ENZYMES AND VITAMINS

WHAT ARE ENZYMES?

 Catalyst for biochemical reactions
 Mainly proteins a. Oxidoreductase
 Enzyme activity is affected by alteration in:  Catalyzed an oxidation-reduction reaction
 pH  The transfer of electrons from one
 temperature molecule (the oxidant) to another
ENZYMES: GENERAL STRUCTURE molecule (the reductant)
Simple enzymes  A– + B → A + B–
 composed only of protein (amino acid chains)  Example: Lactate dehydrogenase
Conjugated enzymes (oxidoreductase) NAD+ (coenzyme)
 composed of proteins and non-proteins parts
 apoenzyme- protein part (inactive
alone)
 cofactor/coenzyme- nonprotein part

b. Transferase
 Catalyzes the transfer of a function grup from
one molecular to another
 Transaminase – catalyzes the transfer
of an amino group from one molecule
to another (Ex: Serum Glutamic
Pyruvic Transaminase)
 apoenzyme + cofactor =
Holoenzyme (biochemically active)

 Kinase- catalyzes the transfer of a

phosphate group from adenosine
triphosphate (ATP) to produce
adenosine diphosphate (ADP) and
ENZYMES: NOMELNCLATURE AND CLASSOFICATION phosphorylated product.
 Named with reference to their function
 Focal points
 Type of reaction catalyzed
 Substrate identity
Substrate
 Substance upon which the enzyme acts
 Example: in the fermentation process, sugar is c. Hydrolase
converted to alcohol  Catalyzes a hydrolysis reaction
 In this reaction, sugar is the substrate  Reaction involved the addition of a water
Important aspect of the naming process molecule to a bond, which causes the bond to
1. Suffix – ase identifies a substance as an break
enzyme  Carbohydrase –hydrolyzes glycosidic
 Example: sucrose, nuclease, lipase bond in oligo and polysaccharides
 Exception: trypsin and pepsin  Protease – effects the breaking of
2. Type of reaction catalyzed by an enzyme often peptide linkages in proteins
used as a prefix  Lipase- effects the breaking of ester
 Oxidase: oxidation reaction lingkages in triacylglycerols
 Hydrolase: hydrolysis reaction
3. Identity substrate is often used in addition to
the type of reaction
 Example: glucose oxidase, pyruvate
carboxylase

Classes of enzymes
- grouped based on the types of reaction they catalyze

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 d. Isomerase
 Catalyzes the isomerization of a substrate
Stereochemical specificity
e. Ligase
 Catalyzes the formation of a bond between
two molecules with the participation of ATP
Linkage specificity
 Will act on a particular type of chemical bond,
rest of the molecular structure is not
considered
 Example: Phosphatases → phosphate–ester
bonds
 Enzyme will act on a particular stereoisomer
 Chirality is inherent in an active site
 Example: ʟ-amino-acid oxidase → ʟ-form of an
amino acid

FACTORS AFFECTING ENZYME ACTIVITY

Enzyme Activity
 Measure of the rate at which an enzyme
MODEL OF ENZYME ACTION converts substrate to products in a
Enzyme Active Site biochemical reaction
 Small part of an enzyme’s structure that is A. Temperature
involved in catalysis  Higher temperature results in
 Formed due to folding and bending of higher kinetic energy
the protein  Causes molecules to move
 Usually crevice like location in the faster and collide frequently
enzyme
 Increases the rate of reaction
Enzyme- substrate Complex
 Optimum temperature
 Formed when substrate binds to the active
 Temperature
site of an enzyme
which enzyme
 Results in faster formation of the product exhibits
Lock- and- Key Model maximum
 Enzyme has a fixed, rigid geometrical activity.
conformation B. pH
 Only substrates with a complementary  small changes in pH can result
geometry can be accommodated at the site in denaturation of proteins
 Optimum pH
 pH at which an
enzyme
exhibits
maximum
Induced Fit Model activity
 Active site allows for small changes in space  range: 7.0 to
to accommodate the substrate 7.5
 exception:
pepsin (2.0)
and typsin
(8.0)

Forces that Assist Substrate Binding C. Substrate concentration

 Electrostatic interactions  At a constant enzyme concentration,
 Hydrogen bonds the enzyme activity increases with
 Hydrophobic interactions increased substrate concentration
Enzyme Specificity D. Enzyme concentration
Absolute Specificity  At a constant substrate
 Enzyme will catalyze only one reaction concentration, enzyme activity
 Example: Catalase → hydrogen peroxide increases with the increase in
(H2O2) enzyme concentration
Group specificity
ENZYME INHIBITION
 Will act only on molecules that have specific
Enzyme Inhibitor
functional group
 Substance that slows down or stops the
 Example: Carboxypeptidase → cleaves amino
normal catalytic function of an enzyme by
acids (one at a time, from the carboxyl end of
binding it
the peptide chain)

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  Competitive inhibitor: molecule that
resembles an enzyme substrate in shape and  Vitamin B6 (pyridoxine, pyridoxal,
charge distribution pyridoxamine)
o Competes with the substrate for the  Vitamin B7 (biotin)
same active site  Vitamin B (folate, folic acid)
 Noncompetitive inhibitor: does not compete  Vitamin B12 (cobalamin)
with the substrate for the same active site
o Binds to the enzyme at a location FAT- SOLUBLE VITAMINS
other than active site.  Involved in processes that occur in
Reversible Competitive Inhibitor membranes
 Competitive enzyme inhibitor decreases  Structure are more hydrocarbon-like (fewer
enzyme activity by binding to the active site functional groups)
 Enzyme-inhibitor complex formation via weak Vitamin A
interactions (hydrogen bonds, etc.)  3 forms of vitamin A are active in the body
(retinoids)
 Retinold
 Retinal
 Retinoic Acid
 Derived from β-carotene
Reversible Noncompetitive Inhibitor
 Decreases enzyme activity by binding to a site
on the enzyme other than the active site.
 Causes a change in the structure of the
enzyme
ENZYMES: MEDICAL USES
 Produced in certain organs/tissue, if found in Vitamin D
blood, may indicate organ. Tissue damage  Active forms in the body (Vitamin D2 and D3)
 Blood clots in the heart can be dissolved by  Known as calciferol
using tissue plasminogen activator (TPA)  Vitamin D3 is synthesized by the exposure of
 Enzyme urease converts urea into ammonia in the skin to sunlight (ultraviolet radiation)
the blood, which is detected in the blood urea  Maintains normal blood levels of calcium ion
nitrogen (BUN) test and phosphate ion in order for bones to
absorb the ions
VITAMINS: GENERAL CHARACTERISTICS Vitamin E
 Organic compound essential for the proper  Four forms
functioning of the body (obtained from dietary  Alpha- tocopherol (most active biogical
sources) form of vitamin E)
 Conjugated enzymes contain vitamins as part  Beta- tocopherol
of their structure  Delta- tocopherol
 Required in micro and milligram  Gamma- tocopherol
 There are 13 known vitamins  Sources of vitamin E: vegetable oils, dark
 Classes of vitamins: green vegetables, nuts, and seeds
 Water- soluble  Immune system, flushes toxins
 Fat- soluble  Primary function: Antioxidant
Vitamin K
WATER- SOLUBLE VITAMINS  Has two major forms
Vitamin C  K1: found in leafy green vegetables
 Humans, primates, fruit bats, and guinea pigs  K2: synthesized by intestinal bacteria
need dietary vitamins  Dietary need supply
 In humans, 100 mg/day saturates all  Half of the human body’s vitamin K is
body tissues synthesized by intestinal bacteria and
 General antioxidant half comes from the diet
 Participates in formation of collagen  Essential for the formation of proteins which
The B Vitamins are involved in the regulation of blood clotting
 Serve as precursors for enzyme cofactors  Bone health
 Vitamin B1 (thiamin)
 Vitamin B2 (riboflavin) NUCLEIC ACIDS
 Vitamin B3 (niacin, nicotinic acid,  An unbranched polymer containing monomer
nicotinamid) units called nucleotides
 Vitamin B5 (pantothenic acid)
 Found in cell nuclei and acidic

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NUCLEOTIDE
 A three- subunit molecule in which a pentose
sugar is bonded to both a phosphate group
and a nitrogen- containing heterocyclic base
Pentose Sugars
 Two strand are connected by hydrogen bonds
between their bases
 Two strand are anti- parallel (run in opposite
direction)

Nitrogen- containing heterocyclic bases

DNA
 The amount of adenine
Phosphate and thymine is always
equal as well as the
amount of cytosine and
guanine
 Two strand of DNA are
not identical but
complementary

PRIMARY NUCLEIC ACID STRUCTURE

 Nucleic acids are polymers in which repeating
units, the monomers, are nucleotides
 Nucleotides are linked to each other through
sugar phosphate bonds
 Two types: RNA and DNA
BASE PAIRING
 Pairs involving one small base (a pyrimidine)
and one large base (purine)
 Always written in the direction from the 5’ end
to the 3’ end of the segment

RNA
 RNA is single stranded

THE DNA DOUBLE HELIX

 Has two a double-helix structure that accounts
for the equality of the bases present.

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 BASE PAIRING
Base Pairing for RNA

Types of RNA
 Heterogeneous nuclear RNA (hnRNA)
 Messenger RNA (mRNA)
 Small nuclear (snRNA)
 Ribosomal RNA (rRNA)
 Transfer RNA (tRNA) TRANSLATION: PROTEIN SYNTHESIS
 Process by which mRNA codons are
DNA REPLICATION deciphered and a particular protein molecule
 Process by which DNA molecules produce is synthesized
exact duplicates of themselves
 Key concept is the base pairing associated
with DNA double helix.

TRANSCRIPTION: RNA SYNTHESIS

 Process by which DNA directs the synthesis of
mRNA molecules that carry the coded
information needed for protein synthesis

THE GENETIC CODE

Codon
 Is a three- nucleotide sequence in an mRNA
molecule that codes for specific amino acid
Genetic Code
 Is the assignment of the 65 mRNA codons to
specific amino acid (stop signals)

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