Enzymes and Its Components

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WHAT ARE ENZYMES AND ITS COMPONENTS

What are enzymes?


In 1833, a French Chemist Anselme Payen (1795-1871), was first to
discover the vitak force that drove this reaction and named it "enzyme". Enzymes are
typically proteins, although some are made of RNA molecules known as ribozymes.
Components of Enzymes Enzymes are composed of two main components:
1. Apoenzyme: This is the protein portion of the enzyme. It provides the basic
structure and shape of the enzyme, which is crucial for its function.
2. Cofactor: This is the non-protein component that is essential for the enzyme's
activity. Cofactors can be either inorganic ions (e.g., metal ions like iron, magnesium,
or zinc) or organic molecules known as coenzymes.
Cofactor Types
There are three main types of cofactors:
Prosthetic groups: These are tightly bound to the enzyme and remain associated
with it throughout its lifespan. An example is flavin adenine dinucleotide (FAD).
Coenzymes: These bind to the enzyme only during catalysis, meaning they are
involved in the reaction but then detach. A common example is nicotinamide adenine
dinucleotide (NAD+).
Metal ions: Some enzymes require a specific metal ion at their active site for
catalysis. These ions form coordinate bonds with the enzyme. Zinc ions (Zn2+) are a
good example.
ENZYMES CLASSIFICATION

According to the International Union of Biochemists (I U B), enzymes


are divided into six functional classes and are classified based on the type of
reaction in which they are used to catalyze. The six kinds of enzymes are
hydrolases, oxidoreductases, lyases, transferases, ligases and isomerases.
Listed below is the classification of enzymes discussed in detail:
Types Biochemical Property

The enzyme Oxidoreductase catalyzes the oxidation reaction


Oxidoreductases where the electrons tend to travel from one form of a molecule to
the other.

The Transferases enzymes help in the transportation of the


Transferases
functional group among acceptors and donor molecules.

Hydrolases are hydrolytic enzymes, which catalyze the hydrolysis


Hydrolases
reaction by adding water to cleave the bond and hydrolyze it.

Adds water, carbon dioxide or ammonia across double bonds or


Lyases
eliminate these to create double bonds.

The Isomerases enzymes catalyze the structural shifts present in a


Isomerases
molecule, thus causing the change in the shape of the molecule.

The Ligases enzymes are known to charge the catalysis of a


Ligases
ligation process.

MECHANISM OF ENZYME REACTION


Any two molecules have to collide for the reaction to occur along with the right
orientation and a sufficient amount of energy. The energy between these molecules
needs to overcome the barrier in the reaction. This energy is called activation energy.
1.The SUBSTRATE is a molecule on which an enzyme functions in biochemistry.
Chemical processes involving the substrate(s) are catalysed by enzymes. The active
site transforms the substrate into one or more products, which are then released.

2.The ACTIVE SITE of an enzyme is the part of the enzyme where substrate
molecules bind, and a chemical reaction takes place. The active site is made up of
amino acid residues that establish temporary bonds with the substrate (binding site)
as well as residues that catalyse that substrate's reaction (catalytic site).
3.The mechanism of ENZYMATIC ACTION . An enzyme attracts substrates to its
active site, catalyzes the chemical reaction by which products are formed, and then
allows the products to dissociate (separate from the enzyme surface).

4. The combination formed by an enzyme and its substrates is called the ENZYME–
SUBSTRATE COMPLEX.

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