Collegedunia Team Content Curator
Content Curator
Difference between Cofactor and Coenzyme is based on their chemical nature and function. Cofactors form a large group of auxiliary molecules (organic or inorganic). Human body is made up of billions of cells, units, groups, enzymes and systems. Coenzymes and cofactors help in proper functioning of an enzyme or protein. Coenzymes are organic molecules that bind loosely to the active site of an enzyme whereas cofactors do not bind the enzyme.
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| Table of Content |
Key terms:- Coenzymes, chemical compound, protein, Cofactor, auxiliary molecules, Vitamins.
What is Cofactor?
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Cofactors are a chemical compound that is not a protein. It is attached to the protein, and is required for the biological activity of the protein. Another term for these is 'auxiliary molecules' because they help biochemical transformations. There are two types of cofactors:
- Coenzymes are cofactors that are only loosely bound to an enzyme.
- Prosthetic groups are cofactors that are tightly bound to an enzyme.
Additionally, an enzyme can be outside the cofactor, which is called apoenzyme. An enzyme is considered complete if it contains the cofactor and is called a holoenzyme. A coenzyme, on the other hand, is a small, organic, non-protein molecule. It transfers chemical groups between enzymes. It is not considered part of the structural structure of the enzyme.
Vitamins are a good example of a coenzyme. They carry chemical groups of enzymes. Another term for them is co-substrate.
Also Read:- Restriction Enzymes
What is Coenzyme?
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Coenzyme is a small organic non protein molecule. She transfers chemical groups between enzymes. It is not considered a part of the structure of the enzyme. Vitamins are a good example of a coenzyme. They carry chemical groups between enzymes. Another term for them is co-substitution.
Also Read:- Digestive Enzymes
Difference Between Cofactor and Coenzyme
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The key differences between cofactor and coenzyme have been tabulated below:
| Characteristics | Cofactor | Coenzyme |
|---|---|---|
| Substitute Names | Accessory Molecules | Secondary Substrate |
| Definition | The small starcan helper or accessory molecule necessary to bring an inactive apoenzyme to an active state is called a holoenzyme or complete enzyme. Apoenzymes are conjugated Proteins that require an additional factor to act like a functional or catalytically active enzyme. | It refers to co-substrate or secondary substrate, which is a group of inactive, non-proteinate, and small organic molecules of low molecular weight ( 1000DA) They are directly involved in the catalytic reactions of the enzyme. |
| Chemical Nature | Organic and Inorganic Molecules | Organic Molecules |
| Association with Enzyme | It can be covalent or non-covalently associated with an apoenzyme. | It binds it loosely or non-covalently to an apoenzyme. |
| Division | Separation of cofactors can be easy, or difficult (only after the denaturation of the enzyme ). | Coenzymes are temporarily bound with an apoenzyme and are easily separated. |
| Dialyse | Some of the Cofactors are dialysable | It is dialysable |
| Category | The types of organospheric cofactors differ depending upon the enzymatic activity. | It is a subtype of cofactors that belongs to the category of organic cofactors. |
| Essential Part | A cofactor is a collective term for activating metal ions, coenzymes, or prosthetic groups that are required for the function of an ineffective enzyme. | The essential component of coenzymes is vitamins. |
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Things to Remember
- Coenzymes and cofactors are non-proteins that are needed for some enzymes to catalyze a reaction.
- Coenzymes are organic molecules that transfer electrons frequently. They are exchanged and recycled.
- Cofactors are often ions. They are not changed in the reaction. Concrete examples are chloride ions and zinc ions.
- Cofactor is a collective term that includes inorganic metal ions, organic compounds (coenzymes) and organic groups of prosthetics.
- Coenzymes and cofactors are additional factors that facilitate the catalytication of enzymes by combining with the inactive protein, which alone cannot transform a substrate into a product.
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Previous Years Questions
- which one of the following colours of light so as to….[NEET 2005]
- According to fluid mosaic model, plasma membrane is….[NEET 1998]
- Acetabularia used in Hammerling's nucleocytoplasmic...[NEET 1988]
- All types of plastids possess essentially….[NEET 1992]
- An outer covering membrane is absent over….[NEET 1992]
- Balbiani rings are the sites of...[NEET 1993]
- The Golgi apparatus is also concerned with the...[NEET 1994]
- A bivalent consists of...[NEET 1989]
- A cell organelle containing hydrolytic enzymes is...[NEET 2016]
- Water soluble pigments found in plant cell vacuoles….[NEET 2016]
- Which of the following are not membrane - bound?….[NEET 2015]
- Electron microscope has a high resolution power…. [NEET 1990]
- Flagella of prokaryotic and eukaryotic cells….[NEET 2004]
- A major site for synthesis of lipids is….[NEET 2013]
- Biological organisation starts with….[NEET 2007]
Sample Questions
Ques. What are the different types of coenzymes and cofactors? (1 Mark)
Ans. Some texts consider all helper molecules that bind to an enzyme to be cofactor groups, while others divide the class of chemicals into three groups. Coenzymes are organic non-protein molecules that loosely bind an enzyme.
Ques. How could cofactors be removed from an enzyme? (1 Mark)
Ans. Cofactors can be removed from an enzyme by denaturing the enzyme Cofactors increase the rate of reaction catalyzed by the enzyme in question Cofactors, like metal ions, are bonded to an enzyme. Cofactors support the function of the respective enzyme.
Ques. Is Coenzyme A a protein or cofactor? (2 Marks)
Ans. The coenzyme may be a non-protein molecule that is organic in nature. Another name for coenzyme is co-factors More about the ubiquinone, the uses of the coenzyme Q10, ubiquinol and functions of enzymes will be offered. Coenzymes, as studied above, are the factors responsible for catalyzing enzyme reactions.
Ques. How Cofactors are used in Chemical Reaction? (2 Marks)
Ans. Cofactors are molecules that combine with an enzyme in the chemical reactions. In general, all compounds that help enzymes are cofactors. But the cofactors are divided into these three subgroups. They are non-particular reusable molecules that contain carbon (organic). They bind rapidly to an enzyme at the active site to catalyze the reactions.
Ques. Give examples for coenzymes - cofactor. (2 Marks)
Ans. Vitamins are a good example of a coenzyme. They bind chemical groups between alternative enzymes. Another term for them is co-substrate. A coenzyme is a type of cofactor. It is the loosely bound cofactor of an enzyme. Cofactors are chemical compounds wrapped in proteins.
Ques. What do you need to know about cofactors? (2 Marks)
Ans. A cofactor is a chemical compound or metal ion other than proteins that is required for an enzyme to be supported as a catalyst (a substance that increases the rate of a chemical reaction). Cofactors are irradiated inorganic compounds Two types of cofactors are coenzymes and prosthetic groups.
Ques. How are coenzymes and prosthetics related? (3 Marks)
Ans. They could be organic or metallic ions and are often covalent bonded to proteins. The same cofactors can bind several different types of enzymes, some of which are loosely binding as coenzymes and others as prosthetic groups. Some cofactors can always bind their enzymes tightly.
A coenzyme prosthetic group is tightly bound to the enzyme and remains bound during the catalytic cycle. The original coenzymes are regenerated during the catalytic cycle. That means, a coenzyme substrate is loosely bound to an enzyme and dissociates in an altered form as part of the catalytic cycle.
Ques. How does a cofactor bind to an apoenzyme? (2 Marks)
Ans. Coenzymes bond to the apoenzyme and support enzyme activity. Cofactors are also called "auxiliary molecules" that help the apoenzyme catalytic reactions. Biotin, coenzyme A, NADH, NADPH and adenosine triphosphate (ATP), riboflavin, thiamine and folic acid Metal ions such as Mg2+, Cu2+, Mn2+, or in argent - sulphuric clusters.
Ques. Differentiate between coenzyme and prosthetic group. (4 Marks)
Ans. Here are the key differences between coenzyme and prosthetic group:
| Criteria | Prosthetic group | Coenzyme |
|---|---|---|
| Type of Molecule | Either metal ions or small organic molecules. | Small organic molecules. |
| Binding | Tightly-bound or stably-associated with the enzyme. Loosely-bound to the enzymes. | Binding Tightly-bound or stably-associated with the enzyme. Loosely-bound to the enzymes. |
| Role | Assists the functioning of the enzyme by binding with the apoenzyme. | Facilitates the biological transformation of the enzymes. |
| Examples | Metal ions such as Co, Mg, Cu, Fe and organic molecules such as biotin and FAD. | Coenzyme A, biotin, folic acid, vitamin B12. |
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