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7-Biopterin Sale

(Synonyms: Primapterin, L-Primapterin) 目录号 : GC46735

A pterin

7-Biopterin Chemical Structure

Cas No.:2636-52-4

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500 μg
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产品描述

7-Biopterin is a 7-substituted pterin.1 It is formed by non-enzymatic rearrangement of 4a-hydroxy-tetrahydropterin in the absence of pterin-4a-carbinolamine dehydratase (PCD) in vitro and levels are elevated in the urine of hyperphenylalaninemia patients carrying heterozygous mutations in the PCBD gene encoding PCD.1,2

1.ThÖny, B., Neuheiser, F., Kierat, L., et al.Hyperphenylalaninemia with high levels of 7-biopterin is associated with mutations in the PCBD gene encoding the bifunctional protein pterin-4a-carbinolamine dehydratase and transcriptional coactivator (DCoH)Am. J. Hum. Genet.62(6)1302-1311(1998) 2.Curtius, H.C., Kuster, T., Matasovic, A., et al.Primapterin, anapterin, and 6-oxo-primapterin, three new 7-substituted pterins identified in a patient with hyperphenylalaninemiaBiochem. Biophys. Res. Commun.153(2)715-721(1988)

Chemical Properties

Cas No. 2636-52-4 SDF
别名 Primapterin, L-Primapterin
Canonical SMILES O=C1N=C(N)N=C2NC([C@@H](O)[C@@H](O)C)=CN=C21
分子式 C9H11N5O3 分子量 237.2
溶解度 aqueous acid: slightly soluble 储存条件 Store at -20°C
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1 mM 4.2159 mL 21.0793 mL 42.1585 mL
5 mM 0.8432 mL 4.2159 mL 8.4317 mL
10 mM 0.4216 mL 2.1079 mL 4.2159 mL
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Research Update

Tetrahydro-6-biopterin is associated with tetrahydro-7-biopterin in primary murine mast cells

FEBS Lett 1992 Jul 28;307(2):147-50.PMID:1644167DOI:10.1016/0014-5793(92)80755-6.

Murine bone marrow-derived mast cells proliferate in response to interleukin 3. In addition to 6-biopterin, 7-Biopterin was identified in these cells by HPLC analysis of iodine oxidized extracts and by alkaline permanganate oxidation to the 6- and 7-carboxylic acids. 7-Biopterin comprised 31.9 (+/- 7.7)% of the total biopterin. It was absent in cells which were grown with of L-p-chlorophenylalanine, an inhibitor of tryptophan 5-mono-oxygenase. Both 6- and 7-Biopterin were present in the cell as their tetrahydro forms. From these data we conclude that 7-Biopterin, in contrast to e.g. brain tissue, regularly occurs as a normal metabolite in primary mast cells and that it is generated during hydroxylation of tryptophan.

7-Substituted pterins. A new class of mammalian pteridines

J Biol Chem 1990 Mar 5;265(7):3923-30.PMID:2303485doi

Three novel pteridines have been isolated from the urine of patients with a new variant of 6-(L-erythro-1',2'-dihydroxypropyl)-5,6,7,8-tetrahydropterin (tetrahydrobiopterin) deficiency, showing hyperphenylalaninemia. From the results of high performance liquid chromatography, oxidative degradation, and gas chromatography-electron impact mass spectrometry, their structures were identified as 7-(D-erythro-1',2',3'-trihydroxypropyl)-pterin (7-neopterin), 7-(L-erythro-1',2'-dihydroxypropyl)-pterin (7-Biopterin), and 6-oxo-7-(L-erythro-1',2'-dihydroxypropyl)-pterin (6-oxo-7-biopterin). The ratio of biopterin to 7-Biopterin in the patients' urines was 1:1, and after oral loading with tetrahydrobiopterin, 7-Biopterin excretion rose parallel to biopterin. This finding suggests that 7-substituted pterins may be formed endogenously by a yet unknown isomerization reaction. The cause of hyperphenylalaninemia is still unclear. The activities of the enzymes involved in tetrahydrobiopterin biosynthesis and regeneration were found to be normal in the patients, and no effect of 7-Biopterin on these enzymes was observed in vitro. However, compared with the normal cofactor, tetrahydrobiopterin, the Km values of tetrahydro-7-biopterin for phenylalanine hydroxylase and dihydropteridine reductase are 20 and 5 times higher, respectively.

Conversion of 6-substituted tetrahydropterins to 7-isomers via phenylalanine hydroxylase-generated intermediates

Proc Natl Acad Sci U S A 1991 Jan 15;88(2):385-9.PMID:1988938DOI:10.1073/pnas.88.2.385.

A new variant form of hyperphenylalaninemia has recently been discovered in which the patients characteristically excrete 7-Biopterin in their urines in addition to the natural 6-biopterin (Curtius, H. Ch., Kuster, T., Matasovic, A., Blau, N. & Dhondt, J.-L. (1988) Biochem. Biophys. Res. Commun. 153, 715-721). This isomer had not been found previously in humans, and although its origin was not established, preliminary evidence suggested that it might be produced from 6-biopterin. We have now found that 7-Biopterin can be formed in vitro from (6R)-tetrahydrobiopterin during the hydroxylation of phenylalanine catalyzed by phenylalanine hydroxylase [L-phenylalanine, tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating), EC 1.14.16.1]. The resulting 7-Biopterin was unequivocally identified by the following criteria: preparative isolation and conversion to 7-hydroxymethylpterin following periodate oxidation and borohydride reduction, quantitative conversion to pterin-7-carboxylic acid after oxidation with permanganate, and liquid chromatography/thermospray mass spectrometry. Addition of 4a-carbinolamine dehydratase, an enzyme involved in the regeneration of tetrahydrobiopterin from the pterin carbinolamine intermediate (also called 4a-hydroxytetrahydrobiopterin) formed in the phenylalanine hydroxylase reaction, greatly decreased the amount of the 7-Biopterin formed. This result implies that the in vitro formation of 7-Biopterin occurs via the nonenzymatic rearrangement of the unstable substrate of the dehydratase, 4a-hydroxytetrahydrobiopterin, and suggests that this new variant of hyperphenylalaninemia may be caused by a lack of 4a-carbinolamine dehydratase activity. A mechanism for the rearrangement is proposed that predicts that other 6-substituted tetrahydropterin substrates of the aromatic amino acid hydroxylases could also give rise to rearranged products from an opening of the pyrazine ring of the corresponding 4a-hydroxytetrahydropterin intermediate.

Hyperphenylalaninemia with high levels of 7-Biopterin is associated with mutations in the PCBD gene encoding the bifunctional protein pterin-4a-carbinolamine dehydratase and transcriptional coactivator (DCoH)

Am J Hum Genet 1998 Jun;62(6):1302-11.PMID:9585615DOI:10.1086/301887.

Pterin-4a-carbinolamine dehydratase (PCD) is required for efficient tetrahydrobiopterin regeneration after phenylalanine hydroxylase activity. This catalytic function was proposed to be specifically defective in newborns with a mild form of hyperphenylalaninemia (HPA) and persistent high urinary levels of primapterin (7-Biopterin). A second regulatory task of the same protein is DCoH, a coactivation of transcription by hepatocyte nuclear factor 1alpha (HNF-1alpha), a function that is apparently not impaired in these HPA individuals. It has been shown elsewhere that the human PCD/DCoH bifunctional protein is encoded by a single 4-exon-containing gene, PCBD, located on chromosome 10q22. We have now examined the PCBD gene for mutations at the genomic level in six such HPA patients from four different families. By the use of new intron-specific primers, we detected, in all six patients, single, homozygous nucleotide alterations, in exon 4, that were inherited from their parents. These homozygous alterations predicted mutant PCD/DCoH with a single amino acid exchange, in two cases (alleles T78I), or premature stop codons, in the other four patients (alleles E86X and Q97X). Recombinant expression in Escherichia coli revealed that the mutant proteins-T78I, E86X, and Q97X-are almost entirely in the insoluble fraction, in contrast to wild type, which is expressed as a soluble protein. These data support the proposal that HPA in combination with urinary primapterin may be due to autosomal recessive inheritance of mutations in the PCBD gene specifically affecting the dehydratase activity.

Determination of six pterins in urine by LC-MS/MS

Bioanalysis 2012 Jul;4(14):1739-46.PMID:22877220DOI:10.4155/bio.12.131.

Background: The present work describes an analytical method for urinary pterins by LC-MS/MS, with emphasis on the separation of 6- and 7-positional isomers of bio- and neopterins. Results: Urine sample preparation consisted of oxidation by MnO(2), filtration and direct dilution in the mobile phase. The method was validated in urine spiked at five concentration levels with true triplicates of each level. Separation of the pterins, including the positional isomers, was achieved by employing a LUNA amino column. Six pterins were quantified (pterin, isoxanthopterin, 6-biopterin, 7-Biopterin, 6-neopterin, 7-neopterin) and a linear behavior was observed; LOD varied from 7 to 360 pg/ml and correlation coefficients above 0.98 were obtained for all pterins. In addition, pterin levels were evaluated in 41 urine samples of healthy subjects, in ten urine samples of patients with classical phenylketonuria (PKU) and in one with atypical PKU. Conclusion: The proposed method allowed to identify, separate and quantify six pterins in urine, using a simple and rapid sample preparation. The atypical PKU was unequivocally differentiated from the classical form, demonstrating that this method could be very useful for characterization and follow-up of diseases.