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The main alcohol dehydrogenase in yeast is larger than the human one, consisting of four rather than just two subunits. It also contains zinc at its catalytic site. Together with the zinc-containing alcohol dehydrogenases of animals and humans, these enzymes from yeasts and many bacteria form the family of "long-chain"-alcohol dehydrogenases.
Tryptophan hydroxylase (TPH; EC 1.14.16.4) is the rate-limiting enzyme in the synthesis of serotonin (5-hydroxytryptamine, or 5HT). 5HT is causally involved in numerous central nervous activities, and it has several functions in peripheral tissues, including the maintenance of vascular tone and gut motility.[supplied by OMIM] [7]
Tryptophan hydroxylase (TPH) is an enzyme (EC 1.14.16.4) involved in the synthesis of the monoamine neurotransmitter serotonin. Tyrosine hydroxylase , phenylalanine hydroxylase , and tryptophan hydroxylase together constitute the family of biopterin-dependent aromatic amino acid hydroxylases .
Metabolites involved in the kynurenine pathway include tryptophan, kynurenine, kynurenic acid, xanthurenic acid, quinolinic acid, and 3-hydroxykynurenine. [2] [3] The kynurenine pathway is responsible for about 95% of total tryptophan catabolism. [4] Disruption in the pathway is associated with certain genetic and psychiatric disorders. [5] [2 ...
The reinforcing effects of alcohol consumption are mediated by acetaldehyde generated by catalase and other oxidizing enzymes such as cytochrome P-4502E1 in the brain. [60] Although acetaldehyde has been associated with some of the adverse and toxic effects of ethanol, it appears to play a central role in the activation of the mesolimbic ...
This bidirectional communication between astrocytes and neurons add complexity to brain signaling, with implications for brain function and neurological disorders. [10] [11] Enzyme degradation – proteins called enzymes break the neurotransmitters down. Reuptake – neurotransmitters are reabsorbed into the pre-synaptic neuron.
Expression of tryptophan 2,3-dioxygenase in mammals is normally restricted to the liver, but it has been identified in the brain and epididymis of some species, and, in some tissues, its production can be induced in response to stimuli. [8] TDO from rat was the first to be expressed recombinantly (in E. coli). [10] Human TDO has also been ...
4129 109731 Ensembl ENSG00000069535 ENSMUSG00000040147 UniProt P27338 Q8BW75 RefSeq (mRNA) NM_000898 NM_172778 RefSeq (protein) NP_000889 NP_766366 Location (UCSC) Chr X: 43.77 – 43.88 Mb Chr X: 16.58 – 16.68 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Monoamine oxidase B (MAO-B) is an enzyme that in humans is encoded by the MAOB gene. The protein encoded by this gene belongs ...