by staff

What is a Coenzyme? A Coenzyme is a chemical-free molecule that combines with an enzyme to fasten a reaction, and it does not contain proteins. Coenzymes are also called Cofactors. However, they differ chemically. A Coenzyme becomes useful when combined with an enzyme, but it can’t operate alone. Alternatively, an enzyme is a protein that plays the role of a catalyst to bond and fastens a chemical reaction. So a coenzyme strengthens the function of an enzyme.

How Do Coenzymes Function?
Apoenzyme is an enzyme without a coenzyme. Additionally, a holoenzyme or an active enzyme is an enzyme that has acquired a coenzyme. Active enzyme’s role is to help an organism perform essential functions, chemical or physiological, by converting substrates into useful products. Just like enzymes, coenzymes can be used again without necessarily altering the reaction efficiency. Coenzymes hook themselves onto the active part of an enzyme that helps the accelerated reaction to take place. However, an enzyme can be affected negatively by excessive temperature or PH. And if such a case occurs, a coenzyme can no longer hook up itself onto the active site.

What Are the Types of Enzymes?
Cofactors usually link themselves to an enzyme in the process of chemical reactions. So, all molecules that assist enzymes to function are referred to as Cofactors. Cofactors are classified into three distinct subgroups regarding their functions and what they are comprised of chemically. These are:

Coenzymes
What are Coenzymes? They are organic molecules without proteins and can be recycled as well. They link themselves closely to an active site of an enzyme to assist in catalyzing reactions. In most cases, they are usually vitamins from nucleotides or vitamin by-products.

Cofactors
These differ from coenzymes in that they are inorganic molecules that do not contain proteins and can also be recycled. They are commonly found in metal ions such as cobalt, copper, zinc, and iron. Cofactors attach themselves just about the enzyme’s active site. They should be supplemented in meals because most living organisms can’t synthesize metal ions naturally.

Prosthetic Groups
Contrary to Coenzymes and Cofactors, these groups attach firmly to enzymes to assist in catalyzing reactions. The groups commonly play a considerable role in photosynthesis and cellular respiration. They can be classified as sugars, lipids, inorganic metal ions, or organic vitamins.

Which Are the Examples of Coenzymes?
Usually, living organisms can’t produce Coenzymes in large amounts for efficiency. That is why they are occasionally introduced into organisms, and this happens in two methods;

Vitamins
Most Coenzymes are mainly vitamins or are gotten from vitamins, though not all Coenzymes. If an organism takes small amounts of vitamins, likely, they won’t have enough Coenzymes that can aid in catalyzing reactions. Vitamins that are water-soluble such as vitamin B and vitamin C, resulting in the generation of Coenzymes. The essential Coenzymes obtained from vitamins are; nicotinamide adenine dinucleotide (NAD) and Coenzyme A. NAD is obtained from Vitamin B3. If an organism lack NAD Coenzyme, they usually experience a lot of fatigue. This Coenzyme is also responsible for protecting cells from dangerous substances. Naturally, Coenzyme A is obtained from Vitamin B5. This Coenzyme triggers fatty acid production from cells and the citric acid cycle, leading to ATP production.

Non-Vitamins
These generally help in the chemical transfer of enzymes. Are responsible for blood clotting and metabolism in an organism. They are found in nucleotides like uracil, guanine, inosine, and adenosine. Adenosine Triphosphate is a perfect example of a non-vitamin Coenzyme that distributes the energy used in chemical reactions and muscle contraction.

Conclusion
Enzymes can’t catalyze reactions without the help of Coenzymes and Cofactors. The enzyme might not even be useful. And there are no reactions taking place in an organism; of course, the organism will lose its life.

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