BIOCHEMISTRY

BACHELOR OF SCIENCE IN NURSING

YEAR 1

LESSON 7: ENZYMES AND VITAMINS

OUTLINEOUTLINE
TOPIC OUTLINE ● Classes of Enzymes
I. General characteristics and structure of enzymes o Enzymes are grouped based on the types of reactions they
II. Nomenclature and classification of enzymes catalyze
III. Enzyme activity
IV. Enzyme inhibition 1. OXIDOREDUCTASE
V. Medical uses of enzymes o Catalyzes an oxidation-reduction reaction (transfer of
VI. General characteristics of vitamins electrons from one molecule to another molecule)
VII. Water-soluble vitamins  The transfer of electron from one molecule (the
VIII. Fat soluble vitamins oxidant) to another molecule (the reductant)
 A- + B → A + B-

I. GENERAL CHARACTERISTICS OF ENZYME

● ENZYMES
o Catalysts for biochemical reactions
o mainly proteins
o enzyme activity is affected by alterations in:
 pH
 temperature 2. TRANSFERASE
o Catalyzes the transfer of a functional group from one
ENZYMES: GENERAL STRUCTURE molecule to another
 Transaminase
● Simple enzymes  Kinase
o composed only of protein (amino acid chains) (inactive) o Transaminase
● Conjugated Enzymes ▪ catalyzes the transfer of an amino group from
o composed of protein and non-protein parts one molecule to another
 Apoenzyme - protein part (inactive alone)  Example: Serum Glutamic Pyruvic
 Coenzyme/cofactor - non-protein part Transaminase
 Apoenzyme + Cofactor = Holoenzyme  SGPT; enzyme that occurs naturally in
(biochemically active) liver because they help convert food into
\ energy

o Kinase
▪ transfer of a phosphate group from adenosine
triphosphate (ATP) to produce adenosine
II. ENZYMES: NOMENCLATURE AND CLASSIFICATION diphosphate (ADP) and a phosphorylated
● Enzymes are named with reference to their function product
● Focal points ▪ Example:
 Type of reaction catalyzed
 Substrate identity
● SUBSTRATE
o substance upon which the enzymes act
o Example: in the fermentation process, sugar is converted to
alcohol
o In this reaction, sugar is the substrate o Hydrolase
▪ catalyzes a hydrolysis reaction
Important aspects of the naming process
1. Suffix -ase indentifies a substance as an enzyme ▪ reaction involves the addition of a water
 Example: sucrase, nuclease, lipase molecule to a bond, which causes the bond to
 Exception: trypsin and pepsin (digestive enzyme) break
2. Type of reaction catalyzed by an enzyme often used as a  Carbohydrates hydrolyzes glycosidic
prefix bonds in oligo- and polysaccharides
 Oxidase: oxidation reaction  Protease effects the breaking of
 Hydrolase: hydrolysis reaction peptide linkages in proteins
3. Identity of substrate is often used in addition to the type of  Lipase effects the breaking of ester
reaction linkages in triacylglycerols
 Example: Glucose oxidase, Pyruvate
carboxylase

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Prepared by: Ino
 Example:
● Enzyme-Substrate Complex
o formed when substrate binds to the active site of an
enzyme
o results in faster formation of the product

o Lyase
▪ catalyzes the breaking of a chemical bond
between two parts of a molecule through
biochemical means other than hydrolysis and
oxidation
▪ DEDHYDRATASE effects the removal of the
components of water from a double bond ● Lock-and-Key Model
o enzyme has a fixed, rigid geometrical conformation
▪ HYDRATASE effects the addition of the o only substrate with a complementary geometry can be
components of water to a double bond accommodated at the site

o Isomerase
▪ isomerase: catalyzes the isomerization (re-
arrangement of atom) of a substrate
▪ same chemical formula but different in structure ● Induced Fit Model
o active site allows for small changes in space to
accommodate the substrate

o Ligase
▪ catalyzes the formation of a bond between two
molecules with the participation of ATP
FORCES THAT ASSIST SUBSTRATE BINDING
● Electrostatic interactions
● Hydrogen bonds
● Hydrophobic interactions

ENZYME SPECIFICITY

1. ABSOLUTE SPECIFITY
o enzyme will catalyze only one reaction
o example: catalase → hydrogen peroxide (H2O2)

2. GROUP SPECIFITY
o enzyme will act only on molecules that have a specific
functional group
o example: Carboxypeptidase → cleaves amino acids (one
at a time, from the carboxyl end of the peptide chain)

3. LINKAGE SPECIFICITY
o enzyme will act on a particular type of chemical bond, rest
of the molecular structure is not considered
o example: Phosphatases → phosphate-ester bonds (DNA-
RNA)

4. STEREOCHEMICAL SPECIFICITY
o enzyme will act on a particular stereoisomer (LEFT OR
MODELS OF ENZYME ACTION RIGHT HANDED ISOMER
● Enzyme Active Site o chirality is inherent is an active site
o Small part of an enzyme’s structure that is involved in o example: L-amino acid oxidase → L-form (OXIDATION) of
catalysis an amino acid
 Formed due to folding and bending of the
protein
 Usually a crevicelike location in the enzyme

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 III. FACTORS AFFECTING ENZYME ACTIVITY REGULATION OF ENZYME ACTIVITY
● Enzyme Activity ● cells continually produce large amounts of enzyme and plentiful
o measure of the rate at which an enzyme converts substrate amounts of a product if the processes are not regulated
to products in a biochemical reaction ● general mechanisms involved in regulation:
▪ Temperature  Feedback control associated with allosteric enzymes
▪ pH  Proteolytic enzymes and symogens
 Covalent modification
▪ Subsrate concentration
▪ Enzyme concentration PROPERTIES OF ALLOSTERIC ENZYMES
● Have quaternary structure
1. Temperature
o Higher temperature results in ● Have at least two binding sites (substrate and regulator)
higher kinetic energy ● Active and regulatory binding sites are distinct from each other
o Causes molecules to move faster ● Binding of molecules at the regulatory site causes changes in the
and collide frequently overall structure of the enzyme
o Increases the rate of reaction
2. Optimum Temperature
o Temperature at which an
enzyme exhibits maximum
activity
3. pH
o Small changes in pH can result in
denaturation of proteins
4. Optimum pH
o pH at which an enzyme exhibits
maximum activity
o Range for most enzymes: 7.0 to
7.5
o Exceptions: pepsin (2.0) and
trypsin (8.0): (digestive)
5. Substrate Concentration ● FEEDBACK CONTROL
o at a constant enzyme o process in which activation or inhibition of the first reaction
concentration, the enzyme activity increases with increased in a reaction sequence is controlled by a product of the
substrate concentration reaction sequence
o If daghan ang substrate, paspas ang o Allosteric enzyme
rate of reaction
6. Enzyme Concentration
o At a constant substrate concentration.
Enzyme activity increases with the
increase in enzyme concentration.

IV. ENZYME INHIBITION

● Enzyme Inhibitor
o substance that slows down or stops the normal catalytic
function of an enzyme by binding to it
o 2 types:
▪ Competitive inhibitor: molecule that resembles
an enzyme substrate in shape and charge
distribution
 Competes with the substrate for the same
active site)
▪ Noncompetitive inhibitor: does not compete
with the substrate for the same active site
 Binds to the enzyme at a location other
than active site
● Reversible Competitive Inhibitor
o competitive enzyme inhibitor decreases enzyme activity by
binding to the active site
o enzyme - inhibitor complex formation is via weak
interactions (hydrogen bonds, etc.)
● Reversible Noncompetitive Inhibitor
o noncompetitive enzyme inhibitor decreases enzyme activity
by binding to a site on an enzyme othher than the active
site
▪ causes a change in the structure of the enzyme
● PROTEOLYTIC ENZYMES AND ZYMOGENS
o mechanism of regulation by production of proteolytic
enzymes in inactive forms
▪ Zymogen: turned on at the appropriate time and
place
▪ Proteolytic enzyme: catalyzes the breaking of
peptide bonds
● Example: pepsinogen → pepsin
● COVALENT MODIFICATION
o common covalent modification; addition and removal of
phosphate group
o Kinase → addition of the phosphate group
(phosphorylation): atp converting into adp
o Phosphatase → removal of the phosphate group
(dephosphorylation)
V. ENZYMES: MEDICAL USES
● Enzymes produced in certain organs/tissues, if found in blood, may
indicate organ/tissue damage (SGPT:LIVER)
● Blood clots in the heart can be dissolved by using tissue plasminogen
activator (TPA)
● Enzyme urease converts urea into ammonia in the blood, which is
detected in the blood urea nitrogen (BUN) test
VI. VITAMINS: GENERAL CHARACTERISTICS
● Organic compound essential for the proper functioning og the body
(obtained from dietary sources)
● Conjugated enzymes contain vitamins as part of their structures
● Required in micro and milligram quantities
● There are 13 known vitamins
● Classes of vitamins:
o Water soluble
o Fat soluble

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 VII. WATER SOLUBLE VITAMINS o essential for the formation of proteins which are involved in
the regulation of blood clotting.
● VITAMIN C
o humans, primates, fruit bats, and guinea pigs need dietary
vitamins
▪ in humans, 100mg/day saturates all body
tissues
o general antioxidant
o participates in the formation of collagen
● THE B VITAMINS
o serves as precursors for enzyme cofactors (inorganic non
protein parts of enzyme)
▪ Vitamin B1 (thiamin)
▪ Vitamin B2 (riboflavin)
▪ Vitamin B3 (niacin, nicotinic acid, nicotinamid)
▪ Vitamin B5 (pantothenic acid)
▪ Vitamin B6 (pyridoxine, pyridoxal, pyridoxamine)
▪ Vitamin B7 (biotin)
▪ Vitamin B (folate, folic acid)
▪ Vitamin B12 (cobalamin)

VIII. FAT-SOLUBLE VITAMINS

● Vitamins A,D,E,K
o involved in processes that occur in cell membranes
o structures are more hydrocarbon-like (nonpolar) (fewer
functional groups)
● Vitamin A
o three forms of vitamin A are active in the body (retinoids)
▪ Retinol → reproduction
▪ Retinal → vision
▪ Retinoic acid → growth
o derived from B-carotene (compound that gives vegetables
its color)

● Vitamin D
o active forms in the body (VITAMIN D2 AND D3)
o known as calciferol
o Vitamin D3 synthesized by the exposure of the skin to
sunlight (UV radiation)
o maintains normal blood levels of calcium ion and
phosphate ion in order for bones to absorb the ions
● Vitamin E
o four forms
▪ Alpha-tocopherol (most active biological form of
Vitamin E)
▪ Beta-tocopherol
▪ Delta-tocopherol
▪ Gamma -tocopherol
o sources of vitamin e: vegetable oils, dark green vegetable,
nuts and seeds
o primary functions: antioxidant
● Vitamin K
o has 2 major forms:
▪ K1: found in leafy green vegeables
▪ K2: synthesized by intestinal bacteria (50%)
o dietary need supply
▪ half of the human body’s vitamin K is
synthesized by intestinal bacteria and half
comes from the diet