6779-87-9

Basic information

• Product Name: 7,8-DIHYDRO-L-BIOPTERIN
• Synonyms: 7,8-dihydrobiopterin;7,8-DIHYDRO-L-BIOPTERIN;2-AMINO-6-(1R,2S-DIHYDROXYPROPYL)-7,8-DIHYDRO-4(1H)-PTERIDINONE;BH2;DIHYDROBIOPTERIN;2-Amino-6-(1,2-dihydroxy-propyl)-7,8-dihydro-3H-pteridin-4-one;2-amino-6-(1,2-dihydroxypropyl)-7,8-dihydro-1H-pteridin-4-one;4(1H)-pteridinone, 2-amino-6-(1,2-dihydroxypropyl)-7,8-dihydro-
• CAS NO: 6779-87-9
• Molecular Formula: C₉H₁₃N₅O₃
• Molecular Weight: 239.23
• Product Categories: All Inhibitors;Inhibitors;Neurochemicals;Amines;Bases & Related Reagents;Chiral Reagents;Heterocycles;Intermediates & Fine Chemicals;Nucleotides;Pharmaceuticals
• Mol File: 6779-87-9.mol
• Article Data: 3

Chemical Properties

• Melting Point: >300°C dec.
• Boiling Point: 470.8 °C at 760 mmHg
• Flash Point: 238.5 °C
• Appearance: /
• Density: 1.88
• Vapor Pressure: 7.66E-11mmHg at 25°C
• Refractive Index: 1.821
• Storage Temp.: −20°C
• Solubility: Aqueous Acid (Slightly, Sonicated), Aqueous Base (Slightly), DMSO (Slightly)
• PKA: 10.47±0.20(Predicted)
• Stability: Hygroscopic
• BRN: 536551
• CAS DataBase Reference: 7,8-DIHYDRO-L-BIOPTERIN(CAS DataBase Reference)
• NIST Chemistry Reference: 7,8-DIHYDRO-L-BIOPTERIN(6779-87-9)
• EPA Substance Registry System: 7,8-DIHYDRO-L-BIOPTERIN(6779-87-9)

Safety Data

• WGK Germany: 3
• F: 3-10
• Hazardous Substances Data: 6779-87-9(Hazardous Substances Data)

Usage

Description

BH2 is a precursor of BH4 synthesis. It is a noncompetitive inhibitor of GTP cyclohydrolase I, with a Ki of 14.4 μM.

Chemical Properties

Yellow Powder

Uses

Different sources of media describe the Uses of 6779-87-9 differently. You can refer to the following data:
1. An oxidation producct of tetrahydrobiopterin, a naturally occurring cofactor of the aromatic amino acid hydroxylase and is involved in the synthesis of tyrosine and the neurotransmitters dopamine and serotonin. It is a noncompetitive inhibitor of G
2. The reduced form of Biopterin. An oxidation product of tetrahydrobiopterin, a naturally occurring cofactor of the aromatic amino acid hydroxylase and is involved in the synthesis of tyrosine and the neurotransmitters dopamine and serotonin. It is a noncompetitive inhibitor of GTP cyclohydrolase I, with a Ki of 14.4 μM.
3. BH2 is a precursor of BH4 synthesis. It is a noncompetitive inhibitor of GTP cyclohydrolase I, with a Ki of 14.4 μM.

references

[1] shen r, alam a, zhang y. inhibition of gtp cyclohydrolase i by pterins[j]. biochimica et biophysica acta (bba)-general subjects, 1988, 965(1): 9-15.[2] sugiyama t, levy b d, michel t. tetrahydrobiopterin recycling, a key determinant of endothelial nitric-oxide synthase-dependent signaling pathways in cultured vascular endothelial cells[j]. journal of biological chemistry, 2009, 284(19): 12691-12700.

InChI:InChI=1/C9H13N5O3/c1-3(15)6(16)4-2-11-7-5(12-4)8(17)14-9(10)13-7/h3,6,15-16H,2H2,1H3,(H4,10,11,13,14,17)/t3-,6-/m0/s1

Upstream product

• 22150-76-1 biopterin 
• 79647-29-3 p-quinonoid (6R)-dihydrobiopterin 

Downstream Products

• 22150-76-1 biopterin 
• 712-30-1 6-formylpterin 
• 948-60-7 pterine-6-carboxylic acid 
• 1131-35-7 7,8-dihydroxanthopterin 
• 13214-44-3 6-formyl-7,8-dihydropterin 

Relevant articles and documents

Reductase-catalyzed tetrahydrobiopterin regeneration alleviates the anti-competitive inhibition of tyrosine hydroxylation by 7,8-dihydrobiopterin

l-Tyrosine hydroxylation by tyrosine hydroxylase is a significant reaction for preparing many nutraceutical and pharmaceutical chemicals. Two major challenges in constructing these pathways in bacteria are the improvement of hydroxylase catalytic efficiency and the production of cofactor tetrahydrobiopterin (BH4). In this study, we analyzed the evolutionary relationships and conserved protein sequences between tyrosine hydroxylases from different species by PhyML and MAFFT. Finally, we selected 7 tyrosine hydroxylases and 6 sepiapterin reductases. Subsequently, the function of different groups was identified by a combined whole-cell catalyst, and a series of novel tyrosine hydroxylase/sepiapterin reductase (TH/SPR) synthesis systems were screened including tyrosine hydroxylase (from Streptosporangium roseum DSM 43021 and Thermomonospora curvata DSM 43183) and sepiapterin reductase (from Photobacterium damselae, Chlorobaculum thiosulfatiphilum and Xenorhabdus poinarii), namely as SrTH/PdSPR, SrTH/CtSPR, SrTH/XpSPR and TcTH/PdSPR, which can synthesize l-Dopa by hydroxylating l-tyrosine in Bacillus licheniformis. Furthermore, we analyzed the characterization of SrTH by enzyme catalysis and demonstrated that 7,8-dihydrobiopterin (BH2) formed by BH4 autooxidation was an anticompetitive inhibitor on SrTH. Finally, pure dihydropteridine reductase from Escherichia coli (EcDHPR) was added to the solution, and l-Dopa could be continually synthesized after 3 h, which was improved by 86% at 6 h in the catalytic reaction by SrTH. This indicates that BH4 regeneration can alleviate the inhibition by BH2 during tyrosine hydroxylation. This study provides a good starting point and theoretical foundation for further modification to improve the catalytic efficiency of tyrosine hydroxylation by tyrosine hydroxylase.

Quinonoid Dihydrobiopterin, an Important Metabolic Intermediate of Biopterin Cofactor in the Aromatic Hydroxylation of Amino Acids

p-Quinonoid (6R)-dihydrobiopterin hydrochloride was synthesized from (6R)-5,6,7,8-tetrahydrobiopterin dihydrochloride by hydrogenperoxide in the presence of potassium iodide.Several characters of quinonoid dihydrobiopterin were examined.