ENZYMES

CHEMICAL REACTIONS

• In order for chemical reactions to take place, enzymes

must be present to help speed up the reaction.
• Chemical bonds connect to atoms to make molecules.
• Chemical reactions can do two things
– They can join atoms to make molecules
– They can break bonds in molecules
• The sum of he chemical reactions that takes place
within a cell is referred as the cell’s metabolism
ENZYMES
• Enzymes are proteins that act as biological catalyst
– Catalysts-speeds up chemical reactions
– Enzymes-speed up chemical reactions in living
things
CHEMICAL REACTIONS

• The molecules or atoms at the beginning of chemical

reactions are called reactants
• The materials produced by the chemical reaction are
called products
Structure and Functions of
Enzymes
• A substrate is the molecule that the enzyme changes
– It is the reactant a chemical reaction controlled by
an enzyme
• Each enzymes has an active site which
is the place where the enzyme
and substrate attached
 Structure and Functions of
Enzymes
• During a chemical reaction the enzyme helps he reactant
turn into product, however the enzymes is not changed
• Enzyme can be used over and over again
Product
Reactant/Substrate
Products are
released
Enzymes ready for
more

Substrate moves towards No change in the shape

active site of enzymes to catalyze
next reaction
• Enzymes are superior to other catalysts in several
ways:
• 1. They have a much greater catalytic power.

• CO 2 + H 2 O carbonic anhydrase H 2 CO 3
• 2. Enzymes are highly specific with varying degrees of
specifity.
– Absolute specifity – they act on one substrate and only on that
substrate.
– Stereospecifity – such enzymes that can detect the difference
between optical isomers (mirror images) and select only one of such
isomers.
– Reaction specifity – enzymes that catalyze certain types of reactions.
– Group specifity – enzymes that catalyzes a group of substances that
contain specific compounds.
ENZYMES SPECIFICITY
• enzymes are very specific- this means that each enzyme
can only on one substrate
– For example
• maltase only breaks down maltose
• Lipase only works on certain lipids
• Protease only works in certain proteins
• Does a specific enzyme work on more than one substrate?
– NO
ENZYMES SPECIFICITY
• Therefore, it needs thousand of enzymes for
thousands of chemical reactions in the body
• The names of many enzymes (amylase, lipase, Pepsin,
trypsin) usually ends in ase or in
• 3. The activity of enzymes is closely regulated,
whereas the catalyst is difficult to control.
 Enzymes and Their Environment
• Enzymes are proteins and therefore undergo all the
reactions that proteins do.
• That is, enzymes can be coagulated by heat, alcohol,
strong acids, and alkaloidal reagents.
Enzymes and Their Environment

• Temperature Requirement
– The higher the temperature, the faster the rate of
reaction.
– The best temperature for enzyme function – the
temperature at which the rate of a reaction
involving an enzyme is the greatest – is called the
“optimum temperature”.
Enzymes and Their Environment

• Role of pH Each enzyme has a pH range within which it

can best function.
• This is called “optimum pH range” for that particular
enzyme.
• For example, the optimum pH range of pepsin, an
enzyme found in gastric juice, is approximately 2.0,
whereas the optimum pH range of trypsin, an enzyme
found in pancreatic juice, is near 8.2.
Enzymes and Their Environment

• Effect of Concentration
– As with the all chemical reactions, the speed is increased
with an increase in concentration of reactants.
– With an increased concentration of substrate, the rate of
the reaction will increase until available enzyme becomes
saturated with substrate.
– Also with an increase in the amount of enzyme, the rate of
reaction will increase, assuming an unlimited supply of
substrate.
ACTIVATORS and INHIBITORS

• Activators – inorganic substances that tend to increase

the activity of enzyme.
• Inhibitors – any substance that will make the enzyme
less active or render it inactive.
– Competitive inhibitors – binds reversibly in the active
site and so block the access by the substrate.
– Incompetitive inhibitors – bind to another site on the
enzyme to render it less active or inactiv
ACTIVATORS and INHIBITORS

• Irreversible inhibitors – form strong covalent bonds

with the enzymes, rendering it inactive. This effect
can’t be overcome by increasing the concentration of
the substrate.
 ACTIVATORS and INHIBITORS
• Poisons
– Many enzymes inhibitors are poisonous because their effect on
enzyme activity.
– Mercury and Lead compounds are poisonous because they react
with sulfhydryl groups ( - SH) of an enzymes and so change its
conformation.
– The subsequent loss of enzyme activity leads to the various
symptoms of lead and mercury poisoning, such as loss of
equilibrium, hearing, sight, and touch, which are generally
irreversible.
ACTIVATORS and INHIBITORS
• Drugs
– While some enzyme inhibitors are poisonous, others are
beneficial to life.
– Pencillin acts as an enzyme inhibitor for transpeptide, a
substance that bacteria need to build their cell walls. If the cell
wall is lacking, osmotic pressure causes the bacterial cell to
burst and die.
– However, new strains of bacteria have developed an enzyme,
penicillinase, that inactivates penicillin.
– To destroy these new strains, synthetically modified penicillins
have been prepared so that this antibiotic remains effective.
ACTIVATORS and INHIBITORS
ACTIVATORS and INHIBITORS
ACTIVATORS and INHIBITORS

• Lock-and key Model Wherein the substrate must

“fit” into the active site of the enzyme – hence the
specifity of the enzyme.
ACTIVATORS and INHIBITORS

• Induced-Fit Model
– Suggests that the active
site is not rigid as the
Lock-and-Key Model,
but flexible. That is, the
site changes in
conformation upon
binding to a substrate in
order to yield an
enzyme-substrate fit.
APOENZYMES and COENZYMES

• Other enzymes are conjugated proteins – they

contain a protein and non-protein part.
• Both parts must be present before the enzyme can
function.
– The protein part is called the “apoenzyme” and
the non-protein (organic part) is called
“coenzyme”
APOENZYMES and COENZYMES

• Coenzymes
– are not proteins and so are not inactivated by heat.
Examples of coenzymes are the vitamins or compounds
derived from vitamins. The reaction involving a coenzyme
can be written as follows:
• coenzyme + apoenzyme = enzyme

– Coenzyme A is essential in the metabolism of

carbohydrates, lipids, and proteins in the body.
NOMENCLATURE

• Formerly enzyme were given names ending in “-in”.

– With no relation being an indicator between the
enzyme and the substance it affects – the
substrate.
• The current system for naming enzymes uses the
name of the substrate or the type of reaction
involved, with the ending “-ase”.
NOMENCLATURE
CLASSIFICATION
• Oxidoreductases – are enzymes that catalyze oxidation-
reduction reactions between two substrates. The
enzymes of the oxidation- reduction reactions in the
body are important because these reactions are
responsible for the production of heat and energy.
• Transferases – are enzymes that catalyze the transfer of a
functional group between two substrates.
CLASSIFICATION
• Hydrolases – hydrolytic enzymes – catalyze the
hydrolysis of carbohydrates, esters and proteins.

• Lyases – are enzymes that catalyzes the removal of

groups from substrates by means other than
hydrolysis, usually with the formation of double
bonds.
CLASSIFICATION
• Isomerases – are enzymes that catalyze the
interconversion of cis-trans isomers.

• Ligases – or synthetases, are enzymes that catalyze

the coupling of two compounds with breaking of
pyrophosphate bonds.
ENZYMES of the KIDNEY

• If an individual’s blood pressure drops, as in the case of

hemorrhaging or in hypokalemia, the kidneys secrete the
enzyme renin (sometimes considered as a hormone) into
the bloodstream.
– angiotensinogen renin angiotensin I converting enzyme angiotensin II
• Angiotensin II increases the force of the heartbeat and
constricts the arterioles, thus causing an increase in
blood pressure.
ENZYMES of the KIDNEY

• Angiotensin II brings about the contraction of

smooth muscle and also triggers the release of the
hormone aldosterone which aids in the retention of
water.
• Actually, angiotensin I is the most powerful
vasoconstrictor known. It is an octapeptide;
Angiotensin I is a decapeptide.
ENZYMES of the KIDNEY

• Other kidney enzymes include glucose-6-phosphatase ,

which is involved in the removal of the phosphate group
from glucose-6-phosphate, thereby enabling glucose to
diffuse from the cell into the blood stream;
• Glutaminase , which is involved in the conversion of
glutamine into glutamic acid and NH4+ ; and a
• hydroxylase , which is involved in the synthesis of
calcitriol.
CHEMOTHERAPY
• Chemotherapy is the use of chemicals to destroy
infectious microorganisms and cancerous cells
without damaging the host’s cells.
• These chemicals function by inhibiting certain
cellular enzyme reactions.
• Among the chemotherapeutic agents are the
antibiotics and the antimetabolites.
CHEMOTHERAPY
• Antibiotics – are compounds produced by one
microorganisms that are toxic to another
microorganisms. Among the most commonly used
are the penicillin and tetracyclin .
CHEMOTHERAPY
• Antimetabolites – are chemicals that have structures
closely related to those of the substrate enzymes act
on, thus inhibiting enzyme activity. Mercaptopurine
are used in the treatment of leukemias. Some are
antibiotics
CLINICAL SIGNIFICANCE OF PLASMA ENZYME
CONCENTRATIONS

• The measurement of plasma enzyme levels can be of

great diagnostic value. Many other plasma enzymes
are useful in the diagnosis of various diseases.
CLINICAL SIGNIFICANCE OF PLASMA
ENZYME CONCENTRATIONS
CLINICAL SIGNIFICANCE OF PLASMA
ENZYME CONCENTRATIONS
ISOZYMES

• Isozymes or Isoenzymes
– are enzymes with the same function but slightly
different structural features.
– The reason for their existence is not unknown, but
they are made use of clinically.
– Lactate dehydrogenase (LDH), creatine kinase , and
alkaline phosphatase all occur in isoenzyme form and
are diagnostic value. LDH has five forms.
CLINICAL SIGNIFICANCE OF PLASMA
ENZYME CONCENTRATIONS
LACTOSE INTOLERANCE
• Lactose Intolerance Individuals who cannot eat
food containing lactose are said to be lactose
intolerant .
• They lack enzyme lactase, which is requires for
the hydrolysis of lactose.
• As a result, lactose acCumulates in the
intestinal tract and pulls water out of the
tissues by osmosis. This is turn causes
abdominal cramps, distention, and diarrhea.
LACTOSE INTOLERANCE
• To overcome such an effect today, an
individual may take Lactaid orally to
supply the missing enzyme.