Enzymes

By: Engr. Vera Marie L. Lanaria

What are enzymes?
Proteins that are capable of catalyzing
a reaction in which various substrate
are converted to products through the
formation of an intermediate enzymesubstrate complex.
Source of enzyme?
They are produced by living cells
(animals, plants, microorganisms) and
are absolutely essential as catalyst in
biochemical reactions
Function of an enzyme?
As a catalyst, it will increase the rate
of reaction without them undergoing
permanent chemical changes.
The catalytic ability of enzymes is due
to its particular protein structure
Advantages..
1. Very efficient catalysts
2. Environmentally acceptable
3. Act under mild conditions
4. Highly specific
Disadvantages.
1. Provided by nature in only one
enantiomeric form
2. Require narrow operation
parameters
3. Display their highest activities in
water
4. Prone to inhibition phenomena
5. May cause allergies
6. May be expensive
Nomenclature of Enzymes
Originally enzymes were given nondescriptive names such as:
rennin: curding of milk to start
cheese-

making process
pepsin: hydrolyzes proteins at acidic
pH
trypsin: hydrolyzes proteins at
alkaline pH
1. Later, it was improved by adding
the suffix
ase to the name of the substrate
with which the enzymes functions, or
to the reaction that is catalyzed.
Example:
lactase: lactose glucose +
galactose
lipase: fat fatty acids + glycerol
maltase: maltose glucose
urease: urea + water 2NH3 + CO2
cellobiase: cellobiose glucose
2. Reaction which is catalyzed + ase
Ex. glucose isomerase:
glucose to fructose
glucose oxidase:
D-glucose + O2 + H2O to gluconic
acid
lactic acid dehydrogenase:
lactic acid to pyruvic acid
New Scheme in Nomenclature
By 1964, the International Enzyme
Commission suggested that enzymes
will be categorize into 6 major classes:
1) oxidoreductases
2) transferases
3) hydrolases
4) lyases
5) isomerases
6) ligases
EC 1 Oxidoreductases
Involved in redox reactions in which
hydrogen, oxygen atoms or electrons
are transferred between molecules
Ex.
EC 1.1.3.4 Glucose Oxidase

-D-glucose + O2 to D-glucose-1, 5lactone

+ hydrogen
peroxide
EC 2 Transferases
Catalyze the transfer of an atom or
group of atoms between two
molecules, but excluding such
transfers classified in the other groups
(e.g. oxidoreductases and hydrolases)
Ex. EC 2.6.1.1 Aspartate
Aminotransferases
L-aspartate: 2-oxoglutarate
aminotransferases
EC 3 Hydrolases
Involved in hydrolytic reactions and
their reversal
Ex. EC 3.4.23.4 Chymosin (also
known
as
rennin)
k-casein + H2O para-k-casein +
caseino
macropeptide
EC 4 Lyases
Involved in elimination reactions in
which a group of atoms is removed
from the substrate, often leaving
double bonds
Ex. EC 4.3.1.3 Histidine AmmoniaLyase

L-histidine urocanate + ammonia

EC 5 Isomerases
Catalyze molecular isomerizations
Include epimerases, racemases, and
intramolecular transferases
Ex. EC 5.3.1.5 Xylose Isomerases
-D-glucopyranose -Dfructofuranose
EC 6 Ligases
Involved in the formation of a covalent
bond joining two molecules together,
coupled with the hydrolysis of a
nucleoside triphosphate
Ex. EC 6.3.2.3 Glutathione
Synthetase
ATP + L-glutamyl-L-cysteine +
glycine
ADP + phosphate + glutathione
Units of Enzyme Activity
Katal - the amount of enzyme needed
to produce 1 mole of product per
second under standard conditions
U - The amount of enzyme needed to
produce 1 mole of product per minute
under standard conditions
1 Kat = 60,000,000 U