Enzymes

Definition
Biological catalysts which speed up the rate
of reaction without becoming part of the
reaction but themselves cannot initiate any
chemical reaction.
Increase the rate of reaction by lowering the
energy of activation
Importance
 Enzymes play an important role in
Metabolism, Diagnosis, and
Therapeutics.
 All biochemical reactions are enzyme
catalyzed in the living organism.
 Level of enzyme in blood are of
diagnostic importance e.g. it is a good
indicator in disease such as myocardial
infarction.
 Enzyme can be used therapeutically
such as digestive enzymes.
Nomenclature
Enzymes :
First name is of substrate
second, ending in “ASE” indicating type of
reaction catalyzed.
Clarify the reaction , e.g. Malic Enzyme
L- Malate + NAD  Pyruvate + NADH-H + CO2
Malate NAD oxidoreductase (Decarboxylating)
 TRIVAL NAME

 Gives no idea of source, function or reaction

catalyzed by the enzyme.
 Example: trypsin, thrombin, pepsin.
 SYSTEMATIC NAME

According to the International union Of Biochemistry an

enzyme name has two parts:
-First part is the name of the substrates for the enzyme.
-Second part is the type of reaction catalyzed by the
enzyme.This part ends with the suffix “ase”.
Example: Lactate dehydrogenase
 CLASSIFICATION OF ENZYMES

Formulated by the enzyme commission of I.U.B six major

classes based on the type of reactions catalyzed.

1. Oxidoreductases
 Catalyzing oxidation reduction reactions
2. Transferases
 Catalyzing group transfer
3. Hydrolases
 Catalyzing hydrolytic breakdown
4. Lyases
 Catalysing removal of groups by mechanism other than hydrolysis and
leaving behind double bonds
5. Isomerases
 Catalysing interconversion of isomers
6. Ligases
 Catalysing formation of bonds and new compounds
 1. Oxidoreductases

Catalyzing oxidation reduction reaction where one

substrate is oxidized and other is reduced

Oxidases. Catalyzing oxidation of the substrate and

atomic oxygen acts as recipient of hydrogen e.g.
Ascorbic acid oxidase, Cytochrome oxidase, Tyrosinase

Ascorbic acid
Oxidase
Ascorbic acid + O2 Dehydro ascorbic acid
 Aerobic Dehydrogenases.

Catalyzing oxidation of the substrate and molecular

oxygen acts as recipients of hydrogen e.g. Glucose
oxidase, L amino acid dehydrogenase, Xanthene
dehydrogenase

glucose oxidase
Glucose Gluconolactone
Anaerobic Dehydrogenases. Catalyzing oxidation of the
substrate and coenzymes act as recipients of hydrogen e.g.
Lactate Dehydrogenase with NAD and Glucose 6
phosphate dehydrogenase with NADP

Lactate
dehydrogenase
Lactic acid Pyruvic acid
+ NAD + NADH – H+
Oxygenases:
Is an enzyme that oxidizes a substrate by transferring
the oxygen from molecular oxygen O2 (as in air) to it.
Types :

a. Monooxygenases:
Transfer one oxygen atom to the substrate, and reduce
the other oxygen atom to water.
b. Dioxygenases:
Incorporate both atoms of molecular oxygen (O2) into the
product(s) of the reaction.
Among the most important monooxygenases are
the cytochrome P450 oxidases, responsible for breaking
down numerous chemicals in the body.
 2.TRANSFERASES
Transaminases. Catalyzing transfer of amino group between an
amino acid and a ketoacid e.g. Aspartate transaminase (AST),
Alanine transaminase (ALT)
Aspartate
transaminase (AST)
Glutamic acid +  ketoglutaric acid +
Oxalo acetic acid Aspartic acid

Alanine
transaminase (ALT)
Glutamic acid +  ketoglutaric acid +
Pyruvic acid Alanine
Transmethylases. Catalyzing transfer of methyl group between to
substrates e.g. COMT
Catechol-O-
methyltransferase (COMT)
Noradrenalin Adrenaline
+ CH3
Transpeptidases. Catalyzing transfer of amino acids to substrates
e.g. Benzyl-SCoA transpeptidase

Benzyl-SCoA
transpeptidase
Benzyl - SCoA Hippuric acid
+ Glycine
Phosphotransferases. Catalyzing transfer of phosphate
group to substrates e.g. Hexokinase, glucokinase

2.7.1.1 ATP D hexose 6 phosphotransferase [Hexokinase]

ATP + Glucose Hexokinase ADP + D-Glucose –6-P
Acetyltransferase. Catalyzing transfer of acetyl group to
substrates e.g. choline acetyltransferase
Acetyl-CoA+ Choline  CoA + Acetyl- Choline
 3. HYDROLASES
Catalysing hydrolytic breakdown of different bonds. Most of the GIT
enzymes belong to this class
Enzymes hydrolyzing carbohydrates
1. Polysaccharidases
Starch Amylase Maltose, maltotrios, dextrins

2. Oligosaccharidases
Dextrins Dextrinase glucose

3. Disacharidases
Maltose, Lactose, Sucrose Disacharidases Maltase, Lactase, Sucrase monosaccharides
Enzymes Hydrolyzing Lipids
Triacyl glycerol lipase monoacyl glycerol + 2 F.F.A

Cholesterol ester cholesterol free cholesterol + FFA

esterase
Phospholipids Phospholipase lysophospholipids

Lecithin Lysolecithin
Enzymes Acting on Peptide Bonds:

exopeptidases carboxypeptidase amino acids

endopeptidase aminopeptidases e. g pepsin (smaller peptides)

Tripeptidase : Tripeptide  A.A
Dipeptidase : Dipeptide  A.A
Phosphatases
1. Phosphomonoesterases:
Glucose – 6.P. + H2O Phosphatase G 6. Phosphate Glucose +Pi

2. Phosphodiesterases:
Removal of phosphate Group of diesters breakdown of 3’-5’
p linkages in cyclic AMP
 4. LYASES
 Catalysing reactions in which groups are removed without
hydrolysis leaving a double bond or add groups to already existing
double bonds.

CH3. CO. COOH CH3. CHO+ CO2

(pyruvate) pyruvate decarboxylase (acetaldehyde)

COOH.CH = CH. COOH Fumerase COOH-CHOH. CH2-COOH

(Fumaric acid) (malic acid)
5. ISOMERASES
 Involved in inter conversion of pair of isomeric compounds

 Glucose 6. P Phosphogluco mutase glucose I.P

 Glucose 6.P Phosphohexose isomerase Fructose 6.P

 All trans retinene Retinene 11- CIS retinene

Isomerase
 6. LIGASES
 Catalyze reactions in which linking together of two
molecules occur coupled with the breakdown of a high
energy phosphate bonds like ATP, GTP
Acetate + CoA +ATP Acetyl CoA Acetyl CoA+AMP
Synthetase

Succinate + CoA + ATP Succinyl CoA Succinyl CoA + ADP+ Pi

Synthetase

Pyruvate + CO2 + ATP Pyruvate Oxaloacetate + ADP + Pi

Carboxylase

Fatty acid + CoA + ATP Acyl CoA Acyl CoA (Activated fatty acid) + AMP + PiPi
Synthetase
 UNIQUE FEATURES
 Enzyme-catalyzed reactions have very high catalytic
efficiency.
 Enzymes have a high degree of specificity for their
substrates.
 Enzymatic activities are highly regulated in response to
the external changes.
 HIGH SPECIFICITY

Unlike conventional catalysts, enzymes

demonstrate the ability to distinguish
different substrates. There are three
types of substrate specificities.
 Absolute specificity
 Relative specificity
 Stereospecificity
ABSOLUTE SPECIFICITY
Enzymes can recognize only one type of
substrate and implement their catalytic
functions.
NH2 urease
O C + H2O 2NH3 + CO2
NH2
urea

NH CH3
O C + H2O
NH2

methyl urea
RELATIVE SPECIFICITY
Enzymes catalyze one class of substrates or one kind
of chemical bond in the same type.

protein kinase A To phopharylate the -OH group of serine

protein kinase C and threonine in the substrate proteins,
leading to the activation of proteins.
protein kinase G
 1
CH2OH CH2OH
H O H O H
sucrose H 1
OH H H OH
OH O CH2OH
H OH OH H
CH2OH
OH O H sucrase
H 1
OH H 1
H O CH2 CH2OH
H O H O H
H OH H 1 OH
OH H H
raffinose OH O CH2OH
H OH OH H
 Stereospecificity
The enzyme can act on only one form of
isomers of the substrates.
H H

C C
OH COOH
H3C COOH H3C OH

B B C
A C A

LACTATE DEHYDROGENASE CAN RECOGNIZE ONLY

THE L-FORM BUT NOT THE D-FORM LACTATE.
 ACTIVE CENTER
 Almost all the enzymes are proteins having well defined
structures.
 Some functional groups are close enough in space to
form a portion called the active center.
 Active centers look like a cleft or a crevice.
 Active centers are hydrophobic.
TWO ESSENTIAL GROUPS

The active center has two essential

groups in general.

• Binding group: to associate with the

reactants to form an enzyme-substrate
complex
• Catalytic group: to catalyze the
reactions and convert substrates into
products
 Protein chain

Substrate
molecule
Essential groups
outside the
active center
+ Catalytic group
-
Active center

Binding group
 MOLECULAR COMPONENTS
 Simple enzymes: consists of only one peptide chain
 Conjugated enzymes:
holoenzyme = apoenzyme + cofactor
(protein) (non-protein)

 Cofactors: metal ions; small organic molecules

 METAL IONS

 Metal-activated enzyme: ions necessary but loosely

bound. Often found in metal-activated enzyme.
 Metalloenzymes: Ions tightly bound.
 Particularly in the active center, transfer electrons,
bridge the enzyme and substrates, stabilize enzyme
conformation, neutralize the anions.
ORGANIC COMPOUNDS

 Small size and chemically stable compounds

 Transferring electrons, protons and other groups
 Vitamin-like or vitamin-containing molecule
COENZYMES
 Loosely bind to apoenzyme. Be able to be separated
with dialysis.
 Accepting H+ or group and leaving to transfer it to
others, or vise versa.

Prosthetic groups

• Tightly bind through either covalent or

many non-covalent interactions.
• Remained bound to the apoenzyme during
the course of reaction.
MECHANISM OF ENZYME-
CATALYZED REACTIONS
To understand the molecular details of
the catalyzed reaction.

 Proximity and orientation arrangement

 Multielement catalysis

 Surface effect
 Lock-and-key model

Both E and S are rigid and fixed, so they must

be complementary to each other perfectly in
order to have a right match.
 Induced-fit model

The binding induces conformational changes

of both E and S, forcing them to get a perfect
match.