling out
(leaking) into the bloodstream.
➢ Enzymes can also be used in
the treatment of diseases. A
recent advance in treating
heart attacks is the use of tissue
plasminogen activator (TPA),
which activates the enzyme
plasminogen. When so
activated, this enzyme
dissolves blood clots in the
heart and often provides
immediate relief.
➢ Another medical use for
enzymes is in clinical laboratory
chemical analysis. For example,
no simple direct test for the
measurement of urea in the
blood is available. However, if
the urea in the blood is
converted to ammonia via the
enzyme urease, the ammonia
produced, which is easily
measured, becomes an
indicator of urea. This blood
urea nitrogen (BUN) test is a
common clinical laboratory
procedure. High urea levels in
the blood indicate kidney
malfunction.
❑ A vitamin is an organic
compound, essential in small
amounts for the proper
functioning of the human
body, that must be obtained
from dietary sources because
the body cannot synthesize it.
❑ Vitamins differ from the major
classes of foods (carbohydrates,
lipids, and proteins) in the
amount required; for vitamins
it is microgram or milligram
quantities per day compared
with 50–200 grams per day for
 the major food categories. To
illustrate the small amount of
vitamins needed by the human
body, consider the
recommended daily allowance
(RDA) of vitamin B12, which is
2.0 micrograms per day for an
adult. Just 1.0 gram of this
vitamin could theoretically
supply the daily needs of
500,000 people. A well-
balanced diet usually meets all
the body’s vitamin
requirements. However,
supplemental vitamins are
often required for women
during pregnancy and for
people recovering from certain
illnesses. One of the most
common myths associated
with the nutritional aspects of
vitamins is that vitamins from
natural sources are superior to
synthetic vitamins.
The spelling of the term vitamin was
originally vitamine, a word derived
from the Latin vita, meaning “life,”and
from the fact that these substances
were all thought to contain the amine
functional group. When this
supposition was found to be false, the
fi nal e was dropped from vitamine,
and the term vitamin came into use.
Some vitamins contain amine
functional groups, but others do not.
There are 13 known vitamins, and
scientists believe that the discovery of
additional vitamins is unlikely. Despite
searches for new vitamins, it has been
over 50 years since the last of the
known vitamins (B12) was discovered.
Strong evidence that the vitamin
family is complete comes from the
fact that many people have lived for
years being fed, intravenously,
solutions containing the known
vitamins and nutrients, and they have
not developed any known vitamin
deficiency disease.
Water Soluble Vitamins: Vitamin C
Vitamin C, which has the simplest
structure of the 13 vitamins, exists in
two active forms in the human body:
an oxidized form and a reduced form.
Humans, monkeys, apes, and guinea
pigs are among the relatively few
species that require
dietary sources of vitamin C. Other
species synthesize vitamin C from
carbohydrates.
Vitamin C’s biosynthesis involves L-
gulonic acid, an acid derivative of the
monosaccharide
L-gulose . L-Gulonic acid is changed
by the enzyme lactonase into a cyclic
ester (lactone, ring closure involves
carbons 1 and 4. An oxidase then
introduces a double bond into the
ring, producing L-ascorbic acid.
The four —OH groups present in
vitamin C’s reduced form are
suggestive of its biosynthetic
monosaccharide (polyhydroxy
aldehyde) origins. Its chemical name,
L-ascorbic acid, correctly indicates
that vitamin C is a weak acid.
Although no carboxyl group is
present, the carbon 3 hydroxyl group
hydrogen atom exhibits acidic
behavior as a result of its attachment
to an unsaturated carbon atom.
In human beings, an intake of 100 mg/
day of vitamin C saturates all body
tissues with the compound. After
tissue saturation, all additional
Vitamin C is rapidly metabolized and
excreted in the urine. The RDA for
vitamin C varies from different
country to country. It is 30mg/day in
Great Britain, 60mg/day in the United
States and Canada, and 75mg/day in
Germany. A variety of fruits and
vegetables have relatively high
vitamin C content.
Important biochemical functions for
vitamin C in the human body include
the following:
1.Collagen Synthesis- Vitamin C
functions as a cosubstrate in the
formation of the structural protein
collagen, which makes up much of
the skin, ligaments, and tendons and
also serves as the matrix on which
bone and teeth are formed.
2. General Antioxidant- Besides
being a specific antioxidant, eral
antioxidant functions for water-
soluble substances in the blood and
other body fluids.
3.Synthesis of Neurotransmitters-
Synthesis of the neurotransmitters
dopamine and norepinephrine from
the amino acid of tyrosine and the
neurotransmitter serotonin from the
amino acid tryptophan depend on the
presence of Vitamin C
Water-Soluble Vitamins: The B
Vitamins
There are eight B vitamins. Our
discussion of them involves four
topics: nomenclature, function,
structural characteristics, and dietary
sources. Much confusion exists about
the B vitamins’ names. Many have
“number” names as well as “word”
names (often several). The preferred
names for the B vitamins (alternative
names in parentheses) are:
1. Thiamin (vitamin B1)
2. Riboflavin (vitamin B2)
3. Niacin (nicotinic acid,
nicotinamide, vitamin B3)
4. Vitamin B6 (pyridoxine, pyridoxal,
pyridoxamine)
5. Folate (folic acid)
6. Vitamin B12 (cobalamin)
7. Pantothenic acid (vitamin B5)
8. Biotin
B vitamin structure is very diverse. The
only common thread among
structures is that all structures, except
that of pantothenic acid, involve
heterocyclic nitrogen ring systems.
The element sulfur is present in two
structures (thiamin and biotin), and
vitamin B12 contains a metal atom
(cobalt). (Biotin does not contain a tin
atom, as the name might imply.)
Table 21.6 gives structural forms for
the eight B vitamins. Note that for two
B vitamins (niacin and vitamin B6),
more than one form of the vitamin
exists.
Thiamin (Vitamin B1)
which contain nitrogen) with the
monosaccharide ribose attached to
the middle ring.
Riboflavin was once called the “yellow
vitamin” because of its color. It’s name
come from its color (flavin means
“yellow” in Latin) and its ribose
component.
Niacin (Vitamin B3)

❑ “Free” thiamin’s structure

consists of a central carbon
atom to which is attached a six-
membered heterocylic amine
and a five-membered
thiazole(sulfur-nitrogen) ring
system. The name thiamin
comes from “thio” which
means “sulfur” and “amine”
which refers to the numerous
amine groups present.
❑ The coenzyme form of the
thiamin is called thiamin
pyrophosphate (TPP),
molecule in which
pyrophosphate group (two
phosphates bonded to each
other) has been attached to the
side chain. The coenzyme TPP
is needed in step 4 of the citric
acid cycle and also in the
conversion of pyruvate to
acetyl CoA.
Niacin occurs in food in two different,
but similar, forms: nicotinic acid and
nicotinamide
The nicotinic acid form of niacin was
first described in 1973, long before the
concept of vitamins was known. It was
prepared by oxidizing nicotine using
nitric acid; hence the name nicotinic
acid. When the biological significance
of nicotinic acid was realized the
name niacin was coined to
a disassociate this vitamin from the
a name nicotine and to avoid the
perception that niacin-rich foods
contain nicotine or that cigarettes
contain vitamins.
Pantothenic Acid (Vitamin B5)

Riboflavin (Vitamin B2)

The name pantothenic acid is based

Riboflavin’s structure involves three
fused six-membered rings (two of
on the Greek word “pantothen”,
which means “from everywhere.” This
vitamin is found in almost every plant
and animal tissue.
Vitamin B6 (Pyridoxine, Pyridoxal,
Pyridoxamine)
Vitamin B6 is a collective term for
three related compounds: pyridoxine
(found in foods of plant origin) and
pyridoxal and pyridoxamine( found in
foods of animal origin).

Biotin( Vitamin B7)

The name cobalamin comes form the
fact that an atom of the metal cobalt
and numerous amine groups are
present in the structure of Vitamin
B12, which is by far the most complex
of all vitamin structures. Vitamin B12 is
unique in that it is the only vitamin
that contains a metal atom.

Biotin is unique among the B vitamins B Vitamin Summary

in that it can be obtained both from
dietary intake and also via biotin-
producing bacteria (microbiota,
hence the name biotin) present in the
human large intestine.
Folate( Vitamin B9)
The following table summarizes the
B-vitamin coenzyme chemistry
presented in this section. In general
terms, vitamin B- containing
coenzymes serve as temporary
carriers of atoms or functional groups
in redox and group transfer reactions
associated with the metabolism of
ingested food in order to obtain
energy from the food.

Several forms of folate are found in

food. All of them have structures that
consist of three parts (1) a nitrogen-
containing double-ring system
(pteridine). (2) paraaminobenzoic acid
(PABA), and (3) one of more residues
of the amino acid glutamate.

Vitamin B12 (Cobalamin)

Fat- Soluble Vitamins
The four fat-soluble vitamins are
designated using the letters A, D, E,
and K. Many of the functions of the
fat-soluble vitamins involve processes
that occur in cell membranes. The
structures of the fat-soluble vitamins
are more hydrocarbon-like, with
fewer functional groups than the
water-soluble vitamins. Their
structures as a whole are nonpolar,
which enhances their solubility in cell
membranes.
Vitamin A
Normal dietary intake provides a
person with both preformed and
precursor forms (pro- vitamin forms)
of vitamin A. Preformed vitamin A
forms are called retinoids. The
retinoids include retinal, retinol, and
retinoic acid.
Foods derived from animals,
including egg yolks and dairy
products, provide compounds (retinyl
esters) that are easily hydrolyzed to
retinoids in the intestine.
Vitamin A has four major functions
in the body.
1. Vision. In the eye, vitamin A (as
retinal) combines with the protein
opsin to form the visual pigment
rhodopsin. Rhodopsin participates in
the conversion of light energy into
nerve impulses that are sent to the
brain. Although vitamin A’s
involvement in the process of vision is
its best-known function (“Eat your
carrots and you’ll see better”), only
0.1% of the body’s vitamin A is found in
the eyes.
2. Regulating Cell Differentiation. Cell
differentiation is the process whereby
immature cells change in structure
and function to become specialized
cells. For example, some immature
bone marrow cells differentiate into
white blood cells and others into red
blood cells. In the cellular
differentiation process, vitamin A (as
retinoic acid) binds to protein
receptors; these vitamin A–protein
receptor complexes then bind to
regulatory regions of DNA molecules.
3. Maintenance of the Health of
Epithelial Tissues. Epithelial tissue
covers outer body surfaces as well as
lining internal cavities and tubes. It
includes skin and the linings of the
mouth, stomach, lungs, vagina, and
bladder. Lack of vitamin A (as retinoic
acid) causes such surfaces to become
drier and harder than normal. Vitamin
A’s role here is related to cellular
differentiation involving mucus-
secreting cells.
4. Reproduction and Growth. In men,
vitamin A participates in sperm
development. In women, normal fetal
development during pregnancy
requires vitamin A. In both cases, it is
the retinoic acid form of vitamin A
that is needed. Again vitamin A’s role
is related to cellular differentiation
processes.
Vitamin D
The two most important members of
the vitamin D family of molecules are
vitamin D3 (cholecalciferol) and
vitamin D2 (ergocalciferol). Vitamin
D3 is produced in the skin of humans
and animals by the action of sunlight
(ultraviolet light) on its precursor
molecule, the cholesterol derivative 7-
dehydrocholesterol (a normal
metabolite of cholesterol found in the
skin).
❑ The principal function of
vitamin D is to maintain normal
blood levels of calcium ion and
phosphate ion so that bones
can absorb these ions. Vitamin
D stimulates absorption of
these ions from the
gastrointestinal tract and aids
in their retention by the
kidneys.
❑ Vitamin D triggers the
deposition of calcium salts into
the organic matrix of bones by
activating the biosynthesis of
calcium-binding proteins.
Vitamin E
There are four forms of vitamin E:
alpha-, beta-, delta-, and gamma-
tocopherol. These forms differ from
each other structurally in what
substituents (9CH3 or 9H) are present
at two positions on an aromatic ring.
The tocopherol form with the greatest
biochemical activity is alpha-
tocopherol, the vitamin E form in
which methyl groups are present at
both the R and R positions on the
aromatic ring. Gamma-tocopherol is
the main form of vitamin E in vitamin-
E rich foods.
A most important location in the
human body where vitamin E exerts
its antioxidant effect is the lungs,
where exposure of cells to oxygen
(and air pollutants) is greatest. Both
red and white blood cells that pass
through the lungs, as well as the cells
of the lung tissue itself, benefit from
vitamin E’s protective effect.
Infants, particularly premature
infants, do not have a lot of vitamin E,
which is passed from the mother to
the infant only in the last weeks of
pregnancy. Often, premature infants
require oxygen supplementation for
the purpose of controlling respiratory
distress. In such situations, vitamin E
is administered to the infant along
with oxygen to give antioxidant
protection.
Vitamin K
Like the other fat-soluble vitamins,
vitamin K has more than one form.
Structurally, all forms have a
methylated naphthoquinone
structure to which a long side chain of
carbon atoms is attached. The various
forms differ structurally in the length
and degree of unsaturation of the side
chain.
Vitamin K1, also called phylloquinone,
has a side chain that is predominantly
saturated; only one carbon–carbon
double bond is present. It is a
substance found in plants. Vitamin K2
has several forms, called
menaquinones, with the various
forms differing in the length of the
side chain. Menaquinone side chains
have several carbon–carbon double
bonds, in contrast to the one carbon–
carbon double bond present in
phylloquinone. Vitamin K2 is found in
animals and humans and can be
synthesized by bacteria, including
those found in the human intestinal
tract.

Typically, about half of the human

body’s vitamin K is synthesized by
intestinal bacteria and half comes
from the diet. Menaquinones are the
form of vitamin K found in vitamin K
supplements. Only leafy green
vegetables such as spinach and
cabbage are particularly rich in
vitamin K. Other vegetables such as
peas and tomatoes and animal
tissues, including liver, contain lesser
amounts.