Coenzyme: Definition, Characteristic, and Examples
Coenzyme Definition
Coenzyme is a molecule necessary for catalysis of a chemical reaction by a specific enzyme. Many are produced from vitamins, particularly water-soluble vitamins that have been phosphorylated. When coenzymes attach to the active site of an enzyme (called an apoenzyme) and then create the active enzyme, they engage in catalysis (called holoenzyme). Despite the fact that coenzymes activate enzymes, they are not considered reaction substrates.
The main role of a coenzyme in a reaction is to act as an intermediary carrier of transferred electrons or functional groups. Nicotinamide adenine dinucleotide (NAD), nicotineamide adenine dinucleotide phosphate (NADP), and flavin adenine dinucleotide constitute examples of coenzymes (FAD). These three coenzymes are involved in hydrogen transport or oxidation. Another is coenzyme A (CoA), which is involved in acyl group transfer.
What is Coenzyme?
Enzymes have the ability to break down complex large molecules into smaller ones, as well as combine tiny molecules or atoms to produce massive metabolites. Enzymes, as a result, play a crucial role in biochemical and cellular order. Enzymes are comparable to catalysts in that they have the chemical capacity to speed up processes without changing or consuming themselves. Carboxyl group transfer, peptide linkage hydrolysis, carbon bond breaking, and the conversion of compounds to their optical isomers are examples of biological processes.
Enzymes may or may not work alone in certain processes, and they may require the aid of a cofactor. A holoenzyme, also known as an active enzyme, is a two-part complex that includes the protein component (apoenzyme) and the cofactor part. The protein component, or apoenzyme, can not operate without the help of the cofactor. An activator, which is generally a cation, might be a cofactor. It might also be a coenzyme, which is an organic molecule with a complex structure. The presence of non-protein molecules termed coenzymes is critical for enzyme catalytic function. Because cofactors are tightly linked to apoenzymes, it is impossible to separate coenzymes from apoenzymes without denaturing the enzyme proteins.
Coenzyme Characteristics
Coenzymes are involved in a variety of biochemical processes, including the breakdown of macronutrients into smaller molecules (catabolism) and the synthesis of new biological substances in the body (anabolism).
Because it binds to the enzyme together with the substrate at the start of a chemical process and leaves the enzyme changed at the conclusion, a coenzyme is also referred to as a co-substrate. Coenzymes, on the other hand, are named after the fact that they attach to the enzyme before other substrates do. Furthermore, other enzymes in the cell convert coenzymes back to their original form, allowing them to be reused. A coenzyme is a type of activated vitamin that is required for metabolic processes to function. Coenzymes and enzymes create complexes. These complexes turn nutrients into energy that may be used. They create biomolecules, which are the building blocks of life.
Cofactors and coenzymes are nutrients that function as cofactors and coenzymes. Others are broken down with the assistance of coenzymes. As a result, it is critical to maintain trace element consumption in the diet in order to create the energy necessary for survival.
Enzymes that rely on coenzymes to operate will be unable to sustain normal metabolic activities or the activity of natural biochemical processes that keep the cell’s normal functions active, such as cell growth, differentiation, division, and repair.
Coenzymes also help to maintain the structural integrity of several regulatory proteins and hormones.
Some vitamins function as coenzymes in biochemical processes such as catabolism, anabolism, and energy generation. Vitamins A and K are fat-soluble vitamins that function as coenzymes or cofactors, although all water-soluble enzymes may do the same. Vitamins play an important part in the synthesis of hormones, the integrity of collagen in bones, blood clotting, and correct eyesight, in addition to their function as cofactors.
Coenzyme Examples
Coenzymes are not substrate-specific; rather, they serve as a carrier for the reaction products. Coenzymes are regenerated so that they can be utilised again. The nicotinamide adenine dinucleotide (NAD) needed to activate the lactic dehydrogenase enzyme is an example of a coenzyme.
NAD is reduced by absorbing hydrogen atoms for catalytic processes in the dehydrogenation of pyruvate to lactate, but certain enzymes require the nicotinamide adenine dinucleotide phosphate (NADP) phosphate, which is also reduced.
NADP coenzyme is necessary for the production of steroids. The reduced enzyme is then re-oxidized by transferring hydrogen through a hydrogen acceptor chain, where it is mixed with molecular oxygen to create a water molecule.
The molecule NAD+ is the first to bind to the enzyme and the last to dissociate from the complex. As a result, it is the biochemical reaction’s rate-limiting phase. As a result, it is classified as a coenzyme rather than a substrate.
Nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP) aid in the catabolic process of amino acids, lipids, and carbohydrates, as well as enzymes involved in the production of steroids, fats, and other metabolites.
Types of Coenzyme
Several enzymes, such as flavoproteins and some pyridoxine-and biotin-containing enzymes, have a built-in cofactor termed prosthetic groups. Metal-containing enzymes are known as flavoproteins. They transfer hydrogen atoms from their coenzymes, such as reduced NAD, to their prosthetic group. When absorbing hydrogen, the flavin adenine dinucleotide (FAD), which is a derivative of riboflavin, functions as a prosthetic group. The flavin is then re-oxidized by coenzyme Q, which continues the electron transport cycle to generate a water molecule. Because biotin is involved in the production of fatty acids, it is predicted to have a role in fatty acid-derived hormones like prostaglandin.
There are several additional biological processes in which coenzymes are involved. Another example is coenzymes that help in the breakdown of carbohydrates for energy generation by removing carbon dioxide (decarboxylation) from a molecule, such as the active form of vitamin B1, thiamin. Others transport hydrogen in order to participate in oxidation processes that generate energy from high-energy foods. About 120 enzymes, including synthetases, racemases, cleavage enzymes, decarboxylases, and transaminases, require the cofactors pyridoxal phosphate (PLP) and pyridoxamine phosphate (PMP). PLP and PMP are involved in distinct metabolic pathways using amino acids.
Coenzyme A is required for fatty acid, amino acid, carbohydrate, and other biological substances metabolism. It includes pantothenic acid (PA), a vitamin B derivative. As an acyl-carrier protein cofactor, PA also plays a role in fatty acid production. The coenzyme forms of vitamin B12 are involved in the production of methionine (amino acid).
Biotin’s coenzyme is biocytin. It helps to improve the metabolism of fatty acids and amino acids by assisting in various carboxylation processes. Biocytin is also involved in the production of urea. The coenzyme form of folate has one carbon unit, which is required for the conversion of amino acids to the pyrimidine and purine bases required for DNA and RNA synthesis.
Hydroxylases require ascorbic acid as a cofactor. They hydroxylate lysine and proline to maintain collagen structure, as well as cholesterol for the production of bile acids and tyrosine hydroxylation for the creation of the hormone noradrenaline.
Retinol, a vitamin A aldehyde form, is a cofactor for apoproteins present in the eye. Apoproteins are responsible for eyesight in low-light situations. They are also important for the retina’s strong light and colour vision.
Function of Coenzyme
As coenzymes or cofactors, minerals and vitamins play a critical part in the anabolic and catabolic processes that lead to the production of biomolecules, including lipids, nucleic acids, proteins, and carbohydrates.
Vitamins as Coenzymes: Because the metabolite form of vitamin A, retinoic acid, serves as a gene regulator, it is critical for cell growth. Vitamin K is a coenzyme that helps enzymes transport CO2 groups around (g-carboxylases). The carboxylic group released binds to calcium, which is necessary for the production of osteocalcin, a key protein in bone remodelling. It is also necessary for the production of prothrombin, which is essential for blood coagulation.
Minerals as Cofactors and Catalysts: Minerals can act as cofactors and catalysts in biological processes. Minerals that function as catalysts do not bind to an enzyme or its substrate. They do, however, speed up the enzyme’s biological interaction with its substrate. Minerals that function as cofactors, on the other hand, become a component of the enzyme or protein structure that is required for the biochemical reaction to take place. Manganese, selenium, magnesium, and molybdenum are minerals that serve as cofactors. Cobalt, iodine, calcium, and phosphorus are minerals that function as cofactors for non-enzymatic proteins. Non-enzymatic and enzymatic proteins, for example, need copper, zinc, and iron as cofactors.
Vitamin Deficiency: The rate of reaction is related to the concentration of enzyme in normal circumstances. As a result of the high concentration of substrate and enzyme, there is a fast rate of product turnover; enzymatic reactions, like catalysed chemical processes, are reversible. However, under normal circumstances, enzymatic reactions only go in one direction since the products are periodically absorbed by the next enzyme in the biochemical reaction chain. Because coenzymes necessary for metabolic processes are lacking in vitamin deficiency, the products of reactions pile up in the body, potentially reversing the reaction.
Coenzyme Citations
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