ENZYME

dr. JANGKI HASHUMAL

DEPARTEMENT OF BIOCHEMISTRY
FACULTY OF MEDICINE
HASANUDDIN UNIVERSITY
DEFINITION
NOMENCLATURE AND CLASSIFICATION
ENZYME-SUBSTRATE INTERACTION
COFACTOR AND COENZYME
EFFECT OF pH TEMPERATURE
SPECIFIC ENZYME EXAMPLE
 DEFINITION
Enzyme is a biological catalyst
Biological → living system
Catalyst → a substance that increase the
rate (velocity) of a chemical reactions
without itself being changed in the overall
process
Biological catalyst
Typically are very large protein
Permit reactions to go at conditions that
the body can tolerate
Can process millions of molecules every
second
Are very specific → react with one or only
a few types of molecules (substrate)
Substrate is a substance that is acted on
by an enzyme
 NOMENCLATURE AND
CLASSIFICATION
Enzyme nomenclature is based on :
What it reacts with
How it reacts
Add –ase ending
Examples :
Lactase : enzyme that reacts with lactose
Pyruvate decarboxylase : removes carboxyl
from pyruvate
Enzyme usually written in trivial name but every
enzyme has an official name from International
Union of Biochemistry (Enzyme Nomenclature
1992)
Based on the official nomenclature system, each
enzyme has a full name and an enzyme
commission number (E.C) derived in the position
in the classification scheme
Example :
Hexokinase has the full name ATP: D-hexose 6-
phosphotransferase and the classification
number E.C 2.7.1.1
Classification of enzymes
Based on type of reaction, enzymes have
been classified to six major classes as
follows :
1.Oxidoreductases : catalyze oxidation-
reduction reactions
2.Transferases : catalyze trnasfer of
functional groups fron one molecule to
another
3.Hydrolases : catalyze hydrolytic cleavage
4. Lyases : catalyze removal of a group
from or addition of a group to a double
bond, or other cleavages involving
electron rearrangment
5. Isomerases : catalyzed intramoleculer
rearrangement
6. Ligases : catalyzed reactions in which
two molecules are joined
 ENZYME-SUBSTRATE
INTERACTION
UNCATALYZED REACTION
Effect of enzyme on
E activation energy :
N ΔG‡
E SUBSTRATE
All reaction must get
R over the activation
G PRODUCT
energy hurdle
Y

VELOCITY
CATALYZED REACTION Enzyme change how
a reaction will
proceed
E
N
Enzyme reduces the
E
R Substrate
activation energy
G
Y Product And it makes the
reaction faster
VELOCITY
Effect of substrate concentration:
For non-catalyzed reaction:
Reaction rate increase with concentration
For enzyme catalyzed reaction :
Also increase, but only to a certain point
Vmax- maximum velocity
At Vmax, the enzyme is working as fast as possible
Characteristics of enzyme active site
Catalytic site
Where the reaction actually occurs
Binding site
Area that holds substrate in proper place
Enzymes uses weak, non-covalent
interactions to hold substrate in place
based on R groups of amino acids
Sites are pockets or cleft on the enzyme
surface
Steps in an enzyme reaction

Enzyme and substrate combine to form a

complex
Complex goes through a transition state
A complex of
the enzyme and
the product is
produced
The enzyme
and product
separate
Characteristic of enzyme active site
Lock and key model
Picture by Emil Fisher (1890)
This model assumed that only a substrate
of the proper shape could fit with the
enzyme
Induced-fit model
Proposed by Daniel Koshland (1958)
This model assumes continuous changes in
active site structure as a substrate binds
This model recognizes that there is much
flexibility in an
enzyme’s structure
According to this
model, an enzyme
is able to conform
to a substrate
COFACTORS AND COENZYMES

A nonprotein component of enzymes is called

the cofactor. Cofactors can be either organic or
inorganic compounds .If the cofactor is organic,
then it is called a coenzyme. Coenzymes are
relatively small molecules compared to the
protein part of the enzyme. Many of the
coenzymes are derived from vitamins. The
inorganic cofactors commonly are metal ions.
(e.g. Ca, Cu, Co, Fe)
Enzymes that require a cofactor, but do
not have one bound are called
apoenzyme. An apoenzyme together with
its cofactor(s) is called a holoenzyme (i.e.,
the active form)

COENZYME + SUBSTRATE NO PRODUCT

APOENZYME + SUBSTRATE NO PRODUCT

APOENZYME + COENZYME + SUBSTRATE PRODUCT

HOLOENZYME
Some vitamins that are often converted to coenzymes :

Vitamin Coenzyme Function

B1 (Thiamine) Thiamine Decarboxylation
pyrophosphate
B2 (Riboflavin) Flavin adenine Carries hydrogen
dinucleotide (FAD)
B3 (Niacin) Nicotinamide Oxidation or
adenine hydrogen transfer
dinucleotide (NAD)
Folic acid Tetrahydrofolic acid Amino acid
metabolism
Pantothenic acid Coenzyme A Acyl group carrier
 EFFECT OF pH & TEMPERATURE ON
ENZYMATIC REACTIONS

Exceeding normal pH
and normal temperature
ranges always reduces
enzyme reactions rates
Temperature
Optimum temperature is
usually 25-40ºC
For pH, most enzymes
work near pH 7
pH
SPECIFIC ENZYME EXAMPLE
CHYMOTRYPSIN
A proteolytic enzyme
Digestion of dietary protein in small intestine
Initially produced in an active form (zymogen) :
chymotrypsinogen; and actived by tripsin
Chymotripsin only works on amino acids
containing an aromatic ring (phenylalanin,
tyrosine, tryptophan)
 CONCLUSION
ENZYME DEFENITION
ENZYME NOMENCLATURE AND
CLASSIFICATION
ENZYME-SUBSTRATE INTERACTION
COFACTOR AND COENZYME
EFFECT OF pH TEMPERATURE
 REFERENCES
Brownie AC, Kernohan JC. Biochemistry. A
core text with self-assesment. Churchill
Livingstone, 1999.
Campbell PN, Smith AD. Biochemistry
Illustrated 4th ed. Churchill Livingstone, 2000.
Mathews CK, van Holde KE, Ahren KG.
Biochemistry 3th ed, Addison-Wesley
Publishing Company, 2000.
Swaminathan R. Handbook of Clinical
Biochemistry. New Delhi. Oxford University
Press, 2004.