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Catechol. A catecholamine (/ ˌ k æ t ə ˈ k oʊ l ə m iː n /; abbreviated CA) is a monoamine neurotransmitter, an organic compound that has a catechol (benzene with two hydroxyl side groups next to each other) and a side-chain amine. [1] Catechol can be either a free molecule or a substituent of a larger molecule, where it represents a 1,2 ...
Catechol (/ ˈ k æ t ɪ tʃ ɒ l / or / ˈ k æ t ɪ k ɒ l /), also known as pyrocatechol or 1,2-dihydroxybenzene, is an organic compound with the molecular formula C 6 H 4 (OH) 2. It is the ortho isomer of the three isomeric benzenediols .
Catechol-O-methyltransferase (COMT; EC 2.1.1.6) is one of several enzymes that degrade catecholamines (neurotransmitters such as dopamine, epinephrine, and norepinephrine), catecholestrogens, and various drugs and substances having a catechol structure. [7] In humans, catechol-O-methyltransferase protein is encoded by the COMT gene. [8]
Since L-DOPA is the precursor for the neurotransmitters dopamine, noradrenaline and adrenaline, tyrosine hydroxylase is therefore found in the cytosol of all cells containing these catecholamines. This initial reaction catalyzed by tyrosine hydroxylase has been shown to be the rate limiting step in the production of catecholamines. [11]
A dopamine molecule consists of a catechol structure (a benzene ring with two hydroxyl side groups) with one amine group attached via an ethyl chain. [14] As such, dopamine is the simplest possible catecholamine, a family that also includes the neurotransmitters norepinephrine and epinephrine. [15]
According to Kukushkin, the memories stored in non-brain cells in other parts of the body are memories strictly related to the roles that those specific cells play in human health. Thus, he detailed:
l-DOPA can be directly metabolized by catechol-O-methyl transferase to 3-O-methyldopa, and then further to vanillactic acid. This metabolic pathway is nonexistent in the healthy body, but becomes important after peripheral l-DOPA administration in patients with Parkinson's disease or in the rare cases of patients with AADC enzyme deficiency. [11]
Mammalian siderophores, specifically catechols, can be found in the human gut and in siderophores, such as enterobactin, and serve as iron-binding moieties. [5] [26] Catechol resembling molecules can act as iron ligands in the cell and in systematic circulation, allowing siderocalin to bind to the iron-catechol complex. [27]