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enzymes.
General Characteristics of Enzyme
1.) A simple enzyme is an
❑ An enzyme is a compound, enzyme composed only of protein
usually protein, that acts as a (amino acid chains).
catalyst for a bio-chemical
reaction. 2.) A conjugated enzyme is an
enzyme that has a nonprotein part in
❑ Each cell in the human body addition to a protein part.
contains thousands of different
enzymes because almost every ✓ An apoenzyme is the protein
reaction in a cell requires its part of a conjugated enzyme. A
own specific enzyme. Enzymes cofactor is the nonprotein part
cause cellular reactions to of a conjugated enzyme.
occur millions of times faster ✓ A holoenzyme is the
than corresponding biochemically active
uncatalyzed reactions. conjugated enzyme produced
❑ Enzymes are not consumed from an apoenzyme and a
during the reaction but merely cofactor. Apoenzyme + cofactor
help the reaction occur more = holoenzyme
rapidly. The word enzyme Why do apoenzymes need cofactors?
comes from the Greek words
en which means ‘in’ and zyme Cofactors provide additional
which means ‘yeast’ chemically reactive functional
groups besides those present
in the amino acid side chains of
❑ Most enzymes are globular apoenzymes.
proteins. It was thought that all It is generally either a small
enzymes are proteins in 1980’s organic molecule or an
A few enzymes are that are inorganic ion (usually a metal
now know are made up of ion).
ribonucleic acid (RNA).
Enzymes undergo all reactions Coenzyme is a small organic
of proteins, including molecule that serves as a
denaturation. Slight cofactor in a conjugated
alterations in pH or enzyme. Typical inorganic ion
temperature can affect cofactors include Zn^2 +
enzyme activity drastically. The Mg^2+, Mn^2+, and Fe^2+. The
biochemist must exercise nonmetallic CI° ion
extreme caution in handling occasionally acts as a cofactor.
enzymes to avoid loss of their Dietary minerals are an
activity. important source of inorganic
ion cofactors.
Enzyme Structure
5. Genetic engineering
techniques are used to insert
the extremozyme gene into
bacteria, which then produce
the extremozyme.
Extremozymes
6. The process is then
An extremozyme is a microorganism commercialized.
that thrives in extreme environments,
Enzyme Inhibition
environments in which humans and
most other forms of life could not The rates of enzyme-catalyzed
survive. reactions can be decreased by a
group of substances called
It was not until the 1970s that the
existence of extremophiles was inhibitors. An enzyme inhibitor is a
recognized. Research during the substance that slows or stops the
1980s and 1990s resulted in the normal catalytic
identification of numerous diverse
function of an enzyme by binding to
types of extremophiles found in many
it. In this section, we consider three
different locations.
modes by which
The enzymes present in
inhibition takes place: reversible
extremophiles are called
competitive inhibition, reversible
extremozymes. An extremozymes is a
microbial enzyme active at conditions
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
❑ 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
Figure 21.10 compares the binding of a active site. In general, such
normal substrate and that of a inhibitors do not have
competitive inhibitor at an enzyme’s structures similar to that of the
active site. Note that the portions of enzyme’s normal substrate.
these two molecules that bind to the
active site have the same shape but
that the two molecules differ in overall The inhibitor–active site bond is
shape. It is because of this overall sufficiently strong that addition of
difference in shape that the substrate excess substrate does not reverse
reacts at the active site but the the inhibition process. Thus the
inhibitor does not. enzyme is permanently
deactivated. The actions of
chemical warfare agents (nerve
Reversible Noncompetitive gases) and organophosphate
Inhibition insecticides are based on
❑ A noncompetitive enzyme irreversible inhibition.
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. The difference between a
reversible competitive inhibitor 2) Proteolytic enzymes and
and a reversible noncompetitive zymogens, and
inhibitor.
3) Covalent modification
Allosteric Enzymes
Vitamins
Medical Uses of Enzymes
General Characteristics of Vitamins
➢ Enzymes can be used to
diagnose certain diseases. ❑ A vitamin is an organic
Although blood serum compound, essential in small
contains many enzymes, some amounts for the proper
enzymes are not normally functioning of the human
found in the blood but are body, that must be obtained
produced only inside cells of from dietary sources because
certain organs and tissues. The the body cannot synthesize it.
appearance of these enzymes ❑ Vitamins differ from the major
in the blood often indicates classes of foods (carbohydrates,
that there is tissue damage in lipids, and proteins) in the
an organ and that cellular amount required; for vitamins
contents are spilling out it is microgram or milligram
(leaking) into the bloodstream. 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 There are 13 known vitamins, and
the body’s vitamin scientists believe that the discovery of
requirements. However, additional vitamins is unlikely. Despite
supplemental vitamins are searches for new vitamins, it has been
often required for women over 50 years since the last of the
during pregnancy and for known vitamins (B12) was discovered.
people recovering from certain Strong evidence that the vitamin
illnesses. One of the most family is complete comes from the
common myths associated fact that many people have lived for
with the nutritional aspects of years being fed, intravenously,
vitamins is that vitamins from solutions containing the known
natural sources are superior to vitamins and nutrients, and they have
synthetic vitamins. not developed any known vitamin
deficiency disease.
The spelling of the term vitamin was
originally vitamine, a word derived Water Soluble Vitamins: Vitamin C
from the Latin vita, meaning “life,”and
from the fact that these substances Vitamin C, which has the simplest
were all thought to contain the amine structure of the 13 vitamins, exists in
functional group. When this two active forms in the human body:
supposition was found to be false, the an oxidized form and a reduced form.
fi nal e was dropped from vitamine, Humans, monkeys, apes, and guinea
and the term vitamin came into use. pigs are among the relatively few
Some vitamins contain amine species that require
functional groups, but others do not.
dietary sources of vitamin C. Other
species synthesize vitamin C from
carbohydrates.
3.Synthesis of Neurotransmitters-
Synthesis of the neurotransmitters
dopamine and norepinephrine from
the amino acid of tyrosine and the
The four —OH groups present in neurotransmitter serotonin from the
vitamin C’s reduced form are amino acid tryptophan depend on the
suggestive of its biosynthetic presence of Vitamin C
monosaccharide (polyhydroxy Water-Soluble Vitamins: The B
aldehyde) origins. Its chemical name, Vitamins
L-ascorbic acid, correctly indicates
that vitamin C is a weak acid. There are eight B vitamins. Our
Although no carboxyl group is discussion of them involves four
present, the carbon 3 hydroxyl group topics: nomenclature, function,
hydrogen atom exhibits acidic structural characteristics, and dietary
behavior as a result of its attachment sources. Much confusion exists about
to an unsaturated carbon atom. the B vitamins’ names. Many have
“number” names as well as “word”
In human beings, an intake of 100 mg/ names (often several). The preferred
day of vitamin C saturates all body names for the B vitamins (alternative
tissues with the compound. After names in parentheses) are:
tissue saturation, all additional
Vitamin C is rapidly metabolized and 1. Thiamin (vitamin B1)
excreted in the urine. The RDA for
2. Riboflavin (vitamin B2)
vitamin C varies from different
country to country. It is 30mg/day in 3. Niacin (nicotinic acid,
Great Britain, 60mg/day in the United nicotinamide, vitamin B3)
States and Canada, and 75mg/day in
4. Vitamin B6 (pyridoxine, pyridoxal,
Germany. A variety of fruits and
pyridoxamine)
vegetables have relatively high
vitamin C content. 5. Folate (folic acid)
Important biochemical functions for 6. Vitamin B12 (cobalamin)
vitamin C in the human body include
the following: 7. Pantothenic acid (vitamin B5)