GENERAL CHARACTERISTICS OF ENZYME

• Came from Greek word “en” which means in and “zyme” which means yeast.
Ex: bread and alcoholic beverages
• Enzymes are catalysts and are not consumed in the reactions
• Enzymes are proteins that act as catalyst for biochemical reactions
• The human body has 1000s enzymes
• Enzymes are the MOST EFFECTIVE catalysts known
• TRYPSIN- hydrolyzes peptide bonds of lysine and arginine
• UREASE – hydrolyzes only urea
• Most enzymes are globular proteins, some are simple CHONs and conjugated
CHONs
• A few enzymes are known to be RIBONUCLEIC ACIDS (RNA)
• Enzymes undergo all the reactions of proteins including DENATURATION.
-hyperthermia

• Enzyme activity is dramatically affected by:

1. Alterations in pH happens when there’s a change in temperature low pH

(7.0-7.5)- maximum activity of majority of enzymes

LOW pH of 2.0 best functioning level for PEPSIN

HIGH pH of 8.0 best functioning for TRYPSIN

2. TEMPERATURE increase in temperature ALSO increase rate of reaction

OPTIMUM TEMPERATURE—> 37 Degree Celsius

⁃ Bacterial enzymes NEEDS high temperature—> autoclave of instruments

3. Other protein denaturants (enzyme and substance concentration)

ENZYME STRUCTURE
Enzymes are of 2 types
• SIMPLE ENZYME
• composed only of protein (amino acid chains)

• CONJUGATED ENZYME
• Has a NONPROTEIN part in addition to a protein part.
• APOENZYME
= protein part of a conjugated enzyme.
• COFACTOR
= nonprotein part of a conjugated enzyme
• HOLOENZYME
= biochemically active conjugated enzyme
= Apoenzyme + Cofactor
COFACTORS
• Important for the chemically reactive enzymes
• Small ORGANIC molecules or INORGANIC ions
• ORAGANIC MOLECULE COFACTORS
• Co- Enzymes or Co- Substrates derived from DIETARY VITAMINS.

• INORGANIC ION COFACTORS

= derived from DIETARY MINERALS

• Typical Metal Ion cofactors

Zn2+, Mg2+, Mn2+ and Fe2+

• Nonmetallic Ion Cofactor

Cl-

ENZYME CATALYSIS
TRYPSIN—> catalyses the hydrolysis of peptide bonds formed by carboxyl group of
lysine and arginine.

OXIDOREDUCTASE
- an oxidoreductase enzyme catalyses an OXIDATION-REDUCTION reaction:
> Oxidation and Reduction reactions are ALWAYS linked to one another
> An oxidoreductase requires a coenzyme that is either Oxidized or Reduced as
the substrate in the reaction.
Example: Lactate dehydrogenase—> is an oxidoreductase

LYASE
- Is an enzyme that catalyses 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.
Example:
Dehydratase—> effects the removal of the components of water from a double
bond.
Hydratase—> effects the addition of the components of water to double bonds.
Aconitase
ISOMERASE AND LIGASES
- An Isomerase is an enzyme that catalyses the isomerization (REARRANGEMENT OF
ATOMS) reactions
Example: Phosphohexose Isomerase
-A Ligase is an enzyme that catalyses the formation of a bond between 2 molecules
involving ATP HYDROLYSIS:
> ATP HYDROLYSIS—> is required because such reactions are
ENERGETICALLY UNFAVOURABLE
> Require the simultaneous input of energy obtained by a hydrolysis of
ATP to ADP
Example: Tryosine-tRNA synthesise

TRANSFERASE
- An enzyme that catalyses the transfer of a functional group from one molecule to
another
TWO MAJOR SUBTYPES:
1. Transaminases—> catalyse transfer of amino group to a substrate.

2. Kinases—> catalyse transfer of phosphate group from ATP to a substrate.

3. Aspartate Amino Transferase

HYDROLASE
- an enzyme that catalyses a hydrolysis reaction
- the reaction involves ADDITION OF A WATER MOLECULE to a bond to cause BOND
BREAKAGE.
- Hydrolysis reactions are central to the PROCESS OF DIGESTION:
1. Carbohydrase—> hydrolyse glycosidic bonds in oligo and polysaccharides
2. Proteases—> breakage of peptide linkages in proteins
3. Lipases—> effect the breaking of ester bonds in triacylglycerols
 4. Acetylcholinesterease

SIX MAJOR CLASSES

- enzymes re grouped into 6 major classes based on the types of reactions they
catalyse.

1. Oxidoreductase
—> Osxidation-reductions
2. Transferase
—> Functional group transfer reactions
3. Hydrolases
—> Hydrolysis reactions
4. Lyases
—> reactions involving addition or removal of groups from double
bonds
5. Isomerase
—> Isomerisation reactions
6. Ligases
—> reactions involving bond formation coupled WITH ATP
hydrolysis

NOMENCLATURE AND CLASSIFICATION OF ENZYMES

3 Important Aspects of the Naming Process

1. Suffix –ase identifies it is an ENZYME

E.g, Urease, sucrose and lipase

Exception: the suffix –in is still found in the names of some digestive enzymes. E.g:
trypsin, chymotrypsin, pepsin

2. Type of reaction catalyzed by an enzyme is often used as a prefix

OXIDASE catalyzes the oxidation reaction
HYDROLASE catalyzes hydrolysis reaction
DEHYDROGENASE dehy

3. Identify of substrate is often used in addition to the type of reaction

E.g, Glucose oxidase, pyruvate carboxylase and succinate dehydrogenase

ENZYME TERMINOLOGIES:
APOENZYME
- PROTEIN PART of an enzyme

COFACTOR
- NONPROTEIN PORTION of an enzyme that is necessary for catalytic
function
example: metal ions (Zn2+ and Mg2+)

COENZYME
- nonprotein organic molecule, frequent in a VITAMIN B, that acts as a
cofactor

SUBSTRATE
- the compound or compounds whose reaction an enzyme catalyses

ACTIVE SITE
- SPECIFIC portion of the enzyme to which a substrate BINDS during
reaction

ACTIVATION
- any process that initiates or increases the activity of an enzyme

INHIBITION
- any process that makes an enzyme LESS ACTIVE or INACTIVE

COMPETITIVE INHIBITOR
- a substance that binds to the active site of an enzyme thereby preventing
binding to substrate.

NONCOMPETITIVE INHIBITOR
- any substances that binds to a portion of an enzyme other than the
active site and thereby inhibits the activity of the enzyme.