‫ﺑﺴﻢ ﷲ اﻟﺮﺣﻤﻦ اﻟﺮﺣﯿﻢ‬

Structure of Enzyme

Bioc. 231

1
 Structure of Enzyme
• Enzymes are proteins, and their function is
determined by their complex structure.
• The reaction takes place in a small part of
the enzyme called the active site, while the
rest of the protein acts as "scaffolding".
• This is shown in this diagram of a molecule
of the enzyme trypsin, with a short length
of protein being digested in its active site.
The amino acids around the active site
attach to the substrate molecule and hold
it in position while the reaction takes place.
This makes the enzyme specific for one
reaction only, as other molecules will not
fit into the active site – their shape is
wrong.
 Active Site
• Enzyme molecules contain a
special pocket or cleft called the
active site.
• The active site contains amino
acids side chains that create a
three-dimensional surface
complementary to the
substrate.
• The active site binds the
substrate, forming an enzyme-
substrate (ES) complex. ES is
converted to enzyme-product
(EP), which subsequently
dissociated to enzyme and
product.
 Structure of Enzymes
• Enzymes catalyze many specific physiological
reactions. These reactions are faciliated by the
enzyme structure and several other factors.
• As a protein, each enzyme contains a specific
amino acid sequence (Primary Structure), with
the resultant polypeptide chains twisting
(Secondary Structure), which then folds (Tertiary
Structure), and results in structural cavities.
• If an enzyme contains more than one polypeptide
unit, the Quaternary Structure refers to the
spatial relationships between the subunits.
 Structure of Protein
§ Primary structure:
• Represents the number
and types of amino
acids in the specific
amino acid sequence.
• In order to function
properly, proteins must
have the correct
sequence of amino
acids.
 Structure of Protein
§ Secondary structure:
• Is regularly representing
structures stabilized by
hydrogen bonds between the
amino acids within the protein.
• Common secondary structures
are the α helix, β pleated sheet,
and turns with the most serum
proteins forming a helix.
• Secondary structures add new
properties to a protein such as
strenghth and flexibility.
 Structure of Protein
§ Tertiary structure:
• Refers to the overall shape, or
conformation, of the protein molecule.
• The conformation is known as the fold, or
the spatial releationship of the secondary
structures to one another.
• Tertiary structures are three-dimensional.
• Tertiary structures results from the
interaction of side chains and is stabilized
through the hydrophobic effect, ionic
attraction, hydrogen bonds, and disulfide
bonds.
• The function, physical, and chemical
properties of a protein depends only on its
tertiary structure.
 Structure of Protein
§ Quaternary structure:
• Is defined as the shape or
structure that results from the
interaction of more than one
protein molecule, or protein
subunits, held together by
noncovalent forces as hydrogen
bonds and electroctatic
interactions, which are part of
the larger protein complex with
a precise three-dimensional
configuration.
Structure of Protein
 Structure of Enzymes -
Cofactors
§ In addition to the basic structure, some enzymes associated
with a non-protein molecule, called a cofactor, may be
necessary for enzyme activity.
§ Commonly encountered cofactors include:
• Inorganic cofactors (metal ions), such as Fe2+, Mg2+, Zn2+,
Cu2+, are called activators.
• Organic cofactors, such as haem, biotin, FAD,
NAD or coenzyme A, are called coenzymes.
Many of these are derived from dietary
vitamins, which is why they are so important.
 Structure of Enzymes -
Cofactors
• The complete active enzyme with its cofactor is called a
holoenzyme, while just the protein part without its cofactor
is called the apoenzyme. In the absence of the appropriate
cofactor, the apoenzyme typically does not show biological
activity.
• A prosthetic group is a tightly bound coenzyme that does
not dissociate from the enzyme.
 Enzyme

Simple Protein Conjugated Protein

(active) (Holoenzyme)

Protein part
Non-protein part
(Apoenzyme)
(Cofactor)
(inactive)

Inorganic complexes Organic complexes

(Activators) (Coenzymes)

loosely bound tightly bound Cosubstrates Prosthetic group

(loosely bound) (tightly bound)