ENZYME

Ns. Shila Wisnasari, S.Kep., M.Biomed

Basic Nursing Department
School of Nursing Faculty of Medicine
Universitas Brawijaya

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Contents

Nomenclature and Type of Enzyme

Roles of Enzymes

Action of Enzyme
Mechanism of Enzyme Action

Model of Enzyme-Substrate Complex Formation

Co-enzyme and Co-factor

Factors Affecting Enzyme Action

Enzyme Inhibition

Uses of Enzyme
 Introduction

Biochemical reactions ALWAYS occur in the body

ENZIM
Introduction

Substances on which
enzymes act to convert
them into products

Catalysts of biological systems

(hence are called as biocatalysts),
colloidal, thermolabile and protein
in nature
 Nomenclature and Type of Enzyme

• Enzymes are generally named after adding the

suffix ‘ase’ to the name of the substrate  enzymes
acting on nucleic acids are known as nucleases
• few exceptions  trypsin, pepsin, and chymotrypsin
are still in use
• few enzymes exist in their inactive forms 
proenzymes or zymogens
e.g. pepsin has pepsinogen as its zymogen
• Many times the active form of enzyme acts on
zymogen and catalyses its conversion into active
form and this process is called as autocatalysis
 Nomenclature and Type of Enzyme

International Union of Biochemistry

(IUB) nomenclature system

Each enzyme is characterized by a code number (enzyme code No

or EC No) comprising four digits separated by points
 1st : class
 2nd : subclass
 3rd : sub-subclass
 4th : specific name
E.C. 2.7.1.1 ATP:D-Hexose 6-phosphotransferase

Specific name : Hexokinase

Sub-subclass 1 : Alcohol is the phosphate acceptor

Subclass 7 : Transfer of phosphate

Class 2 : Transferase
 Nomenclature and Type of Enzyme

Classes of Enzyme
Enzyme Enzyme Type of Reaction
Code Class
(E.C)
1 Oxidoreductases catalyze oxidations and reductions

2 Transferases catalyze transfer of groups from a donor

molecule to an acceptor molecule
3 Hydrolases catalyze the hydrolytic cleavage of C-C, C-O,
C-N, P-O and certain other bonds
4 Lyases catalyze cleavage of C-C, C-O, C-N, and
other bonds by elimination, leaving double
bonds, and also add groups to double bonds
5 Isomerases catalyze geometric or structural changes
within a single molecule
6 Ligases catalyze the joining together of two
molecules, coupled to the hydrolysis of a
pyrophosphoryl group in ATP or a similar
nucleoside triphosphate
 6 Types / Classes of Enzyme

1. OXIDOREDUCTASE 2. TRANSFERASE
 6 Types / Classes of Enzyme

3. HIDROLASE 4. LYASE
 6 Types / Classes of Enzyme

5. ISOMERASE 6. LIGASE
 Roles of Enzymes

 Breakdown of nutrient  energy

 protein building blocks, DNA, etc
 Energy usage for cells motility and
muscles contraction
 Action of Enzymes

 Specific
 Determine the pattern of chemical
transformations
 Mediate the transformation of different
forms of energy
 Under strict regulation in a variety of ways
 most
 Act as a catalyst  increases reaction rate
up to 106 times
Enzyme Mechanism of Action

Collision Theory

Particles must
collide with one
another in order
to react

Most collision fails to

produce products
Enzyme Mechanism of Action
 Enzyme Mechanism of Action

Collision Theory
The molecules need to have enough energy, enough
speed to break and form new bonds when they collide

The minimum
energy required
for a reaction to
occur

Enzymes have immense catalytic power and accelerate reactions

at least a million times, by reducing the energy of activation
Enzyme Mechanism of Action

Collision Theory
 Enzyme Mechanism of Action

Michaelis and Menten hypothesis for enzyme action

E + S  ES  E + P

Intermediate/transient
complex
Enzyme Mechanism of Action

An enzyme-catalyzed reaction takes a different ‘route’

Model of Enzyme-Substrate Complex
Formation

Lock and Key

Model of Enzyme-Substrate Complex
Formation

Lock and Key

 Model of Enzyme-Substrate Complex
Formation

Induced fit
 Model of Enzyme-Substrate Complex
Formation

Induced fit
 Co-enzymes and Co-factors

All the enzymes are protein in nature with large molecular

weight, except ribozymes (RNA molecules with enzymatic
activity)
 Co-enzyme and Co-factor

Co-enzyme

 specific, thermostable, low molecular weight,

non-protein organic substance
 carrier molecule
 may bind covalently or non- covalently to the
apoenzyme

Membawa
elektron
 Co-enzyme and Co-factor

Co-enzyme

Co-enzymes can be classified according to the group

whose transfer they facilitate

For transfer of groups

For transfer of hydrogen
other than hydrogen
• NAD+, NADP+ • Sugar phosphates
• FMN, FAD • CoASH
• Lipoic acid • Thiamine pyrophosphate
• Coenzyme Q (TPP)
• Pyridoxal phosphate
• Folate coenzymes
• Biotin
• Cobamide coenzyme
• Lipoic acid
 Co-enzyme and Co-factor

Co-factor
 Terlibat dalam proses katalisis
 Menstabilkan enzim atau substrat
 Magnesium (Mg), zat besi (Fe), zinc (Zn)
 Non organik
 Co-enzyme and Co-factor

Role of Metal Ions in Enzymes Co-factor

help in either maintaining or producing (or both), active structural
conformation of the enzyme

Formation of enzyme-substrate complex

Making structural changes in substrate molecule

Accept or donate electrons

Activating or functioning as nucleophiles

Formation of ternary complexes with enzyme or substrate

 Factors Affecting Enzyme Action

 Enzim dapat bekerja secara optimal dalam

kondisi lingkungan tertentu
 Lingkungan  pH dan temperature
Factors Affecting Enzyme Action

Effect Temperature
of pH

Substrate and Product Concentration

Enzyme Concentration

Activators and Coenzymes

Modulators and Inhibitors

Time
 Factors Affecting Enzyme Action

Temperature

 Enzyme function optimally at a particular temperature

 Optimum temperature  temperature at which the
activity of the enzyme is maximum (35–40°C)
 Temperature ↓  enzyme activity ↓
 Temperature ↑  kinetic energy ↑, collision ↑
 Semakin tinggi temperature  energy yang diserap >>
reaksi lebih banyak
 Suhu terlalu tinggi  kerusakan struktur (denaturasi)
dan kehilangan fungsi
Factors Affecting Enzyme Action

Temperature
Factors Affecting Enzyme Action

pH  The enzymatic activity is

maximum at a particular
pH which is called its
optimum pH. The
optimum pH of most
enzymes lies in the range
of 4–9
 Terlalu asam/basa 
denaturasi enzim 
muatan electron pada
active site berubah 
ikatan berubah 
struktur berubah 
substrat tidak dapat
berikatan dengan enzim
 Factors Affecting Enzyme Action

Substrate and Product

Concentration

 Need to be enough substrate around

 Substrate <<  reaction rate <<
 Product >>  reaction rate <<
 Factors Affecting Enzyme Action

Enzyme Concentration

 Increasing Enzyme Concentration will

increase the rate of reaction, as
more enzymes will be colliding with
substrate molecules.
 Factors Affecting Enzyme Action

Effect of Activators and

Coenzymes

 The activity of certain enzymes is greatly

dependent of metal ion activators and
coenzymes
Factors Affecting Enzyme Action

Effect of Activators and

Coenzymes
Metal Enzymes

Copper Superoxide dismutase, cytochrome oxidase,

tyrosinase, lysyl oxidase
Calcium Lipase, lecithinase

Iron Catalase, xanthine oxidase, peroxidase cytochrome

oxidase.
Manganese Hexokinase, enolase, phosphoglucomutase, glycosyl
transferase
Magnesium Hexokinase, enolase, glucose-6-phosphatase,
phosphofructokinase
Molybdenum Xanthine oxidase

Zinc Carbonic anhydrase, alcohol dehydrogenase,

carboxy peptidase, alkaline phosphatase (ALP),
lactate dehydrogenase (LDH)
 Factors Affecting Enzyme Action

Effect of Modulators and

Inhibitors

 Whenever the active site is not available for

the binding of the substrate the enzyme
activity may be reduced
 The substances which stop or modify the
enzymatic reaction are called inhibitors or
modulator
 Factors Affecting Enzyme Action

Effect of Time

 The time required for completion of an

enzyme reaction increases with decreases
in temperature from its optimum
 However under the optimum conditions of
pH and temperature, time required for
enzymatic reaction is less
 Enzyme Inhibition

 Enzymes can be inactivated by the agents that

denature them
 The chemical substances which inactivate the
enzymes are called as inhibitors and the
process is called as enzyme inhibition
Enzyme Inhibition

Competitive inhibition
 Enzyme Inhibition

Competitive inhibition
 Reversible
 Increase in substrate concentration  reaction
“reoccurs”
 E.g.: ACE inhibitor
 Enzyme Inhibition

Noncompetitive Inhibition

• If the inhibitor can be removed from its site of

binding without affecting the activity of the enzyme
 Reversible-Non-competitive Inhibition
• If the inhibitor can be removed only at the loss of
enzymatic activity  Irreversible Non-competitive
Inhibition
 glyceraldehyde-3-phosphate
NAD+ + Pi Glyceraldehyde-3-phosphate
NADH + H+ Dehydrogenase
1,3-bisphosphoglycerate
ADP
Phosphoglycerate Kinase
ATP
3-phosphoglycerate
Phosphoglycerate Mutase
2-phosphoglycerate

H2O Enolase
phosphoenolpyruvate
ADP
Pyruvate Kinase Alanine
ATP
pyruvate
 Enzyme Inhibition

Allosteric Competitive
Inhibition

the inhibitor binds to the enzyme at a site other than

the active site but on a different region in the enzyme
molecule  allosteric site
 glucose Glycolysis
ATP
Hexokinase
ADP
glucose-6-phosphate
Phosphoglucose Isomerase
fructose-6-phosphate
ATP
Phosphofructokinase ATP
ADP
fructose-1,6-bisphosphate
Aldolase

glyceraldehyde-3-phosphate + dihydroxyacetone-phosphate
Triosephosphate
Isomerase
Glycolysis continued
Uses of Enzymes

Enzymes estimation in serum and body

fluids for diagnosis and prognosis

Enzyme used as laboratory reagent

Therapeutic uses of enzymes

 Uses of Enzyme

Enzymes for diagnosis and prognosis

 Uses of Enzyme

Enzymes for diagnosis and prognosis

Uses of Enzyme

Serum Enzymes In
Muscle Diseases

S-GOT/S-
Serum Enzymes In
GPT
Gi Tract Diseases
Aldolase
Serum
Amylase
CPK

Serum
Lipase
 Uses of Enzyme

Serum Enzymes In Liver Diseases

Serum Transaminases (SGOT/SGPT)

Serum Alkaline Phosphatase

Serum 5’-Nucleotidase

Serum Lactate Dehydrogenase (LDH)

Serum Isocitrate Dehydrogenase (ICD)

Serum Cholinesterases

Serum ornithine carbamoyl transferase

(OCT)
 Uses of Enzyme

Enzyme used as laboratory reagent

“Glucose oxidase” enzyme is used for
estimation of “true glucose” in blood and
body fluids.
Enzyme “uricase” is used for estimation
of serum uric acid.
Enzyme “urease” is used for estimation
of urea in blood and body fluids.
 Uses of Enzyme

Therapeutic uses of enzymes

 Uses of Enzyme

Therapeutic uses of enzymes

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