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Aromatic amino acid decarboxylase hydroxylases

The synthesis and metabolism of trace amines and monoamine neurotransmitters largely overlap [1]. The trace amines PEA, TYR and TRP are synthesized in neurons by decarboxylation of precursor amino acids through the enzyme aromatic amino acid decarboxylase (AADC). OCT is derived from TYR. by involvement of the enzyme dopamine (3-hydroxylase (Fig. 1 DBH). The catabolism of trace amines occurs in both glia and neurons and is predominantly mediated by monoamine oxidases (MAO-A and -B). While TYR., TRP and OCT show approximately equal affinities toward MAO-A and MAO-B, PEA serves as preferred substrate for MAO-B. The metabolites phenylacetic acid (PEA), hydroxyphenylacetic acid (TYR.), hydroxymandelic acid (OCT), and indole-3-acetic (TRP) are believed to be pharmacologically inactive. [Pg.1218]

Trace Amines. Figure 1 The main routes of trace amine metabolism. The trace amines (3-phenylethylamine (PEA), p-tyramine (TYR), octopamine (OCT) and tryptamine (TRP), highlighted by white shading, are each generated from their respective precursor amino acids by decarboxylation. They are rapidly metabolized by monoamine oxidase (MAO) to the pharmacologically inactive carboxylic acids. To a limited extent trace amines are also A/-methylated to the corresponding secondary amines which are believed to be pharmacologically active. Abbreviations AADC, aromatic amino acid decarboxylase DBH, dopamine b-hydroxylase NMT, nonspecific A/-methyltransferase PNMT, phenylethanolamine A/-methyltransferase TH, tyrosine hydroxylase. [Pg.1219]

Because LCEC had its initial impact in neurochemical analysis, it is not, surprising that many of the early enzyme-linked electrochemical methods are of neurologically important enzymes. Many of the enzymes involved in catecholamine metabolism have been determined by electrochemical means. Phenylalanine hydroxylase activity has been determined by el trochemicaUy monitoring the conversion of tetrahydro-biopterin to dihydrobiopterin Another monooxygenase, tyrosine hydroxylase, has been determined by detecting the DOPA produced by the enzymatic reaction Formation of DOPA has also been monitored electrochemically to determine the activity of L-aromatic amino acid decarboxylase Other enzymes involved in catecholamine metabolism which have been determined electrochemically include dopamine-p-hydroxylase phenylethanolamine-N-methyltransferase and catechol-O-methyltransferase . Electrochemical detection of DOPA has also been used to determine the activity of y-glutamyltranspeptidase The cytochrome P-450 enzyme system has been studied by observing the conversion of benzene to phenol and subsequently to hydroquinone and catechol... [Pg.29]

Dopamine is formed from tyrosine by hyclroxylation with tyrosine hydroxylase and the removal of a CO2 group by aromatic amino acid decarboxylase. The catecholamine is found in high concentrations in parts of the brain—the caudate nucleus, the median eminence, the tuberculum olfactorium, and the nucleus accumbens. Dopamine appears to act as an inhibitory neurotransmitter. [Pg.195]

Dopamine synthesis in dopaminergic terminals (Fig. 46-3) requires tyrosine hydroxylase (TH) which, in the presence of iron and tetrahydropteridine, oxidizes tyrosine to 3,4-dihydroxyphenylalanine (levodopa.l-DOPA). Levodopa is decarboxylated to dopamine by aromatic amino acid decarboxylase (AADC), an enzyme which requires pyri-doxyl phosphate as a coenzyme (see also in Ch. 12). [Pg.765]

Serotonin is an indolamine neurotransmitter, derived from the amino acid L-tryptophan. Tryptophan is converted to 5-hydroxytryptophan (5-HTP) by tryptophan hydroxylase. 5-HTP is converted to 5-hydroxytryptamine (serotonin, 5-HT) by aromatic amino acid decarboxylase. In the pineal gland, 5-HT may be further converted to /V-acetyl serotonin by 5-HT /V-acetyltransferase and then to melatonin by 5-hyroxyindole-O-methyltransferase. 5-HT is catabolized by monoamine oxidase, and the primary end metabolite is 5-hydroxyindoleacetic acid (5-HIAA). [Pg.52]

Following the synthesis of 5-hydroxytryptophan (5-HTP) by tryptophan hydroxylase, the enzyme aromatic amino acid decarboxylase (also known as 5-HTP or dopa decarboxylase) then decarboxylates the amino acid to 5-HT. L-Aromatic amino acid decarboxylase is approximately 60% bound in the nerve terminal and requires pyridoxal phosphate as an essential enzyme. [Pg.71]

Another strategy of some interest is to deplete biogenic amines such as OA by inhibiting their biosynthesis. Inhibitors of such enzymes in the biosynthetic pathway as aromatic amino acid decarboxylase which converts tyrosine to tyramine, or dopamine 3 -hydroxylase which converts tyramine to OA are known and have interesting effects in insects (e.g. see 52,53)t but a discussion of this area lies outside the scope of this paper. Nevertheless, it is a particularly interesting one since these or related enzymes are also needed to produce catecholamines for cuticular sclerotiza-tion, thus offering dual routes to the discovery of compounds with selectively deleterious actions on insects. [Pg.114]

Whilst the term biogenic amine strictly encompasses all amines of biological origin, for the purpose of this article it will be employed to refer to the catecholamine (dopamine, noradrenaline) and serotonin group of neurotransmitters. These neurotransmitters are generated from the amino acid precursors tyrosine and tryptophan, respectively, via the action of the tetrahydrobiopterin (BH4)-dependent tyrosine and tryptophan hydroxylases. Hydroxylation of the amino acid substrates leads to formation of 3,4-dihydroxy-l-phenylalanine ( -dopa) and 5-hydroxytryptophan, which are then decarboxylated via the pyridoxalphosphate-dependent aromatic amino acid decarboxylase (AADC) to yield dopamine and serotonin [4]. In noradrenergic neurones, dopamine is further metabolised to noradrenaline through the action of dopamine-jS-hydroxylase [1]. [Pg.703]

FIGURE 5—34. Serotonin (5-hydroxytryptamine [5HT ) is produced from enzymes after the amino acid precursor tryptophan is transported into the serotonin neuron. The tryptophan transport pump is distinct from the serotonin transporter (see Fig. 5—35). Once transported into the serotonin neuron, tryptophan is converted into 5-hydroxytryptophan (5HTP) by the enzyme tryptophan hydroxylase (TryOH) which is then converted into 5HT by the enzyme aromatic amino acid decarboxylase (AAADC). Serotonin is then stored in synaptic vesicles, where it stays until released by a neuronal impulse. [Pg.170]

The general scheme of the biosynthesis of catecholamines was first postulated in 1939 (29) and finally confirmed in 1964 (Fig. 2) (30). Although not shown in Figure 2, in some cases the amino acid phenylalanine [63-91-2] can serve as a precursor it is converted in the liver to (-)-tyrosine [60-18-4] by the enzyme phenylalanine hydroxylase. Four enzymes are involved in E formation in the adrenal medulla and certain neurons in the brain tyrosine hydroxylase, dopa decarboxylase (also referred to as L-aromatic amino acid decarboxylase), dopamine-P-hydroxylase, and phenylethanolamine iV-methyltransferase. Neurons that form DA as their transmitter lack the last two of these enzymes, and sympathetic neurons and other neurons in the central nervous system that form NE as a transmitter do not contain phenylethanolamine N-methyl-transferase. The component enzymes and their properties involved in the formation of catecholamines have been purified to homogeneity and their properties examined. The human genes for tyrosine hydroxylase, dopamine- 3-oxidase and dopa decarboxylase, have been cloned (31,32). It is anticipated that further studies on the molecular structure and expression of these enzymes should yield interesting information about their regulation and function. [Pg.355]

Tyrosine is converted to dopa by the rate-limiting enzyme tyrosine hydroxylase, which requires tetrahydrobiopterin, and is inhibited by a-methyltyrosine. Dopa is decarboxylated to dopamine by L-aromatic amino acid decarboxylase, which requires pyridoxal phosphate (vitamin B6) as a coenzyme. Carbidopa, which is used with levodopa in the treatment of parkinsonism, inhibits this enzyme. Dopamine is converted to norepinephrine by dopamine P-hydroxylase, which requires ascorbic acid (vitamin C), and is inhibited by diethyldithiocarbamate. Norepinephrine is converted to epinephrine by phenylethanolamine A -methyltransferase (PNMT), requiring S-adeno-sylmethionine. The activity of PNMT is stimulated by corticosteroids. [Pg.518]

One of the best characterized physiological functions of (6R)-tetrahydrobio-pterin (BH4, 43) is the action as a cofactor for aromatic amino acid hydroxylases (Scheme 28). There are three types of aromatic amino acid hydroxylases phenylalanine hydroxylase [PAH phenylalanine monooxygenase (EC 1.14.16.1)], tyrosine hydroxylase [TH tyrosine monooxygenase (EC 1.14.16.2)] and tryptophan hydroxylase [TPH tryptophan monooxygenase (EC 1.14.16.4)]. PAH converts L-phenylalanine (125) to L-tyrosine (126), a reaction important for the catabolism of excess phenylalanine taken from the diet. TH and TPH catalyze the first step in the biosyntheses of catecholamines and serotonin, respectively. Catecholamines, i.e., dopamine, noradrenaline and adrenaline, and serotonin, are important neurotransmitters and hormones. TH hydroxylates L-tyrosine (126) to form l-DOPA (3,4-dihydroxyphenylalanine, 127), and TPH catalyzes the hydroxylation of L-tryptophan (128) to 5-hydroxytryptophan (129). The hydroxylated products, 127 and 129, are decarboxylated by the action of aromatic amino acid decarboxylase to dopamine (130) and serotonin (131), respectively. [Pg.158]

Fig. 1. A. Chemical structure of key molecules involved in the key steps in intracerebral synthesis and metabolism of dopamine. The successive steps are regulated by the enzymes tyrosine hydroxylase (TH), aromatic amino acid decarboxylase (AADC), monoamine oxidase (MAO) and dopamine-p-hydroxylase (DBH). B. Structure of key toxins and other drugs acting on dopamine neurones, including 6-hydroxydopamine (6-OHDA), a-methyl tyrosine, and amphetamine. For further details see Iversen and Iversen (1981) or Cooper et al. (1996). Fig. 1. A. Chemical structure of key molecules involved in the key steps in intracerebral synthesis and metabolism of dopamine. The successive steps are regulated by the enzymes tyrosine hydroxylase (TH), aromatic amino acid decarboxylase (AADC), monoamine oxidase (MAO) and dopamine-p-hydroxylase (DBH). B. Structure of key toxins and other drugs acting on dopamine neurones, including 6-hydroxydopamine (6-OHDA), a-methyl tyrosine, and amphetamine. For further details see Iversen and Iversen (1981) or Cooper et al. (1996).
Figure 13.4. Synthesis of the catecholamines. Tyrosine hydroxylase, EC 1.14.16.2 (see also Fignre 10.10) aromatic amino acid decarboxylase, EC 4.1.1.26 and dopamine -hydroxylase, EC 1.14.17.1. Figure 13.4. Synthesis of the catecholamines. Tyrosine hydroxylase, EC 1.14.16.2 (see also Fignre 10.10) aromatic amino acid decarboxylase, EC 4.1.1.26 and dopamine -hydroxylase, EC 1.14.17.1.
The synthesis of 5-HT from tryptophan in serotonergic neurons occurs in two steps. First, the enzyme tryptophan hydroxylase catalyzes the conversion of tryptophan to 5-hydroxytryptophan (5-HTP). Then, the enzyme aromatic amino acid decarboxylase catalyzes the conversion of 5-FlTP to serotonin. [Pg.100]

Catecholamines are endogenous compounds and are synthesized in the brain, the adrenal medulla, and by some sympathetic nerve fibers. The biosynthesis of catecholamines begins with the hydroxylation of tyrosine by tyrosine hydroxylase to form L-dopa, which is decarboxylated by aromatic amino acid decarboxylase to form dopamine. Norepinephrine... [Pg.487]

Baker H. 1990. Unilateral, neonatal olfactory deprivation alters tyrosine hydroxylase expression but not aromatic amino acid decarboxylase or GABA immunoreactivity. Neuroscience 36 761-771. [Pg.183]

Figure 7.1 Pathways of synthesis and metabolism of catecholamines with enzymes catalyzing various reactions. (1) Tyrosine hydroxylase (2) aromatic amino acid decarboxylase (3) phenylamine-P-hydroxylase (4) phenylethanolamine-A-methyltransferase (5) monoamine oxidase plus aldehyde dehydrogenase (6) catechol-O-methyltransferase (7) conjugating enzymes about 95% phenolsulfo-transferase and 5% phenolglucuronatetransferase (in human). DOPA, dihydroxyphenylalanine DOMA, dihydroxymandelic acid DHPG, dihydroxyphenylglycol DOPAC, dihydroxyphenylacetic acid HVA, homovanillic acid MHPG, methoxyhydroxylphenylglycol VMA, vanilmandelic acid... Figure 7.1 Pathways of synthesis and metabolism of catecholamines with enzymes catalyzing various reactions. (1) Tyrosine hydroxylase (2) aromatic amino acid decarboxylase (3) phenylamine-P-hydroxylase (4) phenylethanolamine-A-methyltransferase (5) monoamine oxidase plus aldehyde dehydrogenase (6) catechol-O-methyltransferase (7) conjugating enzymes about 95% phenolsulfo-transferase and 5% phenolglucuronatetransferase (in human). DOPA, dihydroxyphenylalanine DOMA, dihydroxymandelic acid DHPG, dihydroxyphenylglycol DOPAC, dihydroxyphenylacetic acid HVA, homovanillic acid MHPG, methoxyhydroxylphenylglycol VMA, vanilmandelic acid...
Tyrosine is actively transported into nerve endings and is converted to dihydroxyphenylalanine DOPA) via tyrosine hydroxylase 1). This step is rate limiting in the synthesis of NE. DOPA is converted to dopamine (DA) via L-aromatic amino acid decarboxylase (DOPA decarboxylase). DA in turn is metabolized to NE via DA beta hydroxylase and is taken up and stored in granules (6). Inactivation ofNE via monoamine oxidase (MAO) (2) may regulate prejunctional levels of transmitter in the mobile pool (3) but not the NE stored in granules. [Pg.53]

Figure 12-3. Synthesis and metabolism of serotonin. TH = tryptophane hydroxylase AAD = l-aromatic amino acid decarboxylase MAO = monoamine oxidase ADH = aldehyde dehydrogenase. (Broken arrow indicates possible aberrant pathway.)... Figure 12-3. Synthesis and metabolism of serotonin. TH = tryptophane hydroxylase AAD = l-aromatic amino acid decarboxylase MAO = monoamine oxidase ADH = aldehyde dehydrogenase. (Broken arrow indicates possible aberrant pathway.)...
T. colubriformis, N. brasiliensis and Litomosoides carinii (167). In C. elegans, formaldehyde-induced fluorescence (FIF) revealed eight dopaminergic sensory neurons in A. suum, only four of these sensory neurons show unequivocal DA-like FIF (183). Tyrosine hydroxylase and aromatic amino acid decarboxylase activity are found in C. elegans. [Pg.272]

Fig. 22.3. Tyrosine is hydroxylated in a rate-limiting step by tyrosine hydroxylase (TOH) to form dihydroxylphenylalanine (DOPA), which is decarboxylated by L-aromatic amino acid decarboxylase (AAD) to form dopamine (DA). Newly synthesized DA is stored in vesicles, from which release occurs into the synaptic... Fig. 22.3. Tyrosine is hydroxylated in a rate-limiting step by tyrosine hydroxylase (TOH) to form dihydroxylphenylalanine (DOPA), which is decarboxylated by L-aromatic amino acid decarboxylase (AAD) to form dopamine (DA). Newly synthesized DA is stored in vesicles, from which release occurs into the synaptic...
Norepinephrine is biosynthesized in the neurons of both the central nervous system and the autonomio nervous system, whereas EPI is formed in the ohromaffin cells of the adrenal medulla. Both NE and EPI are derived from L-tyrosine by a series of enzyme-catalyzed reactions (Fig. 44.4 depicts the overall pathway). L-Tyrosine hydroxylase hydroxylates the meta position of L-tyrosine, producing L-dihydroxyphenylalanine (L-DOPA) and is the rate-limiting step. The L-DOPA is then decarboxylated by L-aromatic amino acid decarboxylase to form dopamine, which is converted to NE by the action of dopamine p-hydroxylase. Dopamine p-hydroxylase occurs in storage vesicles of the nerve ending, and the NE formed is stored there until it is released into the synaptic cleft. In the chromaffin cells, the formed NE is converted to EPI by N-methylation catalyzed by phenylethanolamine N-methyltransferase. [Pg.1926]

V-arachidonoyl-dopamine (NADA, 27) is an endogenous capsaicin-like substance in mammalian nervous tissues. NADA activates cannabinoid CB, receptors, but not dopamine D1 and D2 receptors (Bezuglov et al., 2001 Bisogno et al., 2000). NADA occurs in nervous tissues, with the highest concentrations being found in the striatum, hippocampus, and cerebellum and the lowest concentrations in the dorsal root ganglion (Chu et al., 2003). Proposed mechanisms of NADA biosynthesis include the condensation of AA with tyrosine and the subsequent conversion of A-arachidonoyl-tyrosine to NADA by tyrosine hydroxylase and L-aromatic amino acid decarboxylase. [Pg.36]


See other pages where Aromatic amino acid decarboxylase hydroxylases is mentioned: [Pg.355]    [Pg.438]    [Pg.439]    [Pg.164]    [Pg.438]    [Pg.439]    [Pg.126]    [Pg.398]    [Pg.80]    [Pg.431]    [Pg.355]    [Pg.595]    [Pg.1031]   


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