Indolamines are a family of neurotransmitters that share a common molecular structure (namely, indolamine). Indolamines are a classification of monoamine neurotransmitter, along with catecholamines and ethylamine derivatives. A common example of an indolamine is the tryptophan derivative serotonin, a neurotransmitter involved in mood and sleep. Another example of an indolamine is melatonin.
In biochemistry, indolamines are substituted indole compounds that contain an amino group. Examples of indolamines include the lysergamides.
Indolamines are biologically synthesized from the essential amino acid tryptophan. Tryptophan is synthesized into serotonin through the addition of a hydroxyl group by the enzyme tryptophan hydroxylase and the subsequent removal of the carboxyl group by the enzyme 5-HTP decarboxylase.
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The goal of the course is to guide students through the essential aspects of molecular neuroscience and neurodegenerative diseases. The student will gain the ability to dissect the molecular basis of
Indole is an aromatic, heterocyclic, organic compound with the formula . It has a bicyclic structure, consisting of a six-membered benzene ring fused to a five-membered pyrrole ring. Indole is widely distributed in the natural environment and can be produced by a variety of bacteria. As an intercellular signal molecule, indole regulates various aspects of bacterial physiology, including spore formation, plasmid stability, resistance to drugs, biofilm formation, and virulence.
Monoamine neurotransmitters are neurotransmitters and neuromodulators that contain one amino group connected to an aromatic ring by a two-carbon chain (such as -CH2-CH2-). Examples are dopamine, norepinephrine and serotonin. All monoamines are derived from aromatic amino acids like phenylalanine, tyrosine, and tryptophan by the action of aromatic amino acid decarboxylase enzymes. They are deactivated in the body by the enzymes known as monoamine oxidases which clip off the amine group. Monoaminergic systems, i.
Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent. Tryptophan is also a precursor to the neurotransmitter serotonin, the hormone melatonin, and vitamin B3. It is encoded by the codon UGG. Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (–NH3+; pKa = 9.
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