GENERAL CHARACTERISTICS OF
ENZYMES different biological changes.
ENZYMES
- Is a compound, usually a protein, that acts
as a catalyst for biochemical reaction.
- Each cell in the human body contains
thousands of different enzymes because
almost every reaction in the cell requires
its own specific enzyme.
- Enzymes cause cellular reactions to occur
millions of times faster than corresponding
uncatalyzed reactions.
- As catalyst, enzymes are not consumed
during the reaction but merely help in the
reaction occur more rapidly.
- Are chemical substance which hastens
chemical reaction without being affected in
the process.
- Are secreted by living cells and are
complex organic chemical compounds with
definite structure.
- Like the inorganic catalysts, enzymes have
the remarkable property of speeding up
chemical reactions without being
themselves affected in the process.
As a result, they can be use over and over
again.
- Catalysts or enzymes are responsible for
- They make up the largest and most
highly specialized class of proteins.
- The catalytic efficiency of enzyme is so
high that per mole is around 10,000 to
10,000,000 moles of substance per
minute.
- The catalytic action of enzymes is the key
to their importance, for by facilitating
chemical changes, enzymes make
possible the continuous replacement
and renewal processes of all living
organisms.
- The word ENZYME comes from a Greek
word EN, which means “IN” and ZYME,
which means “YEAST”.
YEAST
Long before, yeast is used in the production of
bread and alcoholic beverages.
- Yeast reaction to sugar produces the
carbon dioxide gas that causes the bread
to rise.
- Fermentation of sugars in fruit juice using
the yeast enzymes produces alcoholic
beverages.
EARLY ENZYMES DISCOVERIES
JON JAKOB BERZELIUS – 1835 Swedish
Chemist, termed their chemical action – catalytic.
JAMES B. SUMMER of Cornell +University –
Isolate and crystallize the enzymes urease from
the jack bean.
JOHN H. NORTHROP and WENDELL M.
STANLEY – They discovered a complex
procedure for isolating and purifying pepsin.
ENZYME STRUCTURE
A. Simple Enzymes
Is an enzyme composed only of
protein (amino acid chains)
B. Conjugated Enzymes
 Is an enzyme that has a nonprotein
part in addition to protein part.
 APOENZYME is the protein part of
a conjugated enzymes.
 COFACTOR Is the nonprotein part
of the conjugated enzymes.
 HOLOENZYME Is the
biochemically active conjugated
enzymes produced from an
apoenzyme and a cofactor.
Apoenzyme + Cofactor = Holoenzymes
Why do apoenzyme need cofactor? - CONENZYME is a small organic molecule PROSTHETIC GROUP – The nonprotein
that serves as a cofactor in conjugated component, tightly bound to the apoenzyme by
- Cofactors provide additional chemically
enzyme. covalent bonds is called a prosthetic group.
reactive functional group besides those
- COENZYME is synthesized within the
present in the amino acid side chains of NOMENCLATURE AND CLASSIFICATION
human body using building blocks from the
apoenzymes. OF ENZYMES
nutrients.
APOENZYME and HOLOENZYME o Most often, one of these building
blocks is a B vitamin or B
- The enzyme without its non-protein moiety vitamin derivatives.
is termed as apoenzyme and it is inactive. o Vitamins must be obtained
- Holoenzyme is an active enzyme with its through dietary intake.
nonprotein component. - Many cofactors are permanently bonded,
TWO BROAD CATEGORIES OF COFACTOR: via covalent bond, to the amino acids
portion of enzymes.
A. Simple Metal Ions
- Breaking the covalent bond deactivates Enzymes – are most commonly named by using
B. Small Organic Molecules
the enzymes. a system that attempts to provide information
METAL IONS COFACTOR o Ex. Coenzymes FAD which has about the function (rather than the structure) of
riboflavin (a B vitamin) the enzymes.
- Include Zn, Mg, Fe, and Cu. o Coenzymes NAD which has niacin
- All metal ions must be supplied to human (a B vitamin) - The type of reaction catalyzed, and the
body through dietary mineral intake. substrate identify are focal points in
- Almost any type of diet will provide TYPES OF COFACTORS nomenclature.
adequate amounts of needed metallic - A substrate is the reactant in an enzyme-
COENZYMES – The nonprotein component, catalyzed reaction. The substrate is the
cofactors because they are needed in very
loosely bound to apoenzyme by non-covalent substances upon which the enzymes
small (trace) amounts.
bond. “acts”.
SMALL ORGANIC MOLECULES
Examples: vitamins or compound derived Three important aspects of the enzymes-naming
from vitamins. process are the following:
- The second category of cofactors, as a
group, are called COENZYMES.
1. The suffix ASE identifies the substance
as an enzyme.
a. Thus urease, surcease and lipase
are all enzymes designation.
b. The suffix IN is still found in the
names of some of the first enzymes
studied, many of which are
digestive enzymes.
i. Ex. Trypsin, chymotrypsin,
and pepsin.
2. The type of reaction catalyzed by an
enzyme is often noted with a prefix.
a. An oxidase enzyme catalyzes an
oxidation.
b. A hydrolase enzyme catalyzes a
hydrolysis reaction.
3. The identity of the substrate is often
noted in addition to the type of
reaction.
a. Enzymes names of this type include
glucose oxidase, pyruvate
carboxylase, and succinate
dehydrogenase.
b. In frequently, the substrate but not
the reaction types are given, as in
the name’s urease and lactase.
c. In these names, the reaction
involved is hydrolysis; urease
catalyzes the hydrolysis of urea,
lactase the hydrolysis of lactose.
Enzymes – are grouped into six major classes CLASSIFICATION OF ENZYMES
(EC Number Classification) by the International
Union of Biochemists (I.U.R). On the basis of
types of reactions, they catalyze.
PRINCIPLE OF THE INTERNATIONAL
CLASSIFICATION
Each enzyme has classification number
consisting of four digits:
Example EC: (2.7.1.1) HEXOKINASE
EC: (2.7.1.1) these components indicate the
following groups of enzymes:
2 is class (TRANSFERASE) 1. OXIDOREDUCTASE – Is an enzyme that
catalyzes an oxidation-reduction
7 is subclass (TRASFER OF PHOSPHATE)
reaction.
1 is sub subclass (ALCOHOL IS PHOSPHATE
ACCEPTOR)
1 specific name: ATP, D-HEXOSE-6-
PHOSPHOTRANSFERASE (HEXOKINASE)
An organic oxidation reaction is an oxidation
that increases the number of C-O bonds and/or
decreases the of C-H bonds.
An organic reduction reaction is a reduction that
decreases the number of C-O bonds and/or
increases the number of C-H bonds.
The oxidation-reduction are not independent Kinases which play a major role in metabolic  Catalyze the hydrolysis of various bonds
processes but linked processes that must occur energy-production reactions, catalyzes the add water across a bond.
together. transfer of a phosphate group from adenosine
EXAMPLES:
triphosphate (ATP) give adenosine diphosphate
An oxidoreductase requires a coenzyme that is
(ADP) and phosphorylated products (a  Protein Hydrolyzing Enzymes
oxidized or reduced as the substrate is reduced
phosphate containing an additional phosphate). (Peptidases)
or oxidized.
 Carbohydrases (Amylase, Maltase,
EX. Lactase Dehydrogenase is an Lactase)
oxidoreductase that removes hydrogen atom  Lipid Hydrolyzing Enzymes (Lipase)
from a molecule.  Deaminases
2. TRANSFERASE – Is an enzyme that  Phosphatases
catalyzes the transfer of a functional group
from one molecule to another.

BIOCHEMICAL ACTIVITY: 3. HYDROLASE – Is an enzyme that

catalyzes a hydrolysis reaction in which
 Transfer a functional group (e.g., methyl or
the addition of a water molecule to a
phosphate) between donor and acceptor
molecule to a bond causes the bond to
molecules.
break.
EXAMPLES: 4. LYASES – Is an enzyme that catalyzes the
Hydrolysis Reactions – are central to the addition of a group to a double bond or the
 Transaminases (ALT & AST) process of digestion. removal of a group to form a double bond
 Phosphotransferases (Kinases) in a monomer that does not involve
Carbohydrates effect the breaking of glycosidic
 Transmethylases bonds in oligo and polysaccharides. hydrolysis or oxidation.
 Transpeptidases
Proteases effect the breaking of peptide linkages A dehydratase effects the removal of the
 Transacylases
in protein. components of water from a double bond.
Two major subtypes of transferase are
Lipases effect the breaking of ester linkages in Hydratase effects the addition of the components
transaminases and kinases.
triacylglycerol’s. of water to a double bond.
Transaminase catalyzes the transfer of amino
BIOCHEMICAL ACTIVITY: BIOCHEMICAL ACTIVITY:
group from one molecule to another.
  Cleave various bonds by means other
than hydrolysis and oxidation.
 Add water, ammonia or carbon dioxide
across double bonds, or remove these
elements to produce double bonds.
EXAMPLES:
 Fumarase
 Carbonic Anhydrase
5. 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 product in
reactions where isomerases are operative.
Isomerases – are a general class of enzymes
which convert a molecule from one isomer to
another. The general form of such a reaction is as
follows: A-B – B-A.
BIOCHEMICAL ACTIVITY:
 Catalyze isomerization changes within a
single molecule.
 Carry out many kinds of isomerization:
o L to D isomerization
 Many kinds of isomerization
o L to D isomerization
o Mutase reactions (shifts of chemical
groups)
EXAMPLES:
 Isomerase
 Mutase
6. LIGASES – Is an enzyme that catalyzes
the bonding together of two molecules into
one with the participation of ATP.
ATP involvement is required because such
reaction is generally energetically unfavorable,
and they required the simultaneous input of
energy obtained by a hydrolysis reaction in which
ATP is converted to ADP.
BIOCHEMICAL ACTIVITY:
 Join two molecules with covalent bonds
catalyze reactions in which two chemical
groups are joined (or ligated) with the use
of energy from ATP.
EXAMPLES:
 Acetyl-CoA Carboxylase
 Glutamine Synthetase
 Ligases (Synthetases)
 Catalyze ligation or joining of two
substrates.
 Require chemical energy (e.g., ATP)
7. TRANSLOCASES – catalyzing the
translocation of hydrogen ions, inorganic
cations and anions, amino acids,
carbohydrates or other compounds.