An organic cofactor or prosthetic group (nonprotein portion of the enzyme) whose presence is required for the activity of many enzymes. The prosthetic groups attached to the protein of the enzyme (the apoenzyme) may be regarded as dissociable portions of conjugated proteins. Neither the apoenzyme nor the coenzyme moieties can function singly. In general, the coenzymes function as acceptors of electrons or functional groupings, such as the carboxyl groups in α-keto acids, which are removed from the substrate. See Protein
Well-known coenzymes include the pyridine nucleotides, nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP); thiamine pyrophosphate (TPP); flavin mononucleotide (FMN) and flavinadenine dinucleotide (FAD); iron protoporphyrin (hemin); uridine diphosphate (UDP) and UDP-glucose; and adenosine triphosphate (ATP), adenosine diphosphate (ADP), and adenosine monophosphate (AMP). Coenzyme A (CoA), a coenzyme in certain condensing enzymes, acts in acetyl or other acyl group transfer and in fatty acid synthesis and oxidation. Folic acid coenzymes are involved in the metabolism of one carbon unit. Biotin is the coenzyme in a number of carboxylation reactions, where it functions as the actual carrier of carbon dioxide. See Adenosine diphosphate (ADP), Adenosine triphosphate (ATP), Biotin, Enzyme, Hemoglobin, Nicotinamide adenine dinucleotide (NAD), Nicotinamide adenine dinucleotide phosphate (NADP)