Biochemistery

Coenzyme: Definition,Function,Structure & All types2024

What is Coenzyme and Why Is It Important for Life?

To any agent that an enzyme needs for activity, it is called a cofactor. If the cofactor is an organic substance, it is called a coenzyme. Enzymes may be linked to the cofactor through a covalent or non-covalent bond. Enzymes linked to the cofactor by a covalent bond are called prosthetic groups.

What is Coenzyme

1- Vitamins and Coenzymes

Coenzymes derived from vitamins are generally derived from B vitamins and vitamin C. Thiamine pyrophosphate, CoA, NADP, NAD, FMN, FAD, Methylcobalamin, and pyridoxal phosphate are among the vitamins that are derived from B vitamins. Vitamin C itself acts as a coenzyme in many body reactions.

– Coenzymes derived from vitamins B

Water-soluble vitamins of group B play an important role in the production and synthesis of enzyme cofactors. Many vitamin cofactors are synthesized from B vitamins.

Thiamine pyrophosphate (TPP or ThPP)

Thiamine pyrophosphate (TPP) is synthesized from vitamin thiamine (B1). Enzymes that catalyze oxidative decarboxylation reactions require TPP for activity. The thiamine moiety has a thiazole ring. Thiazole is activated during the reaction and converted to a carbonyl. (read more about vitamin b1 deficiency diseases.)

Carbonyl can attack various compounds and cause their decarboxylation. Alpha-ketoglutarate dehydrogenase, pyruvate dehydrogenase complex, alpha-keto acid branched chain dehydrogenase, and transketolase require TPP for their activity.

Ribonucleofaloprotein coenzymes

FAD and FMN are synthesized from riboflavin. Riboflavin has an isoalloxazine ring that is linked to the sugar alcohol ribitol. The isoalloxazine ring in these enzymes can be reduced reversibly, so these enzymes participate in oxidation-reduction reactions. Enzymes that use these two types of coenzymes are identified as flavoproteins. If flavoprotein also requires a metal for its activity, it is called metalloflavoprotein. Citrate synthase, succinate dehydrogenase, and dihydrolipoamide dehydrogenase use FAD as a coenzyme. Xanthine oxidase, L-amino acid oxidase, and NADH dehydrogenase use FMN as a coenzyme.

Nicotinamide Coenzymes

Nicotinic acid is a derivative of pyridine. Two coenzymes, NAD and NADP, are synthesized from nicotinic acid (B3). The nicotinamide pyridine ring of NAD and NADP can be reduced reversibly, so these coenzymes participate in oxidation-reduction reactions. NAD coenzyme participates more in oxidative reactions and can enter the respiratory chain and produce ATP. Lactate dehydrogenase, pyruvate dehydrogenase, malate dehydrogenase, and glyceraldehyde 3-phosphate dehydrogenase use NAD as a coenzyme. NADP provides the necessary equivalents for synthesizing various substances, such as fatty acids. This coenzyme does not enter the respiratory chain.

Biotin

Biotin acts as a coenzyme in carboxylation reactions. A carboxylate ion is first attached to N-biotin, and an intermediate compound called carboxybiotin is created to perform carboxylation. Carboxybiotin then transfers the carboxylate group to the desired protein.

Coenzyme A

Coenzyme A (CoA) has a thiol group attached to acyl groups. This coenzyme acts as a carrier of acyl groups in the body.

Pyridoxal phosphate (PLP)

Pyridoxal phosphate (PLP) is synthesized from vitamin B6. This coenzyme participates in transamination and non-oxidative decarboxylation reactions. The aldehyde group of this coenzyme forms a Schiff base with the amino acid amino group.

Tetrahydrofolate (TH4)

Tetrahydrofolate (TH4) is a molecule composed of pteridine base, aminobenzoic acid (PABA), and glutamic acid. TH4 can carry an activated one-carbon unit in various ways. TH4 can be converted to N10, N5-methyl H4 folate by receiving a carbon source from serine (the primary source of one-carbon units) through reduction to N5-methyl H4 folate, which participates in the conversion of homocysteine to methionine.

Methylcobalamin and deoxy-Adenosylcobalamin

Methylcobalamin and deoxy-Adenosylcobalamin are forms of Vitamin B12 that contain a corrin ring and can be converted into the coenzymes Methylcobalamin and deoxy-Adenosylcobalamin. Methylcobalamin is involved in converting homocysteine to methionine and methyl tetrahydrofolate to tetrahydrofolate. Daxi Adenosylcobalamin is involved in the conversion of methylmalonyl CoA to succinyl CoA.

Vitamin Coenzyme Role
B1 (Thiamine) Thiamine pyrophosphate (TPP) Involved in the oxidative decarboxylation of pyruvate, \uD835\uDEFC-keto acids, and transketolase reactions
B2 (Riboflavin) Flavin mononucleotide (FMN) Participates in electron transfer reactions in carbohydrate, lipid, purine, and amino acid metabolism
B2 (Riboflavin) Flavin adenine dinucleotide (FAD) Participates in electron transfer reactions in carbohydrate, lipid, purine, and amino acid metabolism
B3 (Niacin) Nicotinamide adenine dinucleotide (NAD) Acts as an electron carrier in oxidation-reduction reactions in glycolysis, Krebs cycle, and fatty acid oxidation
B3 (Niacin) Nicotinamide adenine dinucleotide phosphate (NADP) Acts as an electron carrier in oxidation-reduction reactions in the pentose phosphate pathway, fatty acid synthesis, and cholesterol synthesis
B5 (Pantothenic acid) Coenzyme A (CoA) Carries acyl groups in fatty acid synthesis and degradation, Krebs cycle, and amino acid metabolism
B6 (Pyridoxine) Pyridoxal phosphate (PALP) Acts as a coenzyme for various enzymes involved in amino acid metabolism, such as transamination, decarboxylation, and racemization
B7 (Biotin) Biocytin Acts as a coenzyme for carboxylases that catalyze the addition of CO2 to various substrates
B9 (Folic acid) Tetrahydrofolic acid (THFA) Transfers one-carbon units in nucleotide synthesis, amino acid metabolism, and methylation reactions
B12 (Cobalamin) Deoxyadenosyl cobalamin Acts as a coenzyme for enzymes that catalyze the rearrangement of carbon skeletons, such as methylmalonyl-CoA mutase
B12 (Cobalamin) Methylcobalamin Acts as a coenzyme for methionine synthase, which transfers a methyl group from N5-methyl-THFA to homocysteine to form methionine

– Vitamin C

Vitamin C acts as a reducing agent. Many enzymes require vitamin C as a coenzyme for their activity. Here is a table of enzymes that require vitamin C as a coenzyme:

Enzyme Function
Prolyl hydroxylase Hydroxylation of proline residues in collagen
Lysyl hydroxylase Hydroxylation of lysine residues in collagen
Dopamine beta-hydroxylase Conversion of dopamine to norepinephrine
Peptidylglycine alpha-amidating monooxygenase Amidation of peptide hormones
Tryptophan hydroxylase Conversion of tryptophan to serotonin

2- Metabolic coenzymes

Some coenzymes in the body are not derived from vitamins. These coenzymes may be derived from amino acid derivatives or have a peptide structure. The most important of these coenzymes are listed in the table.

Metabolic coenzymes Function
S- Adenosylmethionine methionine group donor
PAPS Transfer of sulfate group
Glutathione electron donor
Tetrahydrobiopterin Electron transfer
Ubiquitin Electron transfer
Lipoamide The transferor of Acyl groups

Reference:

brenda-enzymes.org/oldstart.php

Mahdi Morshedi Yekta

Nothing fascinates me more than medical science, as it constantly challenges me to learn new things and improve my skills.

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