Enzymes

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No.1 for your science News

BS IN NURSING N02
FOOD SOURCES OF
DIGESTIVE ENZYMES

Vol. 01
50

GROUP ONE

ENZYMES OF
CLINICAL SIGNIFICANCE
Issue#1 | Vol.1 | december 2021
 GROUPONE

CONTENTS
BS IN NURSING NO2 GROUP 4: ENZYMES

01 DEFINITION AND CHARACTERISTICS

What are enzymes? What does it do? What is it for?
Group 4 introduces the enzymes.

02 STRUCTURE
Know enzymes better by knowing what makes
up enzymes and how it is classified based on
structure.

03 COENZYMES
Featuring the helping hand of enzymes,
understand its role on how it enhances enzyme
activity.

12 FOOD SOURCES OF
DIGESTIVE ENZYMES
04 EXCLUSIVE!

CLASSIFICATION AND
NOMENCLATURE OF
ENZYMES

03 ISOENZYMES
The same, but not quite.

06 ENZYMATIC REACTION
08 10 Delve deeper to how enzymes catalyze
reactions that benefits your body.

02
FACTORS AFFECTING ENZYMES OF CLINICAL
ENZYME ACTIVITY SIGNIFICANCE
DECEMBER 2021| ISSUE 01

Understand how different Know the different enzymes

01234. GROUP FOUR. BRGY.
factors improve or worsen that contributes greatly to BACHELOR OF SCIENCE IN
enzyme activity. our health! NURSING. STREET NO2

WWW.ENZYMES.COM/NO2

www.enzymes.com  |    i
Definition
a n d c h a r a c t e r i s t i c s

Plus its structure,

isoenzymes, and
coenzymes
Enzymes

Decemb 2021 | Issue No. 01

what are
Enzymes?
?
Enzymes are protein catalyst produced by
a cell and responsible ‘for the high rate’
and specificity of one or more intracellular
or extracellular biochemical reactions.
Enzymes are biological catalysts
responsible for supporting almost all of
the chemical reactions that maintain
animal homeostasis.

Characteristics
Enzymes do nothing but speed up the ALMOST ALL THE ENZYMES ARE
rates at which the equilibrium positions of PROTEINS AND THEY FOLLOW THE
reversible reactions are attained. In terms PHYSICAL AND CHEMICAL REACTIONS
of thermodynamics, enzymes reduce the OF PROTEINS
activation energies of reactions, enabling ENZYMES ARE SENSITIVE AND LABILE
TO HEAT
them to occur much more readily at low
ENZYMES ARE WATER SOLUBLE
temperatures - essential for biological
ENZYMES COULD BE PRECIPITATED BY
systems. PROTEIN PRECIPITATING AGENTS
SUCH AS AMMONIUM SULFATE AND
TRICHLOROACETIC ACID.

Structure
Enzymes are proteins comprised of amino The complete three-dimensional fold of a
acids linked together in one or more polypeptide chain into a protein subunit is
polypeptide chains. This sequence of known as its tertiary structure. The three-
amino acids in a polypeptide chain is dimensional arrangement of subunits is
called the primary structure. This, in turn, known as its quaternary structure.
determines the three-dimensional Subunit structure is determined by the
structure of the enzyme, including the sequence and characteristics of amino
shape of the active site. The secondary acids in the polypeptide chain.
structure of a protein describes the
localized polypeptide chain structures,
e.g., α-helices or β-sheets.

ENZYMES |  2
 Isoenzymes
physically distinct forms of the same
are The expression of isozymes in specific cells
occurs during certain periods of
enzyme activity. Higher organisms have development, or in response to specific
several physically distinct versions of a physiologic or pathophysiologic changes.
given enzyme, each of which catalyzes the Thus analysis of the presence and
same reaction. Isozymes arise through distribution of enzymes and isozymes are
gene duplication and exhibit differences in often useful in diagnosis.
properties such as sensitivity to particular
regulatory factors or substrate
affinity that adapts them to
specific tissues or circumstances.
Some isozymes enhance
survival by providing a “backup”
copy of an essential enzyme.
Isozymes are expressed only in
specific cell types.
Lactate Dehydrogenase Isoenzymes

Enzymes may be simple proteins, or The heat labile or unstable part of the holo-
complex enzymes. A complex enzyme enzyme is called as apo-enzyme. The apo-
contains a non-protein part, called as enzyme gives necessary three dimensional
prosthetic group (coenzymes). structures required for the enzymatic
Coenzymes are heat stable low chemical reaction. Co-enzymes are
molecular weight organic very essential for the biological
compound. The combined activities of the enzyme.
protein and the
co-enzyme are called
as holo-enzyme.

Co-enzymes are further

Coenzymes The role of coenzymes is to
divided into two groups. act as transporters of
The first group of chemical groups from one
co-enzymes are also reactant to another. In all
called as co-substrates or cases, the coenzymes donate the
secondary substrates. Because carried chemical grouping to an
they are involved in counter-balance in acceptor molecule and are thus
change occurring in the substrate. The regenerated to their original form. This
second group of co-enzymes involves in regeneration of coenzyme and holoenzyme
reactions transferring groups other than fulfills the definition of an enzyme as a
hydrogen. chemical catalyst

www.enzymes.com  |    3
 FEATURING
INTERNATIONAL UNION
OF BIOCHEMISTS NA
DMOLECULAR BIOLOGY
&
Trivial Naming
IUBMB System
Classification
Nomenclature
 INTERNATIONAL UNION OF BIOCHEMISTRY
AND MOLECULAR BIOLOGY
IUBMB System
Enzymes are currently grouped
into six functional classes by the
International Union of
Biochemists and Molecular
Biology (IUBMB). As per the
IUBMB system, each enzyme name
starts with EC (enzyme class)
followed by 4 digits. The first
digit represents the class, the
second digit strands for the
subclass, the third digit
represents the sub-subclass or
subgroup and the fourth digit
IUBMB Executive Committee September 2020
provides the particular enzyme.

Trivial Naming
Since earlier days to still date,
fanciful names such as pepsin,
chymotrypsin, etc. were used to
name enzymes. Later the suffix
“ase” to the substrate was used to
name enzymes. For example the
enzymes lactase acts upon the
lactate and produces glucose and
galactose.

Table 1. Classification of Enzymes

Enzymes are also classified on Metalloenzymes bind and to the class 6 (Ligases).
the basis of their composition. retain their metal atom(s) Enzymes such as Carbamoyl
Enzymes composed wholly of under all conditions with very phosphate synthetase, Arginino
protein are known as simple high affinity. Enzymes with succinate synthetase and
enzymes in contrast to complex lower affinity for metal ion, Glutamine synthetase are
enzymes, which are composed but still require the metal ion examples of the synthetases
of protein plus a relatively for activity, are known as group of enzymes. The enzyme
small organic molecule. metal-activated enzymes. class other than ligases
Complex enzymes are also includes synthases. Synthases
known as holo-enzymes. The Based on requirement of group of enzymes involves in
non-protein component of an ATP, enzymes are further catalyzing biosynthetic
enzyme may be as simple as a classified into two types reactions that do not require
metal ion or as complex as a namely synthetases and ATP directly. Enzymes such as
small non-protein organic synthase. Synthetases are ATP- glycogen synthase and Alanine
molecule. Enzymes that require dependent enzymes catalyzing synthase are examples of
a metal in their composition biosynthetic reactions. synthase group.
are known as metalloenzymes. Synthetases are enzyme belong

ENZYMES | 5
ENZYMATIC
REACTIONS
E N Z Y M E - S U B S T R A T E C O M P L E X T H E O R Y

K C O L
LEDOM

I NTERACT
REACT D N A
TIF

Y E K
DECUDNI

CATALYZE
L E D O M
 ENZYME-SUBSTRATE COMPLEX THEORY LOCK AND KEY THEORY
In 1913, Michaelis and Menten put forward the It states that the three dimensional structure of
Enzyme–Substrate complex theory. the active site of the enzyme is complementary
Accordingly, the enzyme (E) combines with the to the substrate. Thus enzyme and substrate fit
substrate (S), to form an enzyme-substrate (ES) each other. Substrate fits on the enzyme,
complex, which immediately breaks down to the similar to lock and key. The lock can be opened
enzyme and the product (P). by its own key only. However, Fischer
envisaged a rigid structure for enzymes, which
could not explain the flexibility shown by
enzymes.

Lock and Key Model

Induced Fit model

INDUCED FIT THEORY

Conformational changes are occurring at the Partially folded position, but hand can enter into
active site of enzymes concomitant with the it. When the hand is introduced, the glove is
combination of enzyme with the substrate. At further opened. Similarly, conformational
first, substrate binds to a specific part of the changes occur in the enzyme when the
enzyme. This leads to more secondary binding substrate is fixed. When substrate analog is
and conformational changes. The substrate fixed to the enzyme, some structural alteration
induces conformational changes in the enzyme, may occur; but reaction does not take place due
such that precise orientation of catalytic groups to lack of proper alignment. Allosteric regulation
is effected. A simplified explanation is that a can also be explained by the hypothesis of
glove is put on a hand. At first, the glove is in a Koshland.

www.enzymes.com  |    7
VELOCITY OR RATE OF ENZYMATIC
REACTION IS ASSESSED BY THE RATE
OF CHANGE IN CONCENTRATION OF
SUBSTRATE OR PRODUCT AT A GIVEN
TIME DURATION.

Effect of substrate
Concentration

FACTORS AFFECTING
ENZYME ACTIVITY
Effect of product 25
concentration
Reaction velocity of an enzymatic process

ENZYME ACTIVITY
increases with constant enzyme concentration
and increase in substrate concentration. The
velocity (V) is expressed in micromoles of In the case of a reversible reaction catalyzed by an enzyme, as
substrate converted per minute. As the per the law of mass action, the rate of reaction is slowed down
concentration of substrate increases, the with equilibrium. So, the rate of reaction is slowed, stopped, or
velocity of the reaction increases. even reversed with an increase in product concentration. This
phenomenon can be better explained by the equation
The continued increase in substrate
concentration may lead to a reduction in the In the above equation, in case of the absence of the enzyme E3,
rate of the reaction and leads to a flattened the product C will accumulate. Enzymatic activity of E2 will be
curve. The maximum velocity obtained from inhibited with the accumulation of the product C. In such inborn
an enzymatic reaction is called Vmax. Vmax error of one enzyme will block the whole pathway
represents the maximum reaction rate
possible in the presence of excess substrate. Effect of
temperature
Velocity of enzymatic reaction increases
Effect of enzyme with temperature of the medium which
Concentration they are most efficient and the same is
termed as optimum temperature. As
temperatures increases it leads to
denaturation; a molecular arrangement
which causes a loss of the active sites of
the enzyme surfaces and results in a
loss of efficiency

Effect of pH
Like temperature, all enzymes have a
optimum pH, at which the enzymatic
activity will be at maximum. Many
enzymes are most efficient in the
region of pH 6-7, which is the pH of the
As there is optimal substrate concentration, cell. Outside this range, enzyme activity
rate of an enzymatic reaction or velocity (V) is drops off very rapidly.
directly proportional to the enzyme
concentration. Presence of excess substrate
and an increase in the enzyme concentration Reduction in efficiency caused by changes in the pH is due to changes in the
may result in some limitations. It is worthy of degree of ionization of the substrate and enzyme. Highly acidic or alkaline
note that the enzymes are rarely saturated conditions bring about a denaturation and subsequent loss of enzymatic activity.
with substrates under physiological Some exceptions such as pepsin (with optimum pH 1-2), alkaline phosphatase
conditions. (with optimum pH 9-10) and acid phosphatase (with optimum pH 4-5) are even
noticed.
ENZYMES | 8 Continue reading at next page >
 Effect of
temperature
Presence of certain inorganic ions
increases the activity of enzymes.
The best examples are chloride ions
activated salivary amylase and
calcium activated lipases.

Effect of Inhibitors
The catalytic enzymatic reaction may be inhibited by substances which prevent the
formation of a normal enzyme-substrate complex. The level of inhibition then depends
entirely upon the relative concentrations of the true substrate and the inhibitor. Such
inhibition, which depends on competition with the substrate for the active sites of the
enzyme, is termed competitive inhibition. In other cases, the inhibitor combines with the
enzyme-substrate complex to give an inactive enzyme-substrate-inhibitor complex, which
cannot undergo further reaction to give the usual product.

This is termed uncompetitive inhibition. Non competitive inhibition involves

combination of the inhibitor with the enzyme or the enzyme substrate complex, to give
inactive complexes. In this case, the inhibitor binds to sites, on the enzyme other than
enzyme sites, resulting in deformation of the enzyme molecule so that the formation of
the enzymesubstrate complex is slower than normal. Some enzymes undergo
irreversible inactivation; reaction of the inhibitor with a functional group of the
enzyme, resulting in a loss of its catalytic activity

EFFECT OF ENZYME INHIBITORS

www.enzymes.com  |    9
 C
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LIVER ENZYMES
T
he assay of serum enzymes is very
useful for the differential diagnosis and
monitoring of various liver disorders. Liver
enzymes acts as marker of hepatocellular
damage, cholestasis and disturbances in
the hepatocellular synthesis

HEPATOCELLULAR
DAMAGE MARKERS
n case of hepatocellular damage, the

I enzymes which are normally present

inside the hepatocytes are released into the
blood. Aminotransaminases such as
aspartate transaminase (AST) and alanine
transaminase (ALT) are routinely used in
diagnosis of hepatocellular damages.
Transaminases are enzymes involved in the
transfer of an amino group from a 2-amino-
to a 2-oxoacid. The 2oxoglutarate acts as
amino group acceptor and the L-glutamate
serves as donor in all amino-transfer
reactions. The specificity of the individual
enzymes derives from the particular amino
PANCREATIC ENZYMES acid that serves as the other donor of an

ALPHA-AMYLASE amino group.

α-amylase (AMYs) are calcium dependent hydrolyase class of metaloenzyme that catalyzes the
hydrolysis of 1, 4- α-glycosidic linkages in polysaccharides. Molecular weights of AMYs are human
plasma ranges from 54 to 62 kDa. Due to its smaller size they could easily pass the glomeruli of the
kidneys and AMY is the only plasma enzyme physiologically found in urine. The normal values of
amylase is in range of 28-100 U/L. Marked increase of 5 to 10 times the upper reference limit (URL) in
AMYs activity indicates acute pancreatitis and severe glomerular impairment. Pancreatic pseudocyst
occurs if the plasma level of amylase activity fails to fall after an attack of acute pancreatitis

LIPASE

Lipase is single chain glycoprotein of molecular weight 48 kDa. Bile salts and a cofactor called
colipase are required for full catalytic activity of lipase. Colipase is secreted by pancreas. Lipase is
small molecule filtered through the glomerulus and totally reabsorbed by the renal tubules. Lipase is
not normally detected in urine samples. The normal value of lipase ranges from 40-200 U/ L. Increase
in plasma lipase activity indicates acute pancreatitis and carcinoma of the pancreas. So
determination of both amylase and lipase together helps in the diagnosis of acute pancreatitis.
ENZYMES | 10
 ASPARTATE
TRANSAMINASE (AST)

Aspartate transaminase is present in

high concentrations in cells of cardiac
and skeletal muscle, liver, kidney and
erythrocytes. Damage to any of these
tissues may increase plasma AST levels.
The normal value of AST for male is <35
U/ L and for female it is <31 U/L. Marked
increase of AST activity in the range of
10 to 100 times the upper adult
reference limit indicates myocardial
infarction or acute viral or toxic hepatitis.

LIVER ENZYMES
ALKALINE PHOSPHATASES
CHOLESTASIS
Are a group of enzymes that hydrolyse
MARKERS
ALANINE organic phosphates at high pH. They are
Enzymatic markers of cholestasis are
TRANSAMINASE (ALT) present in osteoblasts of bone, the cells of
membrane bound enzymes. Markers of
cholestasis includes alkaline phosphatases, the hepatobiliary tract, intestinal wall, renal
Alanine transaminase is present at high
concentrations in liver and to a lesser gamma-glutamyl transferase and glutamate tubules and placenta.

extent, in skeletal muscle, kidney and dehydrogenase.

heart. Thus in case of liver damage
increase in both AST and ALT were
noticed. While in myocardial infarction GLUTAMATE DEHYDROGENASE GAMMA-GLUTAMYL-TRANSFERASE
AST is increased with little or no Catalyzes the transfer of the γ–glutamyl group
Is a mitochondrial enzyme found in liver, heart
increase in ALT. The normal value of from peptides. The activity of GGT is higher in
muscle and kidneys. Small amounts of GLD
ALT is <45 U/L and <34 U/L for male and men than in women. In male the normal value
are even observed in brain, skeletal muscle
female respectively. In acute viral of GGT activity is <55 U/L and for female it is
tissue and leukocytes. GLD is increased in
hepatitis there is a 100-1000 times <38 U/L. Rise in plasma GGT activity is due to
serum of patients with hepatocellular damage
increase in both ALT and AST but ALT infectious hepatitis and induction of enzyme
offering differential diagnostic potential in the
level is increased more than that of AST synthesis, without cell damage, by drugs or
investigation of liver disease. GLD is released
alcohol.
from necrotic cells and is of value in
estimation of the severity of liver cell damage.
The GLD upper reference limits are 6U/L
(women) and 8U/L (men).

MUSCLE ENZYMES
Clinically important muscle enzymes include creatine kinase and lactate dehydrogenase.

CREATINE KINASE LACTATE DEHYDROGENASE

Is most abundant in cells of brain, cardiac and skeletal. In addition to Catalyses the reversible interconversion of lactate and pyruvate. LD
their abundance in above tissues, it also occurs in other tissues such has a molecular weight of 134 kDa and is widely distributed in the
as smooth muscle. In normal physiological condition the CK activity is body, with high concentrations in cells of cardiac and skeletal muscle,
46171 U/L (for male) and 34-145 U/L (for female). Serum CK level liver, kidney, brain and erythrocytes. Five isoforms (LD-1 to LD-5) of LD
elevates in all types of muscular dystrophy. Quite high values ofCK are are existing. The normal physiological limit of LD is 180-360 U/L.

noted in viral myositis, polymyositis and similar muscle disease. Under

the circumstances of neurogenic muscle disease such as: myasthenia
gravis, multiple sclerosis and Parkinsonism, the level of serum CK is
normal. CK consist of two protein subunits, M (for muscle) and B (for
brain) and exist as three different isoforms namely BB (CK-1), MB (CK-
2) and MM (CK-3). CK-MM is the predominant isoenzyme in skeletal
and cardiac muscle and is detectable in the plasma of normal subjects.
CK-BB is present in high concentrations in the brain and in the smooth
muscle of the gastrointestinal and genital tracts.
www.enzymes.com  |    11
What are the Food
Source of Enzymes?
Issue - 03 December

Main types of
digestive enzymes
(1) Proteases: Break down protein into
small peptides and amino acids
(2) Lipases: Break down fat into three fatty
acids plus a glycerol molecule
(3) Amylases: Break down carbs like starch
into simple sugars

Food that contain

and sources of
enzymes

BSN NO2
Group 1 : Enzymes

Food Source
Proteases

THE THREE MAIN TYPES OF

DIGESTIVE
ENZYMES
Lipases By Group 1

Enzymes are required for the digestive process because

they break down molecules such as lipids, proteins, and
carbohydrates into smaller molecules that may be easily
absorbed.

There are three main types of digestive enzymes:

(1) Proteases: Break down protein into small peptides
and amino acids. A protease (also called a peptidase or
proteinase) is an enzyme that catalyzes (increases
reaction rate or "speeds up") proteolysis, breaking down
proteins into smaller polypeptides or single amino acids,
and spurring the formation of new protein products.

(2) Lipases: Break down fat into three fatty acids plus a
glycerol molecule. Lipase is an enzyme the body uses to
break down fats in food so they can be absorbed in the
Amylases intestines. Lipase is produced in the pancreas, mouth,
and stomach. Along with lipase, the pancreas secretes
insulin and glucagon, two hormones the body needs to
break down sugar in the bloodstream.

(3) Amylases: Break down carbs like starch into simple

sugars. Amylases are one of the main enzymes used in
industry. Such enzymes hydrolyze the starch molecules
into polymers composed of glucose units. Amylases
have potential application in a wide number of industrial
processes such as food, fermentation, and
pharmaceutical industries.

ENZYMES | 13
Fruits, vegetables, and other foods
have natural digestive enzymes.
Adding any of these foods to your
Mango • Mangoes possess the
digestive enzyme amylase, which
converts starch (a complex carb)
FOOD
diet may help promote digestion and
better gut health.
into sugars such as glucose and
maltose. Amylase also aids in the
ripening of mangoes.
THAT
Pineapple • Pineapples are a
wonderful tropical fruit high in
digestive enzymes, and they include
Honey • Honey includes digestive
enzymes such as diastase, amylase,
CONTAIN
a category of digestive enzymes
known as bromelain. These enzymes
are proteases, which deconstruct
invertase, and protease. Raw honey
is not cooked, unlike processed
honey is, which kills digestive
AND
protein into its constituent parts,
including amino acids. This
promotes protein digestion and
enzymes. (e) Kimchi • Kimchi is a
type of fermented vegetable cuisine.
It's fermented with Bacillus species
SOURCES
absorption.

Papaya • Papayas include papain, a

bacteria, which contribute enzymes
including proteases, lipases, and
amylases.
OF
digestive enzyme that breaks down
proteins into building components
such as amino acids. Because high
Ginger • Ginger includes the
protease digesting enzyme
ENZYMES
heat can destroy their digestive
enzymes, ripe papayas are high in
zingibain. It may improve digestion
by allowing food to pass more
BY GROUP 1
enzymes. quickly through the digestive tract.
Raman, R. (2018, May 15). 12 foods that contain natural
digestive enzymes. Healthline.
https://www.healthline.com/nutrition/natural-digestive-
enzymes#TOC_TITLE_HDR_13

FOOD SOURCE OF ENZYMES www.enzymes.com  |    14

ABAJADO | ABOY | ANTENOR | ANTOQUE | ARCAYOS
GROUP 1 | BSN-N02

ENZYMES
NO. 1 FOR YOUR SCIENCE NEWS

DECEMBER 2021• ISSUE 01 • VOLUME 01