BIOCHEMISTRY REVIEWER – MIDTERM 2024

LIPIDS MICELLE
 Biological compounds that are soluble  Spherical cluster of molecules in which:
only in nonpolar solvents  Polar chains are on the surface
 Saponifiable lipids - Contain esters that  Nonpolar chains are located in the
are hydrolyzed under basic conditions interior and are held together by weak
 Classified based on number of dispersion forces
components in the structure  Micelle formation and structure are
 Simple lipids: Contain one or more important for biological functions, such as
fatty acids and an alcohol the transport of insoluble lipids in blood
 Complex lipids: Contain more than
two types of components Characteristics of Fatty Acids
 Components include an alcohol,  Usually straight-chain carboxylic acids (no
fatty acids, and other branching)
components  Sizes range from 10–20 carbons
 Nonsaponifiable lipids - Do not contain  Usually have an even number of carbon
esters and cannot be hydrolyzed atoms
 Can be:
 Saturated - Contain no C=C bonds
THE MAJOR TYPES OF LIPIDS  Unsaturated - Contain one or more
C=C bonds, usually in the cis
configuration

Some important fatty acids

FUNCTIONS OF LIPIDS
 Repel water
 Characteristic of protective wax CHARACTERISTICS OF
coatings found on some plants
 Energy-rich compounds with low densities UNSATURATED FATTY ACIDS
 Used as storage forms of energy in  Cis configuration creates a long kink, or
plants and animals bend, in the fatty acid chain, which
 Used as structural components, especially prevents the chains from packing closely
in the formation of cellular membrane together
 Leads to weaker intermolecular forces
and lower melting point
FATTY ACIDS  Fatty acids are liquids at room
 Building blocks of lipids temperature
 Long-chain carboxylic acids  Melting point decreases as the number of
 Long nonpolar tails are responsible for carbon double bonds increase
most of the fatty or oily characteristics  Fluidity of biological membranes is
of fat explained by the length of the chain
 Carboxyl group, or the polar head, is and presence of double bonds
very hydrophilic under conditions of
physiological pH Essential Fatty Acids
 Exists as —COO−)  Not synthesized within the body and are
obtained through diet

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 Linoleic (omega-6 fatty acid) and linolenic Reactions of Fats and Oils –
(omega-3 fatty acid) acid
 Used to produce hormonelike
Saponification
 Process of reacting triglycerides with a
substances that regulate:
strong base to produce glycerol and
 Blood pressure and blood clotting
soaps (salts of the fatty acids)
 Blood lipid levels
 Properties of the soap depend on the
 Immune and inflammation
base used
responses
 Sodium salts (hard salts) are found in
 Can be converted to other omega-3
cake soap
and omega-6 fatty acids
 Potassium salts (soft soaps) are found
Fats and Oils in shaving creams and liquid soap
 Esters that contain an: preparations
 Alcohol portion, which is derived from  Traditional soap making:
glycerol  Used animal fat as the source of
 Acid portion, which is furnished by triglycerides
fatty acids  Used lye (crude NaOH) or an aqueous
 Esterification results in the formation of extract of wood ash as the source of
triglycerides or triacylglycerols the base
 Natural triglycerides are mixtures of  Was lost with the fall of the Roman
different triglyceride molecules Empire

Differences between Fats and Reactions of Fats and Oils –

Oils Hydrogenation
 Fats are:  Reaction by which fatty acid double
 Derived from animal sources bonds are converted to single bonds
 Solids at room temperature  Decreases the degree of unsaturation
 Primarily composed of triglycerides of  Increases the melting point
long-chain saturated fatty acids  Complete hydrogenation results in a hard
 Oils are: and waxy product
 Derived from plant and fish sources  Partial hydrogenation results in a smooth,
 Liquids at room temperature creamy product
 Composed of triglycerides that contain  Some fatty acid molecules in the cis
unsaturated fatty acids configuration are isomerized into trans
fatty acids
Excessive Dietary Fat  Consumption of trans fatty acids raises
 Influences the development of chronic blood cholesterol levels
diseases and plays a role in raising blood  Current dietary advice is to reduce the
cholesterol levels consumption of products that contain
 High cholesterol is a risk factor in the saturated and trans fatty acids
development of coronary heart
disease, which is the leading cause of Waxes
death in Americans every year  Esters of long-chain fatty acids and long-
chain alcohols
Reactions of Fats and Oils –  Water insoluble and not easily hydrolyzed
Hydrolysis  Occur as protective coatings in nature on
skin, fruits, leaves, and fur
 Important for the digestion of oils and fats
 Used commercially to make cosmetics,
 Results in the formation of glycerol and
candles, ointments, and protective
fatty acids
polishes
 Process can be catalyzed by enzymes
(lipases) of the digestive system Phosphoglycerides
 Complex lipids that contain:
 Glycerol

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 Fatty acids needed to break down these complex

 Phosphoric acid lipids
 Aminoalcohol component
 Referred to as phospholipids
 Contain one of the following alcohols
attached to the phosphate group:
 Choline Membrane Structure
 Ethanolamine  Most membranes are 60% lipid and 40%
 Serine protein
 Predominant types of lipids include
Phosphoglycerides – Lecithins phosphoglycerides, sphingomyelin,
 Contain choline and cholesterol
 Important structural components of most  Fluid-mosaic model
cell membranes  Model of membrane structure in which
 Act as emulsifying and micelle-forming proteins are embedded in a flexible
agents lipid bilayer
 Hydrophobic chains extend toward
Phosphoglycerides – Cephalins the inside
 Contain ethanolamine or serine  Hydrophilic groups are oriented
 Found in most cell membranes, especially toward th outsiede
in brain tissue and blood platelets  When a lipid bilayer is broken and the
 Act as emulsifiers tails are exposed to water, the
resulting repulsion causes the bilayer
Sphingolipids to re-form, and the break seals
 Complex lipids that contain sphingosine
spontaneously
rather than glycerol
 Membrane lipids contain unsaturated
 Sphingosine - Long-chain unsaturated
fatty acid chains that fit into bilayers
aminoalcohol
more loosely than saturated fatty acids
 Types
 Increases flexibility or fluidity of the
 Sphingomyelin - Contains a
membrane
sphingosine, a fatty acid, and
 Proteins either float in the lipid bilayer or
phosphate and choline groups
extend completely through the bilayer
 Glycolipid: Contains a sphingosine, a
 Lipid molecules are free to move
fatty acid, and a carbohydrate unit
laterally within the bilayer
Sphingomyelin Steroids
 Choline is attached to the sphingosine via
 Broad class of compounds that contain
a phosphate group
four rings fused in a particular pattern
 Contains an amide linkage instead of an
 Soluble in nonpolar solvents
ester linkage
 Include cholesterol and bile salts
 Found in the myelin sheath surrounding
nerves and in brain and nerve tissues Cholesterol
 Most abundant steroid in the human body
Glycolipids  Essential component of cell membranes
 Known as cerebrosides because of their
 Precursor for other important steroids
abundance in brain tissue
 Present in food and is synthesized in the
 Do not contain phosphate
liver
Sphingolipids and Diseases  Strong correlation exists between
cholesterol levels in the blood and
 Several human diseases result from an
atherosclerosis (hardening of arteries)
abnormal accumulation of sphingomyelins
and glycolipids in the body
 Each of these diseases is the result of
an inherited absence of an enzyme

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Bile Adrenocorticoid Hormones

 Yellowish-brown or green liver secretion  Produced by the adrenal cortex
that is stored and concentrated in the  Classified on the basis of function
gallbladder  Mineralocorticoids - Regulate the
 When partially digested fatty food concentration of ions in bodily fluids
enters the small intestine, the  Example
gallbladder contracts and empties bile  Aldosterone increases
into the intestine absorption of Na+ and Cl– and
 Chief constituents - Bile salts and waste is involved in water balance in
components the body
 Sodium glycocholate is a principal bile  Glucocorticoids - Enhance
salt carbohydrate metabolism
 Waste components include cholesterol  Example
and bile pigments  Cortisol increases glucose and
glycogen concentrations and
Functions of Bile Salts has powerful anti-inflammatory
 Emulsification of lipids in the intestine by effects in the body
breaking large lipid globules into smaller
droplets Sex Hormones
 Provides more surface area for  Produced by the testes (in men) and
hydrolysis reactions ovaries (in women)
 Emulsification of cholesterol found in bile  Help develop secondary sex
 High cholesterol levels in bile or high characteristics that appear at puberty
concentration of bile salts can lead to  Androgens
the formation of gallstones  Male sex hormones produced by
testes
Gallstones  Include testosterone, which promotes
 Passage of a gallstone causes normal growth of male genital organs
excruciating pain
 Can become lodged in the bile duct and Anabolic Steroids
prevent bile from passing into the  Growth-promoting steroids
duodenum, which prevents normal  Include testosterone and its synthetic
digestion of fats derivatives
 Results in:  Used by athletes to promote muscular
 Pain development without excessive
 Nausea and feeling of being ill masculinization
 Skin taking on a yellow color as bile  Side effects range from acne to deadly
pigments are absorbed into the liver tumors
blood  Affect the male reproductive system and
 Stool becoming gray-colored can cause:
because of the lack of excreted bile  Testicular atrophy
pigments  Decrease in sperm count
 Can be surgically removed  Temporary infertility

Steroid Hormones Female Sex Hormones

 Hormone: Chemical messenger secreted  Important in the reproductive process
by specific glands and carried by the  Estrogen
blood to a target tissue, where it triggers  Essential estrogens include estradiol
a particular response and estrone
 Categories  Involved in the development of the
 Adrenocorticoid hormones ovum
 Sex hormones  Progesterone

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 Causes changes in the uterine wall to Amino Acids and R Group

prepare it to accept a fertilized egg  Amino acids are categorized into groups
and maintain the resulting pregnancy based on the polarity of the R groups
 Neutral and nonpolar side chains (e.g.
Prostaglandins —CH3)
 Cyclical compounds synthesized in the  Neutral but polar side chains (e.g. —
body from the 20-carbon unsaturated CH2—OH)
fatty acid arachidonic acid  Basic side chains (e.g. —
 Designated by codes that refer to the ring CH2CH2CH2CH2—NH3+) or
substituents and the number of side-chain  Acidic side chains (e.g. —CH2—COO—)
double bonds
 Similar to hormones since they are Common Amino Acids of
intimately involved in a host of body
processes
Proteins
 Involved in:
 Regulation of menstruation
 Prevention of conception
 Induction of uterine contractions
 Stimulate blood clotting
 Lead to inflammation and fever, which
can be inhibited by aspirin

Therapeutic Potential of
Prostaglandins
 Prostaglandin E2 (PGE2) and
prostaglandin F2 (PGF2)
 Induce labor
 Used for therapeutic abortion in early
pregnancy
 PGE2 in aerosol form
 Used to treat asthma
 Opens up bronchial tubes by
relaxing the surrounding muscles
 Other prostaglandins inhibit gastric
secretions and are used to treat peptic
ulcers
 Many researchers believe that when they
are fully understood, prostaglandins will
be found useful for treating a much wider
variety of ailments

AMINO ACIDS
 Building blocks of proteins Stereochemistry of Amino Acid
 Only 20 amino acids are commonly found  In 19 of the 20 amino acids, the α-carbon
in natural proteins is chiral
 Alpha-amino acid: Contains both an  Glycine is the achiral amino acid
amino group and a carboxylate group  With few exceptions, the amino acids in
 Amino group is attached to the living systems exist in the ʟ form
carbon next to the carboxylate
group Amino Acid Properties
 Each amino acid has a name, a three-  White crystalline solids
letter abbreviation, and a one-letter  High melting points
abbreviation  High water solubilities

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 Exist in ionic form in solid state and in  Polypeptide: Intermediate chain length
solution polymer with less than 50 amino acids
 Protein: Polymer with more than 50 amino
Zwitterion acids
 Dipolar ion that carries both a positive  Amino acid residue: Amino acid that is a
and a negative charge as a result of an part of a peptide, polypeptide, or protein
internal acid–base reaction in an amino chain
acid molecule  By convention, peptides are written
 Net charge of the zwitterion is zero, but with the N-terminal residue on the left
the form in acid solution has a net and the C-terminal residue on the right
positive charge
 Converted into a negatively charged form Naming Peptides
when it loses a proton  Peptides are named by starting at the N-
 Isoelectric point: Characteristic solution terminal end of the chain and listing the
pH at which an amino acid has a net amino acid residues in order from left to
charge of zero right
 R group Isoelectric point  Structural formulas are simplified by
 Neutral About pH 6 representing peptide and protein
 Acidic Less than pH 6 structures in terms of three-letter
 Basic More than pH 6 abbreviations for the amino acid residues
 At pH values above the isoelectric point, with dashes to show peptide linkages
the amino acid has a net negative value
 At pH values below the isoelectric point, Important Peptides:
the amino acid has a net positive value Vasopressin and
 Amino acid solutions can act as buffers
because they react with both H3O+ and Oxytocin
OH-  Hormones released by the pituitary gland
 Classified as nonapeptides
Reactions of Amino Acid:  Have disulfide bridges
Oxidation  Disulfide bridge: Bond produced by the
 Cysteine, the only sulfhydryl (—SH)- oxidation of —SH groups on two
containing amino acid, can easily be cysteine residues
oxidized to form a disulfide bond (—S—S  Bond loops or holds two peptide
—) chains together
 Structures differ only in third and eighth
Reactions of Amino Acid: amino acid residues
Peptide Formation  Vasopressin is known as an antidiuretic
hormone
 Peptide bond formation enables amino
 Decreases urine formation
acids to make polymers by forming amide
 Oxytocin causes uterine contractions and
(peptide) linkages
stimulates lactation of mammary glands
 Dipeptides: Compounds formed when two
amino acids are bonded by an amide Important Peptides:
linkage
 Peptide linkage or peptide bond: Adrenocorticotropic
Amide linkage between amino acids Hormone (ACTH)
that results when the amino group of
 Synthesized by the pituitary gland
one acid reacts with the carboxylate
 Contains 39 amino acids residues
group of another
 Has no disulfide bridges
 Order of linkage is important because two
 Regulates the production of steroids in
different dipeptides can be formed when
the cortex of the adrenal gland
two unique amino acids react
 Peptide: Amino acid polymer of short
chain length

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Characteristics of Proteins –
Size
 Large natural polymers of amino acids
 Have molecular weights that vary from
about 6000 to several million u
 Too large to pass through cell membranes
 Contained inside the normal cells
where they are formed
 Can leak out if cell is damaged by
disease or trauma Classification of Proteins Based
 Persistent excessive amounts of
protein in urine can indicate
on Their
damaged kidneys Shape
 Presence of enzymes in blood can  Fibrous proteins: Made up of long rod-
indicate a heart attack shaped or stringlike molecules that
 Human cell contains 9000 different intertwine to form fibers
proteins, and the human body contains  Water insoluble and components of
100,000 different proteins connective tissue, elastic tissue, hair,
and skin
Acid–Base Properties of  Examples - Collagen, elastin, and
Proteins keratin
 Proteins take the form of zwitterions  Globular proteins: Form stable
 Have characteristic isoelectric points suspensions or dissolve in water
and can behave as buffers in solutions  Transport proteins
 Can be in solution or form stable  Examples - Hemoglobin and
colloidal dispersions transferrin
 Depends on the repulsive forces
acting between molecules with like Classification of Proteins Based
charges on their surfaces
 Repulsive forces are at their on Composition
weakest at the isoelectric point,  Simple proteins: Made up entirely of
when the net charge is zero amino acid residues
 Proteins tend to clump together  Conjugated proteins: Contain amino acid
and precipitate from solutions in residues and other organic or inorganic
which pH is equal to or close to components
the isoelectric point  Prosthetic groups: Non–amino acid
parts of conjugated proteins
Biological Functions of Proteins
Primary Protein Structure
 Linear sequence of amino acid residues in
a protein chain
 Determines secondary and tertiary
structures
 Important for the functioning of proteins
 Small variations in the primary
structure can cause profound
differences in the functioning of
proteins

Secondary Protein Structure

 Arrangement of protein chains into
patterns as a result of hydrogen bonds

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between amide groups of amino acid Quaternary Protein Structure

residues in the chain  Arrangement of subunits that form a
 Includes larger protein
 α-helix AND β-pleated sheet  Subunit: Polypeptide chain that has
primary, secondary, and tertiary
α-Helix Structure structures
 Occurs when a single protein chain twists  Conjugated proteins with quaternary
to resemble a coiled helical spring structure contain subunits and prosthetic
 Held in shape by intramolecular groups, which may be organic or
hydrogen bonds between carbonyl inorganic components
oxygens and amide hydrogens in  Heme is an example of a prosthetic
adjacent turns of the helical backbone group
 All amide groups in the helix are  Hemoglobin
hydrogen bonded  Subunits - Two identical alpha chains
 Two or more helices interact to form a and two identical beta chains
cable in α-Keratin (found in hair), myosin  Held together by hydrophobic
(found in muscle), epidermin (found in forces
skin), and fibrin (found in blood clots)  Contains four heme groups
β-Pleated Sheet Protein Hydrolysis
 Occurs when several protein chains lie  Heating of a peptide or protein in the
side by side and are held in position by presence of an acid or base causes it to
hydrogen bonds between the carbonyl break into smaller peptides or amino
oxygen atoms of one chain and the amide acids based on:
hydrogen atoms of an adjacent chain  Hydrolysis time
 Found extensively only in silk protein  Temperature
Tertiary Protein Structure  pH
 Process of protein digestion involves
 Specific three-dimensional shape of a
hydrolysis reactions that are catalyzed by
protein resulting from interactions
enzymes in the digestive tract
between R groups of amino acid residues
 Types of R-group interactions Protein Denaturation
 Disulfide bridges - Form between  Process by which a protein loses its
cysteine residues characteristic native structure and
 Salt bridges - Result of ionic bonds function
that form between the ionized side  Native state: Natural three-
chain of an acidic amino acid and the dimensional conformation of a
side chain of a basic amino acid functional protein
 Hydrogen bonds - Form between side  Occurs when protein is exposed to
chains that possess the following physical or chemical conditions
functional groups:  Leads to loss of biological activity
(function)
 May cause some proteins to
precipitate
 Hydrophobic interactions - Form between
ENZYMES
nonpolar residues
 Proteins that catalyze chemical reactions
 In an aqueous environment, the
 Characteristics
interaction of hydrophilic and
 Presence of enormous catalytic power
hydrophobic side chains with water
 Speeds up chemical reactions by
determines shape
lowering activation energies and
allow reactions to achieve
equilibrium more rapidly

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 High specificity in reactions catalyzed  Substrate: urea

and the substances involved  Common name: urea + ase =
 Regulation of catalytic activity by the urease
cell  Alcohol dehydrogenase - Name is
 Reaction rate and the amount of derived from both the substrate name
formation of any product are and the type of reaction
controlled by regulating enzyme  Substrate: alcohol (ethyl alcohol)
action  Reaction type: dehydrogenation
(removal of hydrogen)
Enzyme Specificity  Common name: alcohol
 Absolute specificity: Enzyme acts only on dehydrogenation + ase = alcohol
one substance dehydrogenase
 Relative specificity: Enzyme acts on
structurally related substances Enzyme Cofactors
 Stereochemical specificity: Enzyme has  Nonprotein molecules or ions required by
the ability to distinguish between an enzyme for catalytic activity
stereoisomers  Can either be coenzymes or inorganic
ions
Classifying and Naming  Coenzyme: Organic cofactor that is
Enzymes often derived from vitamins
 Earliest enzymes were given names with  Apoenzyme: Catalytically inactive
an -in ending to indicate their protein protein formed by the removal of the
composition cofactor from an active enzyme
 Examples - Pepsin, trypsin, and  Apoenzyme + cofactor = active
chymotrypsin enzyme
 Enzyme Commission (EC) system  Inorganic ions are metal ions, such as
 Enzymes are grouped based on the Mg2+, Zn2+, and Fe2+
type of reaction catalyzed
 Enzyme name specifies the substrate Mechanism of Enzyme Action
(substance acted on), functional group  All enzymes have an active site
acted upon, and type of reaction  Active site: Location on the enzyme
catalyzed where a substrate is bound and
 Names end in -ase catalysis occurs
 Binding of the substrate may occur
The EC Classification of through hydrophobic attraction, hydrogen
Enzymes bonding, and/or ionic bonding
 Enzyme–substance (ES) complex is
formed when a substrate and enzyme
bond, resulting in conversion of
substrate (S) to product (P)
 Chemical transformation of the
substrate that occurs in the active site
is aided by enzyme functional groups
 After conversion, the product is
released from the active site and the
Common Names for Enzymes enzyme is ready to catalyze again
 Shorter than EC names
 Formed by adding -ase to the name of the Theories on Enzyme Mechanism
substrate or to a combination of the  Lock-and-key theory
substrate name and type of reaction  States that the substrate has a shape
 Examples that exactly fits the active site
 Urea amidohydrolase - Common name  Limitation
is urease

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 Implies that enzyme conformations  Automated and computerized

are fixed or rigid but research experiment that measures enzyme
proves otherwise activity
 Determined activity levels are
reported in terms of enzyme
international units (IU)
 Enzyme international units (IU):
Quantity of enzyme that
catalyzes the conversion of
1µmol of substrate per minute
under specified reaction
conditions

Factors affecting enzyme

activity – enzyme concentration
 Increase in enzyme concentration will
increase the concentration of ES in
compliance with the reaction rate theory
E+S ES INCREASED (E) GIVES MORE
(ES)
 Rate of reaction is directly proportional to
enzyme concentration
 Induced-fit theory
 Modification of the lock-and-key theory Factors affecting enzyme
 States that the conformation of the
active site changes to accommodate activity – Substrate
an incoming substrate concentration
 Active site has a shape that  Initial rate of an enzyme-catalyzed
becomes complimentary to the reaction is responsive to increases in
substrate only after the substrate is substrate concentration
bound  At a certain concentration, the rate
levels out and remains constant
 Maximum rate (Vmax) occurs because
the enzyme is saturated with the
substrate and cannot work faster
under imposed conditions

Factors affecting enzyme

Enzyme Activity activity – temperature
 Rate at which an enzyme catalyzes a  Rates of enzyme-catalyzed reactions
reaction increase with temperature
 Methods of describing enzyme activity  Optimum temperature: Temperature
 Turnover number: Number of (25°C to 40°C) at which enzyme activity
substrate molecules acted on by one is highest
enzyme molecule per minute  Reaction rate is lower above or below
 Enzyme assay this value

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 Beyond this temperature, enzymes are  Interfere with transpeptidase in

vulnerable to denaturation penicillin
 Transpeptidase - Enzyme that is
important in bacterial cell wall
construction

Irreversible Inhibitor - Cyanide

Ion
 Extremely toxic and acts rapidly
 Interferes with the operation of an iron-
containing enzyme called cytochrome
Factors affecting enzyme oxidase
activity – pH  Forms a stable complex and does not
 Enzymes are most effective in a narrow allow the enzyme to function properly
pH range and less active at pH values  Results in cessation of cellular
lower or higher than the optimum pH respiration and causes death in a
(usually around 7) matter of minutes
 Antidote must be administered quickly
 Sodium thiosulfate converts the cyanide
ion to a thiocyanate ion, which does not
bind to the iron of cytochrome oxidase

Irreversible Inhibitor - Heavy

Metal Toxicity
 Caused by the ability of heavy metals,
such as mercury and lead, to render the
protein part of enzymes ineffective
Enzyme inhibitors  Metals act by combining with the —SH
 Substances that decrease enzyme activity groups found on many enzymes
 Reasons to understand enzyme inhibition  Cause nonspecific protein denaturation
 Characteristic function of many  Mercury and lead poisoning can cause
poisons and medicines is to inhibit one permanent neurological damage
or more enzymes and decrease the  Treated by administering chelating
rate of catalytic reaction agents, which combine with metal ions
 Some substances found in cells inhibit and hold them very tightly
enzyme-catalyzed reactions and  Example -
provide a means for internal Ethylenediaminetetraacetic acid
regulation of cellular metabolism (EDTA)
 Classified into:  Chelates all heavy metals
 Irreversible inhibitors except mercury
 Reversible inhibitors  Calcium salt of EDTA is
administered intravenously
Irreversible Inhibitors  Calcium ions are displaced
 Covalently bond with a specific functional by heavy-metal ions that
group of the enzyme and render it bind to the chelate more
inactive tightly
 Include:  Lead–EDTA complex is soluble
 Poisons in body fluids and is excreted in
 Toxic metals the urine
 Antibiotics (penicillin and sulfa drugs)
 Inhibit enzymes essential to the life Reversible Inhibitors
processes of bacteria  Reversibly bind to an enzyme

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 Can be removed from the enzyme by Regulation of Enzyme Activity -

shifting the established equilibrium
Activation
E + I = EI
of Zymogens
 Types  Zymogens (proenzymes): Inactive
 Competitive inhibitors: Compete with precursors of enzymes
substrate for binding at the active site  Some enzymes that would degrade the
 Noncompetitive inhibitors: Bind to the internal structures of the cell are stored
enzyme at a location other than the as inactive zymogens
active site  Released when required
 Activated at the location where the
Competitive Inhibitors reaction occurs
 Have molecular structures that are similar  Involves the cleavage of one or
to the normal substrate of the enzyme more peptide bonds of the
 Example - Action of sulfa drugs on zymogen
bacteria
 Folic acid is essential for the growth of Regulation of Enzyme Activity -
certain disease-causing bacteria Allosteric
 Synthesized within the bacteria by
a process that requires p- Regulation
aminobenzoic acid  Refers to the control of an allosteric
 Sulfanilamide resembles p- enzyme
aminobenzoic acid and competes with  Allosteric enzyme: Enzyme with a
it for the active site of the bacterial quaternary structure whose activity is
enzyme changed by the binding of modulators
 Action can be reversed by:  Modulators: Bind to an enzyme’s
 Increasing substrate concentration active site and alter its catalytic
 Letting LeChâtelier’s principle operate activity
 May increase (activators) or
decrease (inhibitors) activity
 Feedback inhibition
 Process in which the end product of a
• E - Enzyme sequence of enzyme-catalyzed
• S - Substrate reactions inhibits an earlier step in the
process
• I - Competitive inhibitor
Regulation of Enzyme Activity -
Noncompetitive Inhibitors Genetic
 Bear no resemblance to the enzyme
substrate Control
 Interaction between the enzyme and the  Synthesis of all proteins, including
inhibitor causes the 3-D shape of the enzymes, is under genetic control by
enzyme and its active site to change nucleic acids
 Substrate is improperly bound to the  Example
active site  Enzyme induction: Synthesis of an
 Prevents catalytic groups of the enzyme in response to a cellular need
active site from participating in  Example - Synthesis of β-
reaction catalysis galactosidase
 Substrate concentration does not affect
inhibitor action

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 BIOCHEMISTRY REVIEWER – MIDTERM 2024

Enzymes in Clinical Diagnosis

 Changes in blood serum concentrations of
specific enzymes can be used to:
 Detect cell damage and uncontrolled
cell growth
 Suggest the site of damage or cancer
 Estimate extent of cell damage
 Determined by the magnitude of
increase in serum concentration
above normal level
 Measurement of enzyme concentrations
in blood serum has become a major
diagnostic tool in diagnosing diseases of
the heart, liver, pancreas, prostate, and
bones

Isoenzymes
 Slightly different forms of the same
enzyme produced by different tissues
 All forms catalyze the same reaction but
their molecular structures slightly differ
and their locations may vary
 Example - Lactate dehydrogenase (LDH),
whose serum levels are used in the
 diagnosis of:
 Anemias involving the rupture of red
blood cells
 Acute liver diseases
 Congestive heart failure
 Muscular diseases, such as muscular
dystrophy

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