The document discusses enzymes and their classification. It defines enzymes as biological catalysts that are usually proteins and increase the rate of chemical reactions. It describes the six main classes of enzymes based on their catalytic activity as well as the Enzyme Commission (EC) numbering system. The key points are that enzymes have unique active sites that substrates fit into, they are most active at optimal temperatures and pH levels, and their reaction rates depend on enzyme and substrate concentrations.
Active sites of the enzyme is that point where substrate molecule bind for the chemical reaction. It is generally found on the surface of enzyme and in some enzyme it is a “Pit” like structure
The active site is a three-dimensional cleft formed by groups that come from different parts of the amino acid sequence
The active site takes up a relatively small part of the total volume of an enzyme
Active sites are clefts or crevices
Substrates are bound to enzymes by multiple weak attractions.
The specificity of binding depends on the precisely defined arrangement of atoms in an active site.
Pentose phosphate pathway is also called Hexose monophosphate pathway/ HMP shunt/ Phosphogluconate pathway.
It is an alternative route for the metabolism of glucose.
It is more complex pathway than glycolysis.
It is more anabolic in nature.
It takesplace in cytosol.
The tissues such as liver, adipose tissue, adrenal gland, erythrocytes,testes and lactating mammary gland are highly active in HMP shunt.
It concern with the biosynthesis of NADPH and pentoses.
Active sites of the enzyme is that point where substrate molecule bind for the chemical reaction. It is generally found on the surface of enzyme and in some enzyme it is a “Pit” like structure
The active site is a three-dimensional cleft formed by groups that come from different parts of the amino acid sequence
The active site takes up a relatively small part of the total volume of an enzyme
Active sites are clefts or crevices
Substrates are bound to enzymes by multiple weak attractions.
The specificity of binding depends on the precisely defined arrangement of atoms in an active site.
Pentose phosphate pathway is also called Hexose monophosphate pathway/ HMP shunt/ Phosphogluconate pathway.
It is an alternative route for the metabolism of glucose.
It is more complex pathway than glycolysis.
It is more anabolic in nature.
It takesplace in cytosol.
The tissues such as liver, adipose tissue, adrenal gland, erythrocytes,testes and lactating mammary gland are highly active in HMP shunt.
It concern with the biosynthesis of NADPH and pentoses.
Enzymes properties, nomenclature and classificationJasmineJuliet
Enzymes - Definition, Introduction about biocatalysts, Properties of enzymes, Specificity, capacity for regulation, Example for enzyme at specific pH, Nomenclature of enzymes, Systematic name, common name, enzyme commission number, Classification of enzymes: Oxidoreductase, Transferase, lyases, ligases, isomerases, hydrolases.
The flux of metabolites through metabolic pathways involves
catalysis by numerous enzymes. Active control of homeostasis is achieved by the regulation of only a small number of enzymes.
This presentation was prepared in order to take Lecture of students in a summarised way and to provide them with the short, sweet and concise notes. It is based on PCI syllabus and is meant for B. Pharm. Second Semester...
An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process. The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes
What is catalysis, its type and its applicationLovnish Thakur
This document will give you information about catalysis and type of catalysis like homogenious and heterogenious catalysis and its various application .
Enzymes properties, nomenclature and classificationJasmineJuliet
Enzymes - Definition, Introduction about biocatalysts, Properties of enzymes, Specificity, capacity for regulation, Example for enzyme at specific pH, Nomenclature of enzymes, Systematic name, common name, enzyme commission number, Classification of enzymes: Oxidoreductase, Transferase, lyases, ligases, isomerases, hydrolases.
The flux of metabolites through metabolic pathways involves
catalysis by numerous enzymes. Active control of homeostasis is achieved by the regulation of only a small number of enzymes.
This presentation was prepared in order to take Lecture of students in a summarised way and to provide them with the short, sweet and concise notes. It is based on PCI syllabus and is meant for B. Pharm. Second Semester...
An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process. The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes
What is catalysis, its type and its applicationLovnish Thakur
This document will give you information about catalysis and type of catalysis like homogenious and heterogenious catalysis and its various application .
The pigment chlorophyll is found inside the chloroplasts, each leaf contains millions of chloroplasts. Inside each one, there are stacks of membranes that hold the chlorophyll molecules.
Development of
- Improved catalysts to be employed within existing production units for existing reactors
- Improved catalysts for existing reactors using new procedures calling for new equipment
- Integration of catalyst and reactor
Heat transfer and mass transport
- Integration of catalytic reaction and separation of reactants or reaction products
Catalytic distillation as an example : performing a catalytic reaction within a distillation column ......
Chlorophyll and Guarana contains 8 types of Enzymes, rich in Anti-oxidants, Vitamin B1, B2, B6, B12, E, and More essential amino-acids. Cleanse to remove eliminate and body wastes. Reduce body heat and improve urination.
Enzymes are dynamic proteins that accelerate biochemical reactions.
Each enzyme acts on a specific reactant, the substrate.
Enzymes are characterized by greater activity, specificity and susceptibility to the influence of pH, temperature and other environmental changes.
Enzymes act in the presence of non-peptide cofactors or coenzymes.
An enzyme lacking its cofactor is called apoenzyme and the active enzyme with its co-factor, the holoenzyme.
Introduction, Nomenclature of enzymes, Classification of enzymes on the basis of site of action, on the reaction of catalysis and Classification depends upon substrates on they which act, Specificity of Enzymes, Active Site of An Enzyme: 1. Lock-key model 2. Induce fit model, Factors Affecting Enzymes Reaction, Enzyme 1.Inhibition Competitive inhibition, 2. Non-Competitive inhibition, Isoenzymes, Allosteric Enzymes, Co-Factors, Turnover Number of An Enzyme, Pharmaceutical Importance Of Enzymes,
Enzymes are biological molecules (proteins) that act as catalysts and help complex reactions occur everywhere in life. Let's say you ate a piece of meat. Proteases would go to work and help break down the peptide bonds between the amino acids.
This content is made for all student of medical ,nutrition ,doctors ,zoology ,chemistry ,medical who are still preparing for examination .feel free to give suggestions
Introduction
Definition
Historical aspects
Nomenclature of enzymes on the basis of
1. Substrate acted
2. Reaction catalyzed
3. substrate act upon and type of reaction catalyzed
Classification of enzymes
Oxidoreductase
Transferase
Hydrolase
Lyase
Isomerase
Ligase
Property of enzyme
Structure of enzyme
Mechanism of enzyme action
Lock and key model
Induced fit model
factors affecting enzyme activity
Control of enzyme action
Conclusion
Reference
Enzymes mechanism of action, their specificity types, active center structure and action, inhibitor types, fisher and Koshlend theory are presented. Enzymes classification, a new class of enzymes discovered recently, detailed explanation of each class reaction types is presented as well
Enzyme presentation by Rohini Yadav.pptxROHINI YADAV
Defination
Discovery and History
Properties of enzyme
Classification
Nomenclature
Models
Mechanism of action
Factors affecting enzyme activity
Application
Refferences
1. 4th SEMESTER – BOTANY
KARNATAKA UNIVERSITY, DHARWAD
Modified from various internet resources by
Dr. Jayakara Bhandary
Associate Professor of Botany
Government Arts & Science College
Karwar, Uttara Kannada
1
2. Introduction & History
Enzyme, in Greek means in living (en= in, zyme =
living).
Biocatalysts or Organic catalysts, usually high
molecular weight proteins (exception- Ribozymes
or RNA enzymes).
Coined by Kuhne in 1878.
First enzyme extract from Yeast cells by Buchner
(1897).
First purified enzyme is urease, by James B.
Summer (1926).
2
3. Enzymes are Biological Catalysts
Enzymes are proteins that:
Increase the rate of
reaction by lowering the
energy of activation.
Catalyze nearly all the
chemical reactions taking
place in the cells of the
body.
Have unique three-
dimensional shapes that
fit the shapes of reactants.
3
4. Activation Energy
Think of activation energy as the
BARRIER
required to make a product.
Most stable product is the one with
the lowest
energy.
Most reactions require a “push” to
get them
started! “Push” is called “energy
of activation” for
reaction - Also represented by EA
4
5. Trivial Names of Enzymes
The name of an enzyme:
Usually ends in –ase.
Identifies the reacting substance. For
example,
sucrase catalyzes the reaction of sucrose.
Describes the function of the enzyme. For
example, oxidases catalyze oxidation.
Could be a common name, particularly for
the digestion enzymes such as pepsin and
trypsin.
5
6. IUB Classification of Enzymes
Enzymes are classified according to the reaction
they catalyze.
Class Reactions catalyzed
Oxidoreductases Oxidation-reduction
Transferases Transfer groups of atoms
Hydrolases Hydrolysis
Lyases Add atoms/remove atoms
to/from a double bond
Isomerases Rearrange atoms
Ligases Use ATP to combine
molecules
6
7. 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
8. EC number
Enzymes are classified into six different groups
according to the reaction being catalyzed. The
nomenclature was determined by the Enzyme
Commission in 1961 (with the latest update having
occurred in 1992), hence all enzymes are assigned an
“EC” number. The classification does not take into
account amino acid sequence (ie, homology), protein
structure, or chemical mechanism.
9. EC numbers
EC numbers are four digits, for example a.b.c.d, where
“a” is the class, “b” is the subclass, “c” is the sub-
subclass, and “d” is the sub-sub-subclass. The “b” and
“c” digits describe the reaction, while the “d” digit is
used to distinguish between different enzymes of the
same function based on the actual substrate in the
reaction.
Example: for Alcohol:NAD+oxidoreductase EC
number is 1.1.1.1
11. EC 1. Oxidoreductases
Catalyze the transfer of hydrogen or oxygen atoms
or electrons from one substrate to another.
Since these are ‘redox’ reactions, an electron
donor/acceptor is also required to complete the
reaction.
A H2 +B → A+ BH2
Ex. Oxidases, Dehydrogenases,
Reductases.
12. EC 2. Transferases
Catalyze group transfer reactions, excluding
oxidoreductases (which transfer hydrogen or
oxygen and are EC 1). These are of the general
form:
A-X + B ↔ BX + A
Ex: Transaminases (transfer amino group),
Kinases (transfer Phosphate group)
14. EC 4. Lyases
Catalyze non-hydrolytic (covered in EC 3) removal
of functional groups from substrates, often
creating a double bond in the product; or the
reverse reaction, ie, addition of function groups
across a double bond.
A- X +B-Y → A=B + X-Y
Ex: Decarboxylases, Aldolases, Dehydrases,
Deaminases, Synthases, etc.
15. EC 5. Isomerases
Catalyzes isomerization reactions, including
epimerizations and cis-trans
isomerizations.
A →A’
Ex: Isomerases (Cis-Trans),
Epimerases (D—L)
16. EC 6. Ligases
Catalyzes the synthesis of various (mostly C-X)
bonds, coupled with the breakdown of energy-
containing substrates, usually ATP .
A+B → A-B
ATP → ADP+iP
Ex: Synthetases, Carboxylases
20. Active Site
The active site:
Is a region within an
enzyme that fits the
shape of molecules
called substrates.
Contains amino acid R
groups that align and
bind the substrate.
Releases products
when the reaction is
complete.
20
21. Enzyme Specificity
Enzymes may recognize and catalyze:
A single substrate.
A group of similar substrates.
A particular type of bond.
21
22. Mechanism of
Enzyme Catalyzed Reactions
The proper fit of a substrate (S) in an active site
forms an enzyme-substrate (ES) complex.
E+S ES
Within the ES complex, the reaction occurs to
convert substrate to product (P).
ES E+P
The products, which are no longer attracted to
the active site, are released.
Overall, substrate is convert to product.
E+S ES E+P
22
26. Mechanism of Enzyme Action:
1.Lock-and-Key Model
In the lock-and-key model of enzyme action:
The active site has a rigid shape.
Only substrates with the matching shape can
fit.
The substrate is a key that fits the lock of the
active site.
26
27. 2. Induced-fit Model
In the induced-fit model of enzyme action:
The active site is flexible, not rigid.
The shapes of the enzyme, active site, and
substrate adjust to maximum the fit, which
improves catalysis.
There is a greater range of substrate specificity.
27
29. Temperature and Enzyme Action
Enzymes:
Are most active at an
optimum
temperature (usually
37°C in humans).
Show little activity at
low temperatures.
Lose activity at high
temperatures as
denaturation occurs.
29
30. pH and Enzyme Action
Enzymes:
Are most active at
optimum pH.
Contain R groups of
amino acids with
proper charges at
optimum pH.
Lose activity in low or
high pH as tertiary
structure is
disrupted. 30
31. Optimum pH Values
Most enzymes of the body have an optimum pH
of about 7.4.
In certain organs, enzymes operate at lower and
higher optimum pH values.
31
32. Enzyme Concentration
The rate of
reaction increases
as enzyme
concentration
increases (at
constant substrate
concentration).
At higher enzyme
concentrations,
more substrate
binds with
enzyme. 32
33. Substrate Concentration
The rate of reaction
increases as
substrate
concentration
increases (at
constant enzyme
concentration).
Maximum activity
occurs when the
enzyme is
saturated.
33