Enzymes I

Definition, structure
properties, nomenclature and
classification

Dr. Nesreen Alsanousi

Objectives
After reading this lesson, you will be able
to:
 Describe the role enzymes play in biological
systems.
 Define enzyme
 Explain co-enzymes
 classify enzymes
 Explain how enzyme structure determines
enzyme specificity.
Enzymes are biological catalysts that speed up
the rate of a chemical reaction by providing an
alternative pathway with a lower activation
energy.

The enzyme catalyses the reaction but remains

unchanged at the end.

Its presence does not alter the properties or

nature of the final product
 Chemical Nature of Enzymes

All known enzymes are proteins. They are high

molecular weight compounds made up
principally of chains of amino acids linked
together by peptide bonds.
 Enzyme structure

Substrate
Substrate binding site
(active site)
Apoenzyme
Catalytic Site or Active Site:
It is a small three-dimensional (3D) area on or near enzyme
surface that binds the specific substrate(s) and convert into
products

Allosteric Sites:
• These are special sites on enzyme surface other than catalytic
site, which when bind with effectors or modulators alter the
conformation of the catalytic site.
• The enzymes having allosteric sites are called allosteric
enzymes.
• Allosteric sites are of two types: activator site and inhibitor
site.
Apoenzyme + Cofactor = Holoenzyme
 Many enzymes require the presence of other
compounds - cofactors - before their catalytic activity
can be exerted.

 This entire active complex is referred to as the

holoenzyme; i.e., apoenzyme (protein portion) plus
the cofactor (coenzyme, prosthetic group or metal-
ion-activator) is called the holoenzyme.
The cofactor may be:
1. A coenzyme - a non-protein organic substance
which is dialyzable, thermostable and loosely
attached to the protein part.

2. A prosthetic group - an organic substance which

is dialyzable and thermostable which is firmly
attached to the protein or apoenzyme portion.

3. A metal-ion-activator - these include K+, Fe++,

Fe+++, Cu++, Zn++, Mn++, Mg++, Ca++,
 Specificity of Enzymes
One of the properties of enzymes that makes
them so important as diagnostic and research
tools is the specificity they exhibit relative to
the reactions they catalyze.

They are highly specific, which means that they

catalyse a single reaction with a specific
substrate.
 Naming and Classification
Except for some of the originally studied
enzymes such as pepsin, rennin, and trypsin,
most enzyme names end in "ase". The
International Union of Biochemistry (I.U.B.)
initiated standards of enzyme nomenclature
which recommend that enzyme names
indicate both the substrate acted upon and
the type of reaction catalyzed.
 Classification of enzymes

There are six (6) major classes of enzymes based

on their functions.
1. Oxidoreductases
catalyze a variety of oxidation-reduction reactions.
Common names include dehydrogenase, oxidase,
reductase and catalase.

2. Transferases
catalyze transfers of groups (acetyl, methyl, phosphate,
etc.). Common names include acetyltransferase,
methylase, protein kinase and polymerase.
3. Hydrolases
catalyze hydrolysis reactions where a molecule is
split into two or more smaller molecules by the
addition of water. Proteases splits protein
molecules, Nucleases splits nucleic acids.

4. Lyases
catalyze the cleavage of C-C, C-O, C-S and C-N bonds
by means other than hydrolysis or oxidation.
Common names include decarboxylase and
aldolase.
5. Isomerases
catalyze atomic rearrangements within a molecule.
Examples include rotamase, protein disulfide
isomerase (PDI), epimerase and racemase.

6. Ligases
catalyze the reaction which joins two molecules.
Examples include peptide synthase, aminoacyl-
tRNA synthetase, DNA ligase and RNA ligase.
Thank you