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Coenzymes: Structure and Biochemical Functions

Metabolites are formed by combining molecules or atoms. By breaking down complex molecules, enzymes make simpler and smaller molecules.
Metabolites are formed by combining molecules or atoms. By breaking down complex molecules, enzymes make simpler and smaller molecules. The biochemical and cellular organization however have an impact on enzymes. Catalysts and enzymes both accelerate reactions chemically without even wanting modification or change to themselves. The formation of optical isomers involves carboxyl group transfer, peptide linkage hydrolysis, and breaking of carbon bonds, among many other biological processes. A cofactor can be in need if enzymes are unable to function alone in these reactions.

Holoenzymes or active enzymes are complexes made up of two parts: a protein or apoenzyme and cofactors. Proteins or apoenzymes cannot function alone; they need a cofactor to function. Activators, which are usually cations, can be cofactors. In addition to coenzymes, organic molecules possess complex structures. Coenzymes, which are non-protein compounds, are normally required for enzyme catalysis. The highly conjugated nature of cofactors to apoenzymes prevents the separation of the two enzyme components without causing denaturation to the enzyme proteins.

Coenzyme - For an enzyme to catalyze a chemical reaction, it requires a particular molecule. Vitamins are the source of a good deal of them, especially those that contain phosphorylated derivatives of water-soluble vitamins. Coenzymes catalyze reactions by binding to the active site of enzymes (apoenzymes). However, coenzymes are not considered substrates of the reaction even when they activate enzymes. Coenzymes are mainly responsible for transporting electrons between the reactants in reaction chains.

Examples – flavin adenine dinucleotide (FAD), nicotinamide adenine dinucleotide (NAD), and nicotinamide adenine dinucleotide phosphate (NADP).

All three coenzymes play a role in oxidation and hydrogen transfer. During the transfer of acyl groups, coenzyme A (CoA) is involved.

Several biochemical pathways are dependent on coenzymes that occur in the body. Among them are the catabolism of macronutrients and the anabolism of biological compounds.

Coenzymes are normally called co-substrates because, at the beginning of a chemical reaction, they bind to the enzyme along with the substrate and they alter the enzyme at the end. Coenzymes bind to enzymes before other substrates will, which is why they are called coenzymes. In addition, coenzymes are transformed again into their original forms by other enzymes in the cell. Activated vitamins are coenzymes in biochemical pathways.

Enzymes create complexes with coenzymes. This process produces energy from nutrients. Life itself is based on biomolecules that they produce. Cofactors and coenzymes are nutrients, such as vitamins and minerals. The breakdown of coenzymes involves vitamin and mineral cofactors. Thus, maintaining a proper dietary intake of trace elements is crucial for the production of energy.

Functions of co-enzymes

To lead the synthesis of the biomolecules, there are anabolic as well as catabolic pathways in which vitamins and minerals play a very important role. The biomolecules include nucleic acids, carbohydrates, lipids, and proteins as cofactors or coenzymes.

Vitamins as coenzymes - Retinoic acid is a metabolite of vitamin A that functions as a gene regulator and, thus, is important for cell growth. The enzymes that move -CO2 groups (g-carboxylases) require vitamin K as a coenzyme. This step is crucial for osteocalcin, a protein involved in bone remodeling, to form, as the carboxylic group is released. In addition, it is crucial for the coagulation of blood, as prothrombin is formed from it.

Minerals as cofactors and catalysts - A cofactor or catalyst can act as a mineral in biological processes. An enzyme or its substrate cannot be incorporated into minerals that act as catalysts. Their function is to increase the speed of the biochemical reaction between the enzyme and the substrate. A mineral's normal function is to act as a cofactor in biochemical reactions through the structure of enzymes or proteins. Magnesium, manganese, selenium, and molybdenum are minerals that act as cofactors. For certain non-enzymatic proteins, minerals like cobalt, iodine, calcium, and phosphorus have the role of cofactors. Cofactors like copper, zinc, and iron are involved in both enzymatic and non-enzymatic processes.
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Ankur Choudhary is India's first professional pharmaceutical blogger, author and founder of, a widely-read pharmaceutical blog since 2008. Sign-up for the free email updates for your daily dose of pharmaceutical tips.
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