Enzymes

BIOCHEMISTRY
School of Health & Allied Health Sciences
Southwestern University
 Enzymes:
Outline:
✔ Importance of enzymes
✔ Enzyme structure and General function
✔ Co-enzymes
✔ Metalloproteins
✔ Nomenclature and classification of enzymes
✔ MOA of enzymes
✔ Models of enzyme action
✔ Enzyme specificity
✔ Factors That Affect Enzyme Activity)
✔ Extremophiles
✔ Enzyme inhibition
✔ Regulation of enzyme activity
✔ Allosteric enzymes
✔ Proteolytic enzymes
✔ Medically important enzymes
 ENZYMES
• Greek word en “in” and zyme “yeast”
• Enzymes are biological catalyst that speed up the rate of the biochemical reaction.
• Most of the enzymes are three dimensional globular proteins (tertiary and quaternary structure)

Note: With the exception of a few catalytic RNA molecules, or ribozymes which made of ribonucleic acids
and that catalyze cellular reactions involving nucleic acids.
BIOCHEMICAL IMPOTRTANCE of Enzymes
❖ Biological catalyst
▪ They increase the rate of chemical reactions taking place within living
cells with out changing themselves.
▪ As catalyst, enzymes are not consumed during the reaction but merely help
the reaction occur more rapidly.
❖ Specificity
▪ A given enzyme is very selective
▪ Both in the substances with which it interacts and in the reaction
that it catalyzes
❖ Regulate metabolism
▪ play key role in the degradation and synthesis of nutrients: ex.
digestion
presence and maintenance of a complete and balanced set of enzymes is
essential for the breakdown of nutrients to supply energy or to harness
energy to power cell motility and activity
▪ Synthesis of biomolecules
the assembly of those building blocks into proteins, DNA, membranes,
cells, and tissues
TERMS DEFINITION
simple enzyme • is an enzyme composed only of protein (amino acids) not bound to any nonproteins
conjugated enzyme • is an enzyme that has a nonprotein part in addition to a protein part
apoenzyme • is the protein part of a conjugated enzyme or holoenzyme
• enzyme lacking an essential cofactor
cofactor • is the nonprotein part of a conjugated enzyme or holoenzyme
• serve functions similar to those of prosthetic groups but bind in a transient, dissociable
manner either to the enzyme or to a substrate such as ATP.
prosthetic group • Tightly bound cofactor to the apoenzyme
holoenzyme • is the biochemically active conjugated enzyme produced from an apoenzyme and a
cofactor
• Intact and functional enzyme containing all cofactors/ coenzyme
Coenzyme or • is a small organic molecule that serves as a cofactor in a conjugated enzyme
cosubstrate
activator • the inorganic cofactor
Substrate (S) • is the reactant in an enzyme-catalyzed reaction
• biomolecule that enzymes react with
Product (P) • the biomolecules formed by enzyme mediated reactions
metal-activated • Enzymes that require a metal ion cofactor
enzymes
metalloenzymes. • enzymes that contain tightly bound metal ions
Enzyme and substrate interaction
 ENZYME

Nature
of Conjugated
enzyme
Simple Enzyme
Ex. Pancreatic
Ribonuclease

Enzyme:
Apoenzyme Cofactor

PROSTHETIC Coenzyme/ Activator

Cosubstrate
GROUP

METAL ION
Fe 2+, Mn 2+,Zn 2+,Mg2+,
Ca2+,K+,Cu2+, Co2+

METAL-ACTIVATE
D ENZYME
(needs ion)

METALLOENZYME
(has tightly bound
ions)
Cofactor, Coenzyme,
Prothetic group?
• Cofactor – is the nonprotein part of the conjugated enzyme. It
is generally either a small organic molecule or an inorganic
ion (usually a metal ion)

• Coenzyme are organic non-protein compound that binds with

an enzyme to catalyze a reaction. Just like enzymes can be
reused and recycled without changing reaction rate or
effectiveness.
• Prosthetic Groups are distinguished by their tight, stable
incorporation into a protein’s structure by covalent or
noncovalent forces
 T
SUBS
RATE
 Coenzymes:
Vitamins Coenzyme Group transferred
Vit. B1 • Thiamin pyrophosphate (TPP) aldehydes
Thiamin
Vit. B2 • flavin mononucleotide (FMN) hydrogen atoms
Riboflavin • flavin adenine dinucleotide (FAD)
Vit. B3 • nicotinamide adenine dinucleotide (NAD1) hydrogen atoms
Nicotinic acid • nicotinamide adenine dinucleotide phosphate
(NADP1)
Vit. B5 • coenzyme A (CoA) acyl groups
Pantothenic acid
Vit. B6 • pyridoxal-5-phosphate (PLP) amino groups
Pyridoxine • pyridoxine-5’-phophate (PNP)
• pyridoxamine-5’-phosphate (PMP)
Vit. B7 • biotin carbon dioxide (carboxyl
Biotin group)
Vit. B9 • tetrahydrofolate (THF) one-carbon groups other
Folic acid than CO2
Vit. B12 • Methylcobalamin (Cobalt as the prosthetic methyl groups, hydrogen
Cyanocobalamin group metal ion) atoms
 Metalloenzyme:
Metal Enzyme Function
ion
Cu2+, Superoxide Destroy superoxide anion
Zn2+ dismutase
Zn2+ Alcohol They oxidize a range of aliphatic and aromatic alcohols to their corresponding
dehydrogenase aldehydes and ketones using NAD+ as a coenzyme.
DNA polymerase Synthesize DNA

Carboxypeptidase A is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal
(C-terminal) end of a protein or peptide
Mn2+ Pyruvate Synthesize oxaloacetate
carboxylase

Arginase Synthesize Urea

Fe Hemoglobins transports oxygen from the lungs to the capillaries of the tissue.

Cytochromes carry electrons between two segments of the electron-transport chain.

Cytochrome P450 enzymes play a role in the synthesis of many molecules including
steroid hormones, certain fats (cholesterol and other fatty acids), and acids used to
digest fats (bile acids). Additional cytochrome P450 enzymes metabolize external
substances, such as medications that are ingested, and internal substances, such as
toxins that are formed within cells.
Cu2+ Cytochrome hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic
Oxidase side-chains
 Fig.7: Methylcobalamin (coenzyme)
Fig.6: Hemoglobin (metalloenzyme)
 NOMENCLATURE and CLASSIFICATION
OF ENZYME
A. Based upon the substance they act upon (substrate)
- the suffix “ase” is added to the name of the substrate
1. amylase acts on starch
2. maltase acts on maltose
3. cellulase act on urea
4. lipase acts on fats
Except for:
▪ Pepsin – in gastric juice (stomach)
▪ Trypsin – in pancreatic juice (small intestine)
▪ Ptyalin – in saliva
▪ Rennin – the milk curding enzyme
NOMENCLATURE and CLASSIFICATION
OF ENZYME
NOMENCLATURE and CLASSIFICATION
OF ENZYME
B. Based upon the reaction enhanced - the suffix
“ase” is added to the type of chemical reaction
activated
1. Oxidase – oxidation reaction
2. decarboxylase - decarboxylation
3. transaminase - transamination
4. hydrolase - hydrolysis
except: urease – hydrolysis of urea
lactase – hydrolysis of lactose
sucrase – hydrolysis of sucrose
cellulase – hydrolysis of cellulose
5. hydrase or dehydrase – reversible addition or
removal of water
NOMENCLATURE and CLASSIFICATION
OF ENZYME
 IUB CLASSIFICATION OF ENZYME:
Enzymes are classified according to the reaction
CLASSIFICATION OFthey
ENZYME: IUB
catalyze
1. OXIDOREDUCTASE
OXIDOREDUCTASE
1.• Oxidation-Reduction
• is an enzyme that catalyzes an oxidation–reduction reaction.
reaction
• Example:
• Example: Lactate
Lactate dehydrogenase
dehydrogenase
Catalyzed
Phosphate reaction: Lactic acid + NAD ----- Pyruvic acid + NADH+ H+
dehydrogenase

“browning reaction” caused by phenolase (or polyphenoloxidase), a conjugated

enzyme in which copper is present:

• ORGANIC OXIDATION rxn enzyme

• an oxidation that increases the number of C-O bonds and/or decreases the
number of C-H bonds.
substrate
• ORGANIC REDUCTION rxn
• a reduction that decreases the number of C-O bonds and/or increases the
number of C-H bonds.
 IUB CLASSIFICATION OF ENZYME:
Enzymes are classified according to the reaction
they catalyze
2. TRANSFERASES
• is an enzyme that catalyzes the transfer of a functional
group other than hydrogen (ex. methyl, acyl, amino or
phosphate groups) from one molecule to another.
• Examples: transaminases and kinases
 IUB CLASSIFICATION OF ENZYME:
Enzymes are classified according to the reaction
they catalyze
3. HYDROLASE
• an enzyme that catalyzes a hydrolysis reaction in which the
addition of a water molecule to a bond causes the bond to
break
• Hydrolysis reactions are central to the process of digestion.
• Examples:
• Carbohydrases - breaking of glycosidic bonds in oligo- and
polysaccharides
• Proteases- breaking of peptide linkages in proteins
• lipases - breaking of ester linkages in triacylglycerols.
 IUB CLASSIFICATION OF ENZYME:
Enzymes are classified according to the reaction
they catalyze
3. HYDROLASE
•
 IUB CLASSIFICATION OF ENZYME:
Enzymes are classified according to the reaction
they catalyze
4. LYASE
• is an enzyme that catalyzes the addition of a group to a
double bond or the removal of a group to form a double
bond in a manner that does not involve hydrolysis or oxidation.
• Example:
• Dehydratase effects the removal of the components of
water from a double bond
• Hydratase effects the addition of the components of
water to a double bond.
 IUB CLASSIFICATION OF ENZYME:
Enzymes are classified according to the reaction
they catalyze
5. ISOMERASE
• an enzyme that catalyzes the isomerization
(rearrangement of atoms or interconversion of
optical, geometric, or positional isomers) of a
substrate in a reaction, converting it into a molecule
isomeric with itself. There is only one reactant and
one product in reactions where isomerases are
operative.
 IUB CLASSIFICATION OF ENZYME:
Enzymes are classified according to the reaction
they catalyze
6. LIGASE or SYNTHETASE
• an enzyme that catalyzes the bonding together of
two molecules into one with the participation of ATP.
• ATP involvement is required because such reactions
are generally energetically unfavorable and they
require the simultaneous input of energy obtained by
a hydrolysis reaction in which ATP is converted to
ADP
Main Classes and Subclasses of Enzymes
Main Class • Selected subclasses Type of Reaction Catalyzed

OXIDOREDUCT • oxidases • oxidation of a substrate

ASES • reductases • reduction of a substrate
• dehydrogenases • introduction of double bond (oxidation) by formal removal of two H
atoms from substrate, the H being accepted by a coenzyme
TRANSFERASES • Transaminases • transfer of an amino group between substrates
• Kinases • transfer of a phosphate group between substrates
HYDROLASES • Lipases • hydrolysis of ester linkages in lipids
• Proteases • hydrolysis of amide linkages in proteins
• Nucleases • hydrolysis of sugar–phosphate ester bonds in nucleic acids
• Carbohydrases • hydrolysis of glycosidic bonds in carbohydrates
• phosphatases • hydrolysis of phosphate–ester bonds
LYASES • dehydratases • removal of H2O from a substrate
• decarboxylases • removal of CO2 from a substrate
• deaminases • removal of NH3 from a substrate
• hydratases • addition of H2O to a substrate

ISOMERASES • Racemases • conversion of D isomer to L isomer,or vice versa

• Mutases • transfer of a functional group from one position to another in the same
molecule
LIGASES • Synthetases • formation of new bond between two substrates, with participation of
• Carboxylases ATP
• formation of new bond between a substrate and CO2, with participation
of ATP
 OVERVIEW: MECHANISM OF ENZYME ACTION

Enzyme Active Site

the relatively small part of an enzyme’s
structure that is involved in catalysis. Usually
a “crevicelike” location the enzyme.
Enzyme-Substrate Complex
the intermediate reaction species that is
formed when the substrate bind to the active
site of an enzyme.
MODELS OF ENZYME ACTION
1. Lock-and-Key Model
(Emil Fischer)
- only a substrate whose
shape and chemical nature are
complementary to those of the
active site can interact with the
enzyme.
MODELS OF ENZYME ACTION
2. Induced-Fit Model (Daniel
F. Koshland)
• is a result of the enzyme’s
flexibility
• the enzyme active site,
although not exactly
complementary in shape to
that of the substrate, is
flexible enough that it can
adapt to the shape of the
substrate.

Enzyme
specificity
:the extent to which an
enzyme’s activity is restricted
to a specific substrate, a
specific group of substrates, a
specific type of chemical bond,
or a specific type of chemical
reaction
Absolute specificity
• enzyme will catalyze only one reaction.
• Ex. Catalase
• catalyzes the conversion of hydrogen
peroxide (H2O2) to O2 and H2O.
Hydrogen peroxide is the only
substrate it will accept.
Group specificity
• the enzyme will act only on molecules that
have a specific functional group, such as
hydroxyl, amino, or phosphate groups.
• Examples:
• Carboxypeptidase - it cleaves amino
acids, one at a time, from the carboxyl
end of a peptide chain.
• Esterases- acts on ester bonds
• Peptidases-acts on peptide bonds
• Glycosidases- acts on glycosidic bonds.
 Linkage specificity
•the enzyme will act on a particular type
of chemical bond, irrespective of the
rest of the molecular structure. This is
the most general of the common
specificities.
•Ex. Phosphatases
•hydrolyze phosphate-ester bonds in all
types of phosphate esters

Enzyme
Stereochemical specificity
specificity • some enzymes are specific to only one
isomer even if the compound is one type
of molecule:
• Ex. glucose oxidase catalyzes the oxidation
of β-D-glucose but not α-D-glucose, and
arginase catalyzes the hydrolysis of
L-arginine but not D-arginine. Maltase
catalyzes the hydrolysis of α- but not β
–glycosides.
FACTORS THAT AFFECT THE
RATE OF ENZYME ACTIVITY
FACTORS THAT AFFECT THE
RATE OF ENZYME ACTIVITY

Chemical connection:
H. pylori and Stomach
Ulcers
Extremophile • is a microorganism that thrives in extreme
environments, environments in which humans
and most other forms of life could not
survive.

EXTREMOZYME
• is a microbial enzyme active at conditions
that would inactivate human enzymes as well
as enzymes present in other types of higher
organisms.
• cellulases, amylases, xylanases, proteases,
pectinases, keratinases, lipases, esterases,
catalases, peroxidases and phytases
USE:
• detergent formulations
Yellow Stone National Park and
Northeast Pacific Ocean • the petroleum industry during oil well
drilling operations
Extremophile
• acidophiles
• optimal growth at pH levels of 3.0 or below
• alkaliphiles
• optimal growth at pH levels of 9.0 or above
• halophiles
• a salinity that exceeds 0.2 M NaCl needed for growth
• Hypothermophiles
• a temperature between 80°C and 122°C needed to thrive
• cryophiles
• a temperature of 15°C or lower needed for growth
• piezophiles
• a high hydrostatic pressure needed for growth
Extremophile: H. pylori and Stomach Ulcers

• Helicobacter pylori, commonly called H.

H. pylori bacteria
pylori, is a bacterium that can function
in the highly acidic environment of the
stomach
• causes more than 90% of duodenal
ulcers and up to 80% of gastric ulcers.
• TREATMENT: acid-suppression or
acid-neutralization medications PLUS
antibiotics(tetracycline, amoxicillin,metronidazol
e,clarithromycin, and levofloxacin).
• Transmission: fecal–oral or oral–oral
routes.

UREASE
UREA in the surface of the bacterium--------------- NH3+
ENZYME INHIBITION

Clinical Case Scenario:

A 42 year old patient Question:
was rushed in a hospital
due to accidental What was the relevance
intoxication of methanol. of administering alcohol
Immediately upon the (ethanol) to an incident
of poisoning caused by
arrival and examination
another alcohol?
the patient was given
ethanol administered
intravenously.
 Methanol

Ethanol
10X affinity

alcohol
dehydrogenase

formaldehyde
 ENZYME INHIBITION

Competitive Enzyme Inhibitor Noncompetitive Enzyme Inhibitor Irreversible Enzyme Inhibitor

a molecule closely a molecule that binds to a site on an a molecule that forms a

resembling the substrate.
Binds to the active site and
temporarily prevents
substrates form occupying it,
thus blocking the reaction.
enzyme that is not the active site.
The normal substrate still occupies
the active site but the enzyme
cannot catalyze the reaction due to
the presence of the inhibitor.
covalent bond to a part of
the active site, permanently
preventing substrate from
occupying.
 REASON FOR REGULATION: Waste of
energy
Regulation of Enzyme A cell that continually produces large
Activity amounts of an enzyme for which substrate
concentration is always very low
A product of an enzyme-catalyzed
reaction that is present in plentiful (more
than needed) amounts.

WAYS OF REGULATION
(1) feedback control associated with
allosteric enzymes
(2) production of enzymes in an inactive
form:
proteolytic enzymes and zymogens
(3) covalent modification
 Allosteric Enzymes
- Greek allo, means “other,” and
stereos, means “site or space.”
- is an enzyme with two or more protein
chains (quaternary structure) and two
kinds of binding sites (substrate and
regulator)
❖ Regulators- substances that bind
at regulatory sites of allosteric
enzymes.
❖ Positive regulator increases
enzyme activity; the shape of the
active site is changed such that it
can more readily accept substrate.
❖ Negative regulator (a
noncompetitive inhibitor; decreases
enzyme activity; changes to the
active site are such that substrate
is less readily accepted.
Feedback Control associated with Allosteric enzyme

a process in which activation or inhibition of the first

reaction in a reaction sequence is controlled by a
product of the reaction sequence.
Proteolytic Enzymes and Zymogens
proteolytic enzyme
• an enzyme that catalyzes the
breaking of peptide bonds
that maintain the primary
structure of a protein.
zymogen or proenzyme
• is the inactive precursor of a
proteolytic enzyme.

EXAMPLES:
▪ Pepsinogen ------- pepsin
▪ Tyrpsinogen ------- trypsin
▪ Chymotrypsinogen ------ chymotrypsin
▪ Angiotensinogen ------- angiotensin
 Prescription Drugs That
Inhibit Enzyme Activity
ACE Inhibitors Illustration: Effect of ACE inhibitors
- MOA: Blocks the action of
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
angiotensinogen (specifically angiotensin
(Angiotensinogen)
I) to form the vasoconstrictor,
a2- globulin in blood
angiotensin II. These inhibitors also
Renin (kidney)
diminish the rate of bradykinin (potent
vasodilator) inactivation.
- Effect: Vasodilation occurs as a result of Angiotensin I (inactive)
the combined effects of lower
vasoconstriction caused by diminished ACE Inhibitors ACE
levels of angiotensin II and the potent
vasodilating effect of increased Asp-Arg-Val-Tyr-Ile-His-Pro-Phe +
His-Leu
bradykinin. Decrease aldosterone: Decrease Angiotensin II (vasoconstrictor)
Retention of sodium and water

Increase Levels of
Decrease output of sympathetic nervous bradykinin
system
Increase vasodilation of vascular smooth
Overall Effect: DECREASE BLOOD muscle
PRESSURE
Prescription Drugs That Inhibit Enzyme
Activity
Sulfa Drugs
▪ Folic acid coenzymes are required
for the synthesis of purines and
pyrimidines (precursor of RNA and
DNA) and other compounds for
cellular growth and replication.
▪ Folic acid deficiency retards
growth of the bacteria and can
eventually kill them
▪ Sulfonamides are synthetic
structural analogs of PABA
▪ MOA: acts as a competitive
inhibitor to enzymes in the
biosynthetic pathway for converting
PABA into folic acid, specifically
competes with the substrate(PABA)
for the enzyme dihydropteroate
synthetase.
Prescription Drugs That Inhibit Enzyme
Activity
Penicillins
▪Transpeptidase, an enzyme that
catalyzes the formation of peptide
cross links between polysaccharide
strands in bacterial cell walls. These
cross links strengthen cell walls
necessary to protect the bacterium
from lysis

▪MOA: Interfere with the last step of Penicillin, once bound to the active site, the b-lactam
bacterial cell wall synthesis ring opens as the highly reactive amide bond forms a
covalent bond to a critical serine residue required for
(transpeptidation or cross-linkage) normal catalytic action. The result is an irreversibly
thus inhibiting transpeptidase enzyme inhibited transpeptidase enzyme.
(as very selective competitive
inhibitor) exposing the osmotically less
stable membrane causing lysis.
Prescription Drugs That Inhibit Enzyme Activity

Penicillins Penicillinase resistant

Penicillin: Amox and
Methicillin
▪ Penicillinase, an enzyme
which protects bacteria
from penicillin.
▪ Penicillinase selectively
binds penicillin and
catalyzes the opening of
the b-lactam ring before
penicillin can form a
covalent bond to the
enzyme. Once the ring is
opened, the penicillin is
no longer capable of
inactivating
transpeptidase.
Food-Enzyme Interactions That Affect Prescription Medications

cytochrome P450s: an enzyme that helps metabolize drugs in the

body

Amiodarone A drug used to treat and prevent abnormal

heart rhythms (arrhythmias)
Buspirone,sertraline Antidepressants

Carbamazepine An anti-seizure medication

Cyclosporine Immunosuppressant drugs

“GRAPEFRUIT EFFECT: Inhibition of
cP450 by the compound BERGAMOTTIN
and 6',7'-Dihydroxybergamottin of a
grapefruit:
Felodipine , nifedipine, Calcium-channel blockers used to treat high
nimodipine, nisoldipine blood pressure
Saquinavir An HIV medication
Simvastatin, lovastatin , Statins used to treat high cholesterol
atorvastatin
ENZYME ACTIVITY: Inhibitors
& Inducers
CYP 450 Inhibitors CYP 450 Inducers
SICKFACES.COM
– Sodium valproate CRAP GPS
– Isoniazid – Carbamazepines
– Cimetidine – Rifampicin
– Ketoconazole
– Alcohol (chronic)
– Fluconazole
– Alcohol (binge drinking) – Phenytoin
– Chloramphenicol
– Erythromycin – Griseofulvin
– Sulfonamides
– Phenobarbitone
– Ciprofloxacin
– Omeprazole – Sulphonylureas
– Metronidazole
– Grapefruit juice
BIOCHEMICAL IMPOTRTANCE: Enzymes
Important tool in diagnostic procedures (involving
enzyme assay)
• assist to know damaged tissues
• assist the extent of tissue damage
• helps to monitor the course of the
disease
• used as a therapeutic means of
diagnosing a vast array of diseases
MEDICALLY USEFUL ENZYME
Creatine kinase
is an enzyme that is found primarily in skeletal and cardiac
muscle and in smaller fractions in the brain
TYPES OF CK
• muscle (CK-MM)
• brain (CK-BB),
• cardiac tissue (CK-MB) - important marker in
the diagnosis of acute myocardial infarction
(AMI)
MEDICALLY USEFUL ENZYME
• TROPONIN
Description
• Troponin I and T are sensitive markers of cardiac injury.
• Troponin I is found solely in the cardiac muscle, and
• Troponin T is found in both cardiac and skeletal muscle.
Clinical Significance
• Troponin levels begin to rise within 4 hours of onset of chest pain. Levels
should be drawn on admission and within 8 to 12 hours thereafter. Patients
with elevated troponin levels are considered at high risk for a significant
cardiac event.
• Approximately 30% of patients with no elevation in CK-MB may
demonstrate elevated troponin and thus be diagnosed with a non-Q-wave
myocardial infarction.
MEDICALLY USEFUL ENZYME
• GASTROINTESTINAL TESTS
Alanine Aminotransferase/ serum glutamic
pyruvic transaminase (SGPT).
- liver tissue. It is also located in myocardial, muscle, and renal tissue
- considered a specific marker for liver disease
Aspartate Aminotransferase/ serum glutamic
oxaloacetic transaminase (SGOT
- found in the liver. It is also present in the heart, kidney, pancreas,
lungs, and skeletal muscle
For diagnosis of liver disease
MEDICALLY USEFUL ENZYME
GASTROINTESTINAL TESTS
• g-Glutamyl Transpeptidase
an enzyme found in the liver, kidney, and pancreas. GGT levels are
useful in the diagnosis and monitoring of alcoholic liver disease
Increased GGT may be seen in alcoholic liver disease, metastatic liver
disease, obstructive jaundice, cholelithiasis, and pancreatitis
• Lactate Dehydrogenase
enzyme involved in the interconversion of lactate and pyruvate.
is found in many tissues, including heart, brain, liver, skeletal muscle,
kidneys, lungs, and RBCs.
LDH4 and LDH5 are present in liver tissue, and elevations may be
seen in liver disease such as hepatitis and cirrhosis.
LDH1 and LDH2 may be useful in the diagnosis of myocardial
infarction
MEDICALLY USEFUL ENZYME
GASTROINTESTINAL TESTS
• Lipase
• enzyme that aids in the digestion of fat. It is primarily secreted
by the pancreas.
• useful in the diagnosis of pancreatitis and is considered a more
specific marker for pancreatitis than amylase
• Amylase
• enzyme that aids in digestion by breaking down complex
carbohydrates into simple sugars.
• The majority of amylase is produced in the pancreas and
salivary glands, and lesser amounts are secreted by the
fallopian tubes, lungs, thyroid, and tonsils
• Serum amylase levels are most often used in the diagnosis of
acute pancreatitis
Condition
Myocardial infarction
Acute hepatitis
Muscular dystrophy
Megaloblastic anemia
Sickle cell anemia
Arthritis with joint infections
Isoenzyme pattern
Moderate elevation of LDH1, slight
elevation of LDH2
Large elevation of LDH5, Moderate
elevation of LDH4
Elevation of LDH1-3
Large elevation of LDH1
Moderate elevation of LDH1 and LDH2
Elevation of LDH5
Serum Enzyme Major diagnostic use
Amylase Liver and pancreatic disease
Acid phosphate Prostate cancer
Alkaline phosphatase Liver and bone disease
Creatine phosphokinase Myocardial infarction and muscle
disorders
Lactate dehydrogenase Myocardial infarction, leukemia, anemia
Renin Hypertension
Serum Enzyme Major diagnostic use
Glutamic oxaloacetic transaminase Myocardial infarction
(SGOT)
Glutamic pyruvic transaminase (SGPT) Infectious hepatitis
Trypsin Acute pancreatitis
Ceruplasmin Wilson’s disease
 Medical Uses of Enzymes
Serum Enzyme Major Diagnostic Use: Condition Indicated by
Abnormal Level
lactate dehydrogenase (LDH)
LDH1 and LDH2 heart disease (ex. AMI),
LDH4 and LDH5 liver disease (hepatitis and cirrhosis)
creatine phosphokinase (CPK) Heart disease

aspartate transaminase (AST) or heart disease, liver disease, muscle damage

serum glutamic oxaloacetic transaminase (SGOT)
alanine transaminase (ALT) or heart disease, liver disease (Viral hepatitis) ,muscle
serum glutamic pyruvic transaminase (SGPT) damage
gamma-glutamyl transpeptidase (GGTP heart disease, liver disease (alcoholic liver disease)

alkaline phosphatase (ALP) bone disease, liver disease

Amylase Acute pancreatitis

Lipase (more specific marker)
Ceruloplasmin Hepatolenticular degeneration (Wilson’s disease)

Phosphatase, acid Metastatic carcinoma of the prostate

Phosphatase, alkaline (isozymes) Various bone disorders, obstructive liver diseases