ENZYMES Co-Enzymes/Co-Substrates - Derived from dietary vitamins

TYPICAL METAL ION COFACTORS:

GENERAL CHARACTERISTICS OF ENZYMES
 Zn2+ (Zinc Ion)
Enzymes – Are catalysts and are not consumed in reactions
 Mg2+ (Magnesium Ion)
 Proteins that act as a catalyst for Biochemical
Reactions
 Mn2+ (Manganese Ion)
 Most effective catalysts known
 Fe2+ (Ferrous Ion)
 Undergo all the reactions of proteins including
NON-METALLIC ION COFACTOR:
DENATURATION
 Cl- (Chloride)
 Most are GLOBULAR PROTEINS
Inorganic Ion Cofactors - Derived from dietary minerals
 Few of them are now known to be RIBONUCLEIC
ACIDS (RNA) NOMENCLATURE AND CLASSIFICATION OF
ENZYMES
 The human body has 1000s of this protein Nomenclature - Most commonly named with reference to
Enzyme Activity – Dramatically affected by: their function

 Alterations in PH  Type of reaction catalyzed

 Temperature  Identity of the substrate

Substrate – Reactant in an enzyme-catalyzed reaction

 Other protein denaturants
 Substance upon which the enzyme “acts.”
SIMPLE AND CONJUGATED ENZYMES
THREE IMPORTANT ASPECTS OF THE
TWO TYPES OF ENZYMES NAMING PROCESS
 Simple Enzymes 1. Suffix “-ase” identifies it as an enzyme

 Conjugated Enzymes EXAMPLES:

Simple Enzyme - Composed only of Protein (AMINO ACID  Urease

CHAINS)
 Sucrase
Conjugated Enzyme - Has a nonprotein part in addition to a
protein part  Lipase
Apoenzyme – Protein part of conjugated enzyme EXCEMPTION – The suffix “-in” is still found in some
Cofactor – Non-protein part of a conjugated enzyme digestive enzymes

Holoenzyme – Biochemically active conjugated enzyme EXAMPLES:

Apoenzyme + Cofactor = Holoenzyme (Conjugated Enzyme)  Trypsin

COFACTORS  Chymotrypsin
Cofactors - Are important for the chemically reactive
 Pepsin
enzymes

 Small inorganic molecules 2. Type of reaction catalyzed by an enzyme is often

used as a prefix
 Small inorganic ions
EXAMPLES:
Organic Molecule Cofactors – Also called as CO-
 Oxidase - Catalyzes an oxidation reaction
ENZYMES or CO-SUBSTRATES
  Hyrolase - Catalyzes a hydrolysis reaction  Transaminases - Catalyze transfer of an amino
group to a substrate
3. Identity of substrate is often used in addition to
the type of reaction  Kinases - Catalyze transfer of a phosphate group
from Adenosine Triphosphate (ATP) to a substrate
EXAMPLE:
HYDROLASE
 Glucose Oxidase
Hydrolase - Enzyme that catalyzes a hydrolysis reaction
 Pyruvate Carboxylase
 Involves addition of a water molecule to a bond to
 Succinate Dehydrogenase cause bond breakage

FUNCTION OF FOLLOWING ENZYMES  These type of reactions are central to the process of
digestion
Maltase – Hydrolysis of Maltose
Carbohydrases - Hydrolyze glycosidic bonds in oligo- and
Lactate Dehydrogenase - Removal of hydrogen from polysaccharides
lactate ion
Proteases - Effect the breaking of peptide linkages in
Fructose Oxidase - Oxidation of fructose Proteins
Maleate Isomerase - Rearrangement (Isomerization) of Lipases - Effect the breaking of ester linkages in
maleate ion Triacylglycerols
SIX MAJOR CLASSES LYASE
** Enzymes are grouped into SIX MAJOR CLASSES Lyase - Enzyme that catalyzes the addition of a group to a
based on the types of reactions they catalyse ** double bond

 Or the removal of a group to form a double bond in a

manner that does not involve hydrolysis or oxidation

Dehydratase - Effects the removal of the components of

water from a double bond

Hydratase - Effects the addition of the components of water

to double bonds

ISOMERASE AND LIGASE

Isomerase - Enzyme that catalyzes the isomerization
(rearrangement of atoms) reactions

Ligase - Enzyme that catalyzes the formation of a bond

OXIDOREDUCTASE
Oxidoreductase - Catalyzes an oxidation–reduction reaction
 Oxidation and reduction reactions are always linked
to one another
 Requires a coenzyme that is either oxidized or
reduced as the substrate in the reaction
between two molecules involving ATP hydrolysis
ATP Hydrolysis - Required because such reactions are
energetically unfavorable
 Require the simultaneous input of energy obtained by
a Hydrolysis of ATP to ADP

EXAMPLE:

 Lactate Dehydrogenase

TRANSFERASE
Transferase - An enzyme that catalyzes the transfer of a
functional group from one molecule to another

TWO MAJOR SUBSTYPES OF TRANSFERASE:


A. TRANSFERASE
B. LYASE
ENZYME ACTIVE SITE
Enzyme Active Site - Relatively small part of an enzyme’s
structure that is actually involved in catalysis
 Place where substrate binds to enzyme
 Formed due to folding and bending of the protein
 Usually a “crevice like” location in the enzyme
 Some enzymes have more than one active site
ENZYME SUBSTRATE COMPLEX
Enzyme Substrate Complex - Needed for the activity of
enzyme
 Intermediate reaction species formed when substrate
binds with the active site
 Orientation and proximity is favorable and reaction is
fast
TWO MODELS FOR SUBSTRATE BINDING TO
ENZYME
Lock and Key Model - Enzyme has a pre-determined shape
for the active site
 Only substrate of specific shape can bind with active
site
Induced Fit Model - Substrate contact with enzyme will
change the shape of the active site
 Allows small change in space to accommodate
substrate (e.g., how a hand fits into a glove)
FORCES THAT DETERMINE SUBSTRATE
BINDING
 H-Bonding
 Hydrophobic Interactions
 Electrostatic Interactions
ENZYME SPECIFICITY
Absolute Specificity - An enzyme will catalyze a particular
reaction for only one substrate
 This is most restrictive of all specificities (not
common)
 Urease – Is an enzyme with absolute specificity
Stereochemical Specificity - An enzyme can distinguish
between stereoisomers
 Chirality is inherent in an active site (amino acids are
chiral compounds)
 L-Amino-acid Oxidase - Catalyzes reactions of L-
amino acids but not of D-amino acids
Group Specificity - Involves structurally similar
compounds that have the same functional groups
EXAMPLE:
Carboxypeptidase - Cleaves amino acids one at a time
from the carboxyl end of the peptide chain
Linkage Specificity - Involves a particular type of bond
irrespective of the structural features in the vicinity of the
bond
 Considered most general of enzyme specificities
EXAMPLE:
Phosphatases - Hydrolyze phosphate–ester bonds in all
types of phosphate esters
TEMPERATURE
  Optimum pH - pH at which enzyme has maximum
activity

 Most enzymes have optimal activity in the pH range

of 7.0 - 7.5

 Exception - Digestive enzymes

 Pepsin - Optimum pH = 2.0

 Trypsin - Optimum pH = 8.0

SUBSTRATE CONCENTRATION

 Higher temperature results in higher kinetic

energy which causes an increase in number of
reactant collisions, therefore there is higher activity

 Optimum Temperature - Temperature at which the

rate of enzyme catalyzed reaction is maximum
 Optimum temperature for human enzymes is 37ºC
(body temperature)

 Increased temperature (high fever) leads to decreased

enzyme activity Substrate Concentration - At a constant enzyme
concentration, the enzyme activity increases with increased
pH substrate concentration

Substrate Saturation - The concentration at which it reaches

its maximum rate and all of the active sites are full

Turnover Number - Number of substrate molecules

converted to product per second per enzyme molecule under
conditions of optimum Temperature and pH

ENZYME CONCENTRATION

 pH changes affect enzyme activity

 Drastic changes in pH can result in denaturation of

proteins
 Non-Competitive Inhibitors - Do not compete with the
substrate for the same active site

 Binds to the enzyme at a location other than active

site

Enzyme Concentration - Enzymes are not consumed in the

reactions they catalyse

 At a constant substrate concentration, enzyme

activity increases with increase in enzyme
concentration

 The greater the enzyme concentration, the greater the

reaction rate

ANSWERS:

A. Decrease Rate

B. Increase Rate

C. Decrease Rate

D. Decrease Rate

ENZYME INHIBITION
Enzyme Inhibitor – A substance that slows down or stops the
normal catalytic function of an enzyme by binding to it

Competitive Inhibitors - Compete with the substrate for the

same active site

 Will have similar charge & shape