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In Partial-Fulfillment of the Requirements for the Subject

CHE 544 – BIOCHEMICAL ENGINEERING

“ENZYME SPECIFICTY”

Proponent:

Cayasan, Judyll Roi

Submitted to:

Engr. Arjon Lingaya

JUNE 19, 2017


REVIEW:

WHAT IS AN ENZYME?
The word "Enzyme" is derived from the Greek, en (in) +zyme (ferment).

Enzymes are proteins that have catalytic functions indispensable to maintenance


and activity of life. All chemical reactions occurring in a living organism are dependent on
the catalytic actions of enzymes, and this is why enzymes are called Biotransformation.
At present, there are about 4,000 kinds of enzymes whose actions are well known.

Enzymes function in a mild environment similar to the body environment of a living


organism, and they support life by synthesizing and degrading materials that constitute
the building blocks of the organism and by creating energy. Enzymes function as highly
selective catalysis in such a way that they selectivity catalyze specific reactions (reaction
specificity) and specific materials (substrate specificity).

WHAT IS A SUBSTRATE?

In biochemistry, the substrate is a molecule upon which an enzyme acts. Enzymes


catalyze chemical reactions involving the substrate(s). In the case of a single substrate,
the substrate bonds with the enzyme active site, and an enzyme-substrate complex is
formed.

WHAT IS THE ACTIVE SITE

Active site is the region of an enzyme where substrate molecules bind and undergo
a chemical reaction. The active site consists of residues that form temporary bonds with
the substrate (binding site) and residues that catalyse a reaction of that substrate
(catalytic site). The active site is usually a groove or pocket of the enzyme which can be
located in a deep tunnel within the enzyme, or between the interfaces of multimeric
enzymes. An active site can catalyse a reaction repeatedly as its residues are not altered
at the end of the reaction (they may change during the reaction, but are regenerated by
the end).
ENZYME SPECIFICITY

Specificity is the ability of an enzyme to choose exact substrate from a group of


similar chemical molecules. The specificity is actually a molecular recognition mechanism
and it operates through the structural and conformational complementarity between
enzyme and substrate.

TYPES OF SPECIFICITY

Enzymes vary in the specificity of the substrates that they bind to, in order to carry
out specific physiological functions. Some enzymes may need to be less specific and
therefore may bind to numerous substrates to catalyze a reaction. On the other hand,
certain physiological functions require extreme specificity of the enzyme for a single
specific substrate in order for a proper reaction and physiological phenotype to occur. The
different types of categorizations differ based on their specificity for substrates. Most
generally, they are divided into four groups: absolute, group, linkage, and stereochemical
specificity.

ABSOLUTE SPECIFICITY

Absolute specificity can be thought of as being exclusive, in which an enzyme acts


upon one specific substrate. Absolute specific enzymes will only catalyze one reaction
with its specific substrate. For example, lactase is an enzyme specific for the degradation
of lactose into two sugar monosaccharides, glucose and galactose. Another example is
Glucokinase, which is an enzyme involved in the phosphorylation of glucose to glucose-
6-phosphate. It is primarily active in the liver and is the main isozyme of Hexokinase. Its
absolute specificity refers to glucose being the only hexose that is able to be its substrate,
as opposed to hexokinase, which accommodates many hexoses as its substrate.

GROUP SPECIFICITY

Group specificity occurs when an enzyme will only reacts with molecules that have
specific functional groups, such as aromatic structures, phosphate groups, and methyls.
One example is Pepsin, an enzyme that is crucial in digestion of foods ingested in our
diet that hydrolyzes peptide bonds in between hydrophobic amino acids, with recognition
for aromatic side chains such as phenylalanine, tryptophan, and tyrosine. Another
example is hexokinase, in enzyme involved in glycolysis that phosphorylate glucose to
produce glucose-6-phosphate. This enzyme exhibits group specificity by allowing multiple
hexoses (6 carbon sugars) as its substrate. Glucose is one of the most important
substrates in metabolic pathways involving hexokinase due to its role in glycolysis, but is
not the only substrate that hexokinase can catalyze a reaction with.

LINKAGE SPECIFICITY

Linkage specificity, unlike group specificity, recognizes particular chemical bond


types. This differs from group specificity, as it is not reliant on the presence of particular
functional groups in order to catalyze a particular reaction, but rather a certain bond type
(for example, a peptide bond).

STEREOCHEMICAL SPECIFICITY

This type of specificity is sensitive to the substrate’s optical activity of orientation.


Stereochemical molecules differ in the way in which they rotate plane polarized light, or
orientations of linkages (see alpha, beta glycosidic linkages). Enzymes that are
stereochemically specific will bind substrates with these particular properties. For
example, beta-glycosidase will only react with beta-glycosidic bonds which are present in
cellulose, but not present in starch and glycogen, which contain alpha-glycosidic linkages.
This is relevant in how mammals are able to digest food. For instance, the enzyme
Amylase is present in mammal saliva, that is stereo-specific for alpha-linkages, this is
why mammals are able to efficiently use starch and glycogen as forms of energy, but not
cellulose (because it is a beta-linkage).

THEORIES ON ENZYME SPECIFICITY

LOCK AND KEY THEORY

The specific action of an enzyme with a single substrate can be explained using a
Lock and Key analogy first postulated in 1894 by Emil Fischer. In this analogy, the lock is
the enzyme and the key is the substrate. Only the correctly sized key (substrate) fits into
the keyhole (active site) of the lock (enzyme).

Smaller keys, larger keys, or incorrectly positioned teeth on keys (incorrectly


shaped or sized substrate molecules) do not fit into the lock (enzyme). Only the correctly
shaped key opens a particular lock.
INDUCED FIT THEORY

Not all experimental evidence


can be adequately explained by
using the so-called rigid enzyme
model assumed by the lock and key
theory. For this reason, a
modification called the induced-fit
theory has been proposed.

The induced-fit theory


assumes that the substrate plays a
role in determining the final shape of
the enzyme and that the enzyme is
partially flexible. This explains why
certain compounds can bind to the
enzyme but do not react because the
enzyme has been distorted too
much. Other molecules may be too
small to induce the proper alignment
and therefore cannot react. Only the
proper substrate is capable of
inducing the proper alignment of the active site.
REFERENCES

http://osp.mans.edu.eg/medbiochem_mi/Cources/Biochemistry/1st_year_medicine/Enzy
mes/files/Lecture_02.pdf

http://www.easybiologyclass.com/enzyme-substrate-specificity-types-classification/

http://biology.tutorvista.com/biomolecules/enzymes.html

http://www.worthington-biochem.com/introbiochem/specificity.html

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