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Tetrahydrobiopterin aromatic amino acid hydroxylases

PTPS (6-Pyruvoyl Tetmhydropterin Synthase). 6-Pyruvoyl tetrahy-dropterin synthase catalyzes formation of tetrahydrobiopterin biosynthesis. Tetrahydrobiopterin is a cofactor for several important enzymes, such as aromatic amino acid hydroxylases and nitric oxide synthase (57). H. pylori protein HPAG1 0913 shares homology with members of the protein domain family PTPS. H. pylori protein shares poor sequence identity of 14% with the PTPS profile at an E-value of 10 10 and covers about 95% of the length of the profile. Fold recognition results also confirm the relationship between H. pylori protein and the PTPS protein domain family. A fold recognition algorithm ensures fitness of the H. pylori protein sequence on the three-dimensional structure of PTPS from... [Pg.167]

Figure 19-2. Aromatic amino acid hydroxylase reaction. Aromatic amino acids are hy-droxylated by a common mechanism catalyzed by a family of hydroxylases.The enzyme family consists of phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase. In addition to substrate, all three enzymes require molecular oxygen and the cofactor tetrahydrobiopterin.Tetrahydrobiopterin is consumed in this reaction and converted into pterin 4cx-carbinolamine. DOPA, dihydroxyphenylalanine. Figure 19-2. Aromatic amino acid hydroxylase reaction. Aromatic amino acids are hy-droxylated by a common mechanism catalyzed by a family of hydroxylases.The enzyme family consists of phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase. In addition to substrate, all three enzymes require molecular oxygen and the cofactor tetrahydrobiopterin.Tetrahydrobiopterin is consumed in this reaction and converted into pterin 4cx-carbinolamine. DOPA, dihydroxyphenylalanine.
Figure 10.10. Role of tetrahydrobiopterin in aromatic amino acid hydroxylases. Phenylalanine hydroxylase, EC 1.14.16.1 tyrosine hydroxylase, EC 1.14.16.2 tryptophan hydroxylase, EC 1.14.16.4 and dihydrobiopterin reductase (dihydropteridine reductase), EC 1.6.99.7. Figure 10.10. Role of tetrahydrobiopterin in aromatic amino acid hydroxylases. Phenylalanine hydroxylase, EC 1.14.16.1 tyrosine hydroxylase, EC 1.14.16.2 tryptophan hydroxylase, EC 1.14.16.4 and dihydrobiopterin reductase (dihydropteridine reductase), EC 1.6.99.7.
The Role of Tetrahydrobiopterin in Aromatic Amino Acid Hydroxylases... [Pg.294]

Role of tetrahydrobiopterin in aromatic amino acid hydroxylases. 295... [Pg.508]

The fourth class, the pterin-dependent hydroxylases, includes the aromatic amino acid hydroxylases, which use tetrahydrobiopterin as cofactor for the hydroxylation of Phe, Tyr, and Trp. The latter two hydroxylases catalyse the rate-limiting steps in the biosynthesis of the neurotransmitters/hormones dopamine/noradreanalme/ adrenaline and serotonin, respectively. [Pg.268]

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]

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]

The metabolism of phenylalanine will now be considered in some detail, as two inborn errors of metabolism are known that affect this pathway. Phenylalanine is first hydroxylated by phenylalanine hydroxylase to form another aromatic amino acid tyrosine (Fig. 8). The coenzyme for this reaction is the reductant tetrahydrobiopterin which is oxidized to dihydrobiopterin. Phenylalanine hydroxylase is classified as a monooxygenase as one of the atoms of 02 appears in the product and the other in HzO. The tyrosine is then trans-aminated to p-hydroxyphenylpyruvate, which is in turn converted into homogentisate by p-hydroxyphenylpyruvate hydroxylase. This hydroxylase is an example of a dioxygenase, as both atoms of 02 become incorporated into the product (Fig. 8). The homogentisate is then cleaved by homogentisate oxidase, another dioxygenase, before fumarate and acetoacetate are produced... [Pg.378]

Histamine, serotonin and the catecholamines (dopamine, epinephrine and norepinephrine) are synthesized from the aromatic amino acids histidine, tryptophan and phenylalanine, respectively. The biosynthesis of catecholamines in adrenal medulla cells and catecholamine-secreting neurons can be simply summarized as follows [the enzyme catalysing the reaction and the key additional reagents are in square brackets] phenylalanine — tyrosine [via liver phenylalanine hydroxylase + tetrahydrobiopterin] —> i.-dopa (l.-dihydroxyphenylalanine) [via tyrosine hydroxylase + tetrahydrobiopterin] —> dopamine (dihydroxyphenylethylamine) [via dopa decarboxylase + pyridoxal phosphate] — norepinephrine (2-hydroxydopamine) [via dopamine [J-hydroxylasc + ascorbate] —> epinephrine (jV-methyl norepinephrine) [via phenylethanolamine jV-methyltransferase + S-adenosylmethionine]. [Pg.232]

The pterin-dependent oxygenases, typified by the aryl amino acid hydroxylases, are a small family of closely related enzymes, which are essential to mammalian physiology. This class of metalloenzymes employs tetrahydrobiopterin (BH4) as a two-electron donating cofactor for the activation of O2. Members of this class include phenylalanine (PheH), tyrosine (TyrH) and tryptophan (TrpH) hydroxylases, which effect regiospecific aromatic hydroxylations of the namesake amino acids. [Pg.2256]

Epinephrine (adrenaline) (Figure 32-7) is synthesized from tyrosine by conversion of tyrosine to 3,4-dihydro-xyphenylalanine (dopa) by tyrosine-3-monooxygenase (tyrosine hydroxylase) in the cytosol. The mixed-function oxidase requires molecular oxygen and tetrahydro-biopterin, which is produced from dihydrobiopterin by NADPH-dependent dihydrofolate reductase. In the reaction, tetrahydrobiopterin is oxidized to dihydrobiopterin, which is reduced to the tetrahydro form by NADH-dependent dihydropteridine reductase. These reactions are similar to the hydroxylations of aromatic amino acids (phenylalanine and tryptophan), in which an obligatory biopterin electron donor system is used (Chapter 17). [Pg.761]

Tetrahydrobiopterin is the reduced form of dihydrobiopterin, an electron carrier in tyrosine biosynthesis (Figure 21.18). Tyrosine is only aromatic amino acid made in animals. The reaction is catalyzed by phenylalanine hydroxylase. [Pg.669]

Tetrahydrobiopterin (BPH4) is the natural cofactor required for the mammalian aromatic amino acid monooxygenases phenylalanine, tyrosine and tryptophan hydroxylase [4,89]. During the course of the reaction catalyzed by these enzymes, a molecule of oxygen is cleaved in order to hydroxylate the respective amino acid substrate. The remaining atom of oxygen is reduced to water at the expense of the cofactor, which is oxidized to the quinonoid form. Despite the many studies on the pterin-dependent hydroxylases, their precise mechanism of action is not well understood. This discussion will focus on mammalian phenylalanine hydroxylase (PAH), which has been favored for investigation due to its relative stability and ease of... [Pg.381]

Fig. 1.1. Biosynthesis and regeneration of tetrahydrobiopterin including possible metabolic defects and catabolism of phenylalanine. l.l=phenylalanine-4-hydroxylase (PAH) 1.2/1.6 = GTP cyclohydrolase I (GTPCH), 1.3 = 6-pyruvoyl-tetra-hydropterin synthase (PTPS), 1.4 = dihydropteridine reductase (DHPR), 1.5 = pterin-4a-carbinolamine dehydratase (PCD), 1.7 = sepiapterin reductase SR, carbonyl reductase (CR), aldose reductase (AR), dihydrofolate reductase (DHFR), aromatic amino acid decarboxylase (AADC), tyrosine hydroxylase (TH), tryptophan hydroxylase (TPH), nitric oxide synthase (NOS). Pathological metabolites used as specific markers in the differential diagnosis are marked in squares. n.e.=non-enzymatic... Fig. 1.1. Biosynthesis and regeneration of tetrahydrobiopterin including possible metabolic defects and catabolism of phenylalanine. l.l=phenylalanine-4-hydroxylase (PAH) 1.2/1.6 = GTP cyclohydrolase I (GTPCH), 1.3 = 6-pyruvoyl-tetra-hydropterin synthase (PTPS), 1.4 = dihydropteridine reductase (DHPR), 1.5 = pterin-4a-carbinolamine dehydratase (PCD), 1.7 = sepiapterin reductase SR, carbonyl reductase (CR), aldose reductase (AR), dihydrofolate reductase (DHFR), aromatic amino acid decarboxylase (AADC), tyrosine hydroxylase (TH), tryptophan hydroxylase (TPH), nitric oxide synthase (NOS). Pathological metabolites used as specific markers in the differential diagnosis are marked in squares. n.e.=non-enzymatic...

See other pages where Tetrahydrobiopterin aromatic amino acid hydroxylases is mentioned: [Pg.281]    [Pg.231]    [Pg.162]    [Pg.262]    [Pg.281]    [Pg.297]    [Pg.281]    [Pg.262]    [Pg.297]    [Pg.977]    [Pg.210]    [Pg.2]    [Pg.361]    [Pg.105]   


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6- -tetrahydrobiopterin

Amino acids hydroxylases

Amino aromatic

Aromatic amino acids

Aromatic hydroxylase

The Role of Tetrahydrobiopterin in Aromatic Amino Acid Hydroxylases

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