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

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

Basic Nursing Department
School of Nursing Faculty of Medicine
Universitas Brawijaya
LOGO
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
• 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
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
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
3. HIDROLASE 4. LYASE
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
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
Collision Theory
Michaelis and Menten hypothesis for enzyme action
E + S  ES  E + P
Intermediate/transient
complex
An enzyme-catalyzed reaction takes a different ‘route’

Model of Enzyme-Substrate Complex
Formation
Lock and Key

Formation
Lock and Key

Formation
Induced fit
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
 specific, thermostable, low molecular weight,

non-protein organic substance
 carrier molecule
 may bind covalently or non- covalently to the
apoenzyme
Membawa
elektron
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-factor
 Terlibat dalam proses katalisis
 Menstabilkan enzim atau substrat
 Magnesium (Mg), zat besi (Fe), zinc (Zn)
 Non organik
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

 Enzim dapat bekerja secara optimal dalam

kondisi lingkungan tertentu
 Lingkungan  pH dan temperature
Effect Temperature
of pH
Substrate and Product Concentration
Enzyme Concentration
Activators and Coenzymes
Modulators and Inhibitors
Time
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
Temperature
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
Substrate and Product

Concentration
 Need to be enough substrate around

 Substrate <<  reaction rate <<
 Product >>  reaction rate <<
Enzyme Concentration
 Increasing Enzyme Concentration will

increase the rate of reaction, as
more enzymes will be colliding with
substrate molecules.
Effect of Activators and

Coenzymes
 The activity of certain enzymes is greatly

dependent of metal ion activators and
coenzymes
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)
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
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

Uses of Enzyme

LOGO

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

Uploaded by

Copyright:

Available Formats

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

Uploaded by

Document Information

Original Description:

Original Title

Copyright

Available Formats

Share this document

Share or Embed Document

Sharing Options

Did you find this document useful?

Is this content inappropriate?

Copyright:

Available Formats

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

Uploaded by

Copyright:

Available Formats

ENZYME

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

Nomenclature and Type of Enzyme

Model of Enzyme-Substrate Complex Formation

Factors Affecting Enzyme Action

Biochemical reactions ALWAYS occur in the body

Catalysts of biological systems

• Enzymes are generally named after adding the

International Union of Biochemistry

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

Specific name : Hexokinase

Sub-subclass 1 : Alcohol is the phosphate acceptor

Subclass 7 : Transfer of phosphate

2 Transferases catalyze transfer of groups from a donor

 Breakdown of nutrient  energy

Most collision fails to

Enzymes have immense catalytic power and accelerate reactions

Michaelis and Menten hypothesis for enzyme action

An enzyme-catalyzed reaction takes a different ‘route’

Lock and Key

Lock and Key

All the enzymes are protein in nature with large molecular

 specific, thermostable, low molecular weight,

Co-enzymes can be classified according to the group

For transfer of groups

Role of Metal Ions in Enzymes Co-factor

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

 Enzim dapat bekerja secara optimal dalam

Substrate and Product Concentration

Activators and Coenzymes

Modulators and Inhibitors

 Enzyme function optimally at a particular temperature

pH  The enzymatic activity is

Substrate and Product

 Need to be enough substrate around

 Increasing Enzyme Concentration will

Effect of Activators and

 The activity of certain enzymes is greatly

Effect of Activators and

Copper Superoxide dismutase, cytochrome oxidase,

Iron Catalase, xanthine oxidase, peroxidase cytochrome

Zinc Carbonic anhydrase, alcohol dehydrogenase,

Effect of Modulators and

 Whenever the active site is not available for

 The time required for completion of an

 Enzymes can be inactivated by the agents that

• If the inhibitor can be removed from its site of

the inhibitor binds to the enzyme at a site other than

Enzymes estimation in serum and body

Enzyme used as laboratory reagent

Therapeutic uses of enzymes

Enzymes for diagnosis and prognosis

Enzymes for diagnosis and prognosis

Serum Enzymes In Liver Diseases