Group 2

MD 2Y1-2

INTRODUCTION

ENZYME
-organic compound that acts as a CATALYST for a
biochemical reaction
-help reaction to occur more rapidly
-undergo denaturation
-lowers activation energy for the formation of
product
SUBSTRATE
-reactant in an enzyme-catalyzed reaction

ENZYME ACTIVE SITE

Small portion that participates in the interaction

with substrates during a reaction
Three-dimensional entity
Usually a CREVICE-LIKE location in the enzyme

ENZYME-SUBSTRATE
COMPLEX

The intermediate reaction product that is formed

when a substrate binds to the active site of an
enzyme

LOCK-AND-KEY
MODEL

The active site in the enzyme has a fixed, rigid

geometrical conformation. Only substrates with a
complementary shape can be accomodated at the
active site.

INDUCED-FIT MODEL

Indicates that enzymes have flexibility in their

shape where it allows for small changes in the
shape of the active site to accommodate the
substrate.

ENZYME SPECIFICITY

1. Absolute Specificity
-Catalyze reactions for only ONE substrate.
2. Stereochemical Specificity
-Catalyze reactions of L-amino acid
STEREOISOMERS.
3. Group Specificity
-Catalyze reactions of structurally similar
compounds with the same FUNCTIONAL GROUPS.

ENZYME ACTIVITY

Rate at which an enzyme converts substrate to

products in a biochemical reaction
4 Factors affecting enzyme activity
- Temperature
- pH
- Substrate concentration
- Enzyme Concentration

4 FACTORS AFFECTING
ENZYME ACTIVITY

TEMPERATURE
-As the temperature of an enzymatically
catalyzed reaction increases, so does the rate of the
reaction

4 FACTORS AFFECTING
ENZYME ACTIVITY

pH
-Small changes in pH in the active site can
result to denaturation or loss of catalytic activity.
-Optimum pH: 7.0 - 7.5pH

4 FACTORS AFFECTING
ENZYME ACTIVITY

SUBSTRATE CONCENTRATION
-When substrate concentration increases, the
reaction rate increases up to a certain concentration
and then remains constant.

4 FACTORS AFFECTING
ENZYME ACTIVITY

ENZYME CONCENTRATION
-When enzyme concentration increases, the
reaction rate increases because more substrate can be
accommodated.
enzyme concentration =

reaction rate

MAJOR CLASSES

1. Oxidoreductase
2. Transferase
3. Hydrolase
4. Lyase
5. Isomerase
6. Ligase

OXIDOREDUCTASE

Is an enzyme that catalyzes an oxidation-reduction

reaction (REDOX REACTION).
Requires coenzyme. ( NAD & FAD)

OXIDOREDUCTASE

SUBCLASS

REACTION
CATALYZED

EXAMPLE

Oxidases

Oxidation of a
substrate

Glucose Oxidase,
Galactose
Oxidase

Reductases

Reduction of a
substrate

HMG-CoA
reductase

Dehydrogenases

Introduction of a
double bond by
removal of 2 H
atoms from
substrate and
accepted by a
coenzyme

Lactate DH,
Pyruvate DH

TRANSFERASE

Is an enzyme that catalyzes the transfer of a chemical

groups from one molecule to another, or within a
single molecule.
Transaminase requires cofactor (pyridoxal
phosphate or Vit. B6)

TRANSFERASE

SUBCLASS

REACTION
CATALYZED

EXAMPLE

Transaminases

Transfer of an amino
group between
substrates

Aspartate
Transaminase

Kinases

Transfer of a
phosphate group
between substrates

Hexokinase

HYDROLASE

is an enzyme that catalyzes the hydrolysis of

a chemical bond.
A + H2O B + C
Lys- Ala + H2O Lys + Ala
SERINE HYDROLASE
(Protease)

LYASE

- is an enzyme that catalyzes the breaking of

various chemical bonds by means other
than hydrolysis and oxidation, often forming a
new double bond or a new ring structure.
AB+C
Argininosuccinate Aginine + Succinate
ARGININOSUCCINATE LYASE

ISOMERASE

Isomerases are a general class of enzymes which

convert a molecule from one isomer to another.
Isomerases can either facilitate intramolecular
rearrangements in which bonds are broken and
formed or they can catalyze conformational changes.
The general form of such a reaction is as follows:
AB BA

NOMENCLATURE

Generally, "the names of isomerases are formed as

"substrate isomerase" (for example, enoyl CoA
isomerase), or as "substrate type of isomerase" (for
example, phosphoglucomutase)."

ISOMERASES

Involved in inter conversion of pair of isomeric compounds

Glucose 6 P.
Phosphogluco glucose 1 P.
Mutase
Glucose 6 P.
Phosphohexose
Fructose 6 P.
Isomerase
All trans retinene
Retinene
11- CIS retinene
Isomerase
UDP glucose
UDPG-4
UDP Galactose
Epimerase

LIGASES

catalyze the joining of two large molecules by

forming a new chemical bond, usually with
accompanying hydrolysis of a small chemical
group dependent to one of the larger molecules
or the enzyme catalyzing the linking together of
two compounds, e.g., enzymes that catalyze
joining of C-O, C-S, C-N, etc. In general, a ligase
catalyzes the following reaction:
Ab + C AC + b or sometimes
Ab + cD AD + b + c

NOMENCLATURE

The common names of ligase enzymes often include

the word "ligase", such as DNA ligase, an enzyme
commonly used in molecular biology laboratories to
join together DNA fragments. Other common names
for ligases include synthetases, because they are
used to synthesize new molecules.

CLASSIFICATION

Ligases are classified as EC 6 in the EC number

classification of enzymes. Ligases can be further classified
into six subclasses:
EC 6.1 includes ligases used to form carbon-oxygen bonds
EC 6.2 includes ligases used to form carbon-sulfur bonds
EC 6.3 includes ligases used to form carbon-nitrogen
bonds (including argininosuccinate synthetase)
EC 6.4 includes ligases used to form carbon-carbon bonds
EC 6.5 includes ligases used to form phosphoric ester
bonds
EC 6.6 includes ligases used to form nitrogen-metal bonds

LIGASES

Catalyze reactions in which linking

together of two molecules occur
coupled with the breakdown of a high
energy phosphate bonds like ATP,
GTP,NTP


Acetate + CoA +ATP
CoA+AMP+PP
Succinate + CoA + NTP
NDP+ Pi
Pyruvate + CO2 + ATP
ADP + Pi

Acetyl CoA
Synthetase

Succinyl CoA

Acetyl
Succinyl CoA +

Synthetase
Pyruvate

Oxaloacetate +

Carboxylase
(Activated fatty acid) + AMP + PP
Fatty Acyl CoA
+ CoA + ATP

Synthetase

Fatty acid