Difference Between Cofactor And Coenzyme

The fundamental difference between cofactor and coenzyme is based on chemical composition and function. The primary difference between coenzyme and cofactor is that coenzyme is a form of cofactor that binds to the enzyme loosely whereas cofactor sometimes binds tightly to the enzyme. Enzymes are proteins that are essential to regulate metabolic reactions as well as chemical reactions in the body. numerous molecules are involved in catalyzing and regulating biochemical reactions within living organisms. Among these essential molecules are co-factors and co-enzymes, which play pivotal roles in facilitating enzymatic activity and ensuring the smooth functioning of metabolic pathways. In this article, we explore the significance of co-factors and co-enzymes, their classifications, and their essential contributions to the world of biochemistry.

Difference Between Coenzyme and Cofactor:

Feature	Coenzyme	Cofactor
Other Names	Coenzyme is additionally referred to as a Co-substrate and secondary substrate.	A cofactor is additionally referred to as a helper molecule or an accessory molecule.
Chemical Nature	Coenzymes are the organic molecule	Both organic and inorganic substances could serve as cofactors.
Types	Coenzyme is a type of cofactor	Both coenzyme and prosthetic groups are two types of cofactors.
Binding	They are loosely bound with an enzyme	They are tightly bound with an enzyme
Role	Coenzymes act as carriers and molecule substrates to the enzymes.	Cofactors increase the rate of the reaction that is catalyzed by the relevant enzyme
Separation	Coenzyme substrate easily separate because they are loosely bound to an enzyme	Cofactor molecules are tightly bound with the enzyme and are not possible to remove without denaturation
Example	NAD, NADP, etc.	Metal ions like Zinc, Copper, Cobalt, Molybdenum, etc.

What Are Enzymes?

“Enzymes can be defined as biological polymers that catalyze biochemical processes.” Most enzymes are proteins with catalytic abilities necessary for the performance of various processes. Metabolic processes and other chemical reactions in the cell are carried out by a number of vital enzymes. The first step in a metabolic reaction depends on the enzymes that react with the molecule and is called the substrate. Enzymes convert substrates into other unique molecules called products.

What is a Coenzyme?

Coenzymes are organic molecules that are capable of freely circulating and act as cofactors with enzymes by supporting the function of the enzyme. Hence, the coenzyme is a small, organic, non-protein molecule present in the cell. Coenzymes function as intermediate carriers of electrons, particular atoms, or functional groups that must be transported throughout the catalyzing process. For Instance, Electrons participate in NAD-coupled oxidation-reduction reactions.

Coenzymes change throughout the process, and a different enzyme is needed to return them to their original form. Since coenzymes are chemically modified throughout the reaction, It is referred to as co-substrate or secondary substrate which is a group of small, inactive, low molecular weight (<1000 Da) non-proteinaceous organic molecules. They are directly involved in the catalytic process of the enzyme.
An organic subtype of cofactor molecule, known as a coenzyme, helps bind the substrate molecule to the active site of the enzyme. Coenzymes bind insufficiently to inactive proteins or apoenzymes, so they can be easily separated by dialysis. It plays a key role in the functioning of the inactive enzyme.
Prosthetic groups are complex organic groups that bind covalently to a protein. They may be difficult to separate from the enzyme, or they can only be separated by denaturing the enzyme. For example, heme is a prosthetic group made up of an iron atom in a hemoglobin molecule.

What is a Cofactor?

A cofactor is a non-protein chemical substance that binds firmly to the enzyme, and helps in the function of an enzyme. It is associated with an inactive form of an enzyme referred to as apoenzyme, making the enzyme active. Hence, cofactors are known as helper molecules. The active form of the enzymes is referred to as holoenzyme. An enzyme consists of an active site where the particular substrate binds tightly. On the other hand, the allosteric site is the location where the allosteric activators and inhibitors can bind specifically to either accelerate or inhibit the enzymatic activity. Cofactors can be inorganic (such as metal ions) and organic (such as coenzymes and prosthetic groups).

Inorganic components such as metal, which tightly bind with the enzyme and are not possible to remove without denaturation, are referred to as prosthetic groups. Iron and copper are examples of metals used in prosthetic cofactors. Some enzymes function only when a covalently bound metal ion is available in their active site. Coenzymes are organic cofactors that are loosely attached to the enzyme.

Cofactors are divided into two categories according to their chemical nature and relationship with an enzyme.

• A large group of metal ions such as (Mg ²⁺, Cu ⁺, Mn ²⁺) is inorganic cofactors that serve as essential trace components in the human diet. Enzymes that trigger in conjunction with metal ions are known as metal-activated enzymes or metalloenzymes.
• In certain cases, the binding of specific inorganic elements is required for the allosteric regulation of an enzyme. Here, inorganic components are usually effector molecules than cofactors which are considered cofactors. For Example, calcium is involved in the allosteric control of nitric oxide synthase, adenylate kinase, and so on.

Similarities Between both of them

• Cofactors and coenzymes are compounds that support an enzyme’s or protein’s proper functioning.
• Similar to coenzymes, cofactors control, regulate, and modify how rapidly these chemical reactions proceed and have an impact on our bodies.

FAQs on the Difference Between Cofactor And Coenzyme

Q1: Which Enzyme Class Does Not Use Cofactors?

Answer:

An apoenzyme is an inactive enzyme that lacks a cofactor, whereas a holoenzyme is an active enzyme that contains a cofactor.

Q2: What Precisely is Dialysability?

Answer:

Dialysability is a property of ions or molecules that allows them to pass through a semipermeable membrane or be separated by dialysis.

Q3: What are Enzyme Cofactors Comprised of?

Answer:

The proper action of other enzymes is dependent on a cofactor, which is a non-protein molecule. Cofactors are classified into two types: organic molecules known as coenzymes and inorganic ions such as zinc or copper ions. Most coenzymes are either derived from or are vitamins.