6863-06-5 Usage
General Description
2-amino-4-hydroxy-6-hydroxymethylpteridine pyrophosphate is a chemical compound that plays a crucial role in the biosynthesis of tetrahydrobiopterin, an important cofactor for various enzymes involved in neurotransmitter synthesis and nitric oxide production. 2-amino-4-hydroxy-6-hydroxymethylpteridine pyrophosphate is a derivative of pteridine and is formed through a series of enzymatic reactions in the body. It is involved in the conversion of GTP to 7,8-dihydroneopterin triphosphate, an essential step in the biosynthesis of tetrahydrobiopterin. Tetrahydrobiopterin is necessary for the proper functioning of enzymes such as phenylalanine hydroxylase, tyrosine hydroxylase, and nitric oxide synthase, and its deficiency can lead to various neurological and metabolic disorders. 2-amino-4-hydroxy-6-hydroxymethylpteridine pyrophosphate is therefore a vital chemical in the metabolic pathways that regulate neurotransmitter balance and nitric oxide production in the body.
Check Digit Verification of cas no
The CAS Registry Mumber 6863-06-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 6,8,6 and 3 respectively; the second part has 2 digits, 0 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 6863-06:
(6*6)+(5*8)+(4*6)+(3*3)+(2*0)+(1*6)=115
115 % 10 = 5
So 6863-06-5 is a valid CAS Registry Number.
InChI:InChI=1/C7H9N5O8P2/c8-7-11-5-4(6(13)12-7)10-3(1-9-5)2-19-22(17,18)20-21(14,15)16/h1H,2H2,(H,17,18)(H2,14,15,16)(H3,8,9,11,12,13)
6863-06-5Relevant articles and documents
Elucidation of the catalytic mechanism of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase using QM/MM calculations
Jongkon, Nathjanan,Gleeson, Duangkamol,Gleeson, M. Paul
, p. 6239 - 6249 (2018/09/10)
The folate pathway is a recognized intervention point for treating parasitic and bacterial infections in humans. However, the efficacy of treatments targeting dihydropteroate synthase (DHPS) and dihydrofolate reductase (DHFR) has reduced due to disease-related mutations. This has prompted interest in other enzyme targets on this clinically validated pathway, including 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK). A challenge in the design of molecules to target this enzyme is that the precise mechanism of the reaction and the role of the active site residues are not fully understood. In this study, we report the first theoretical analysis of the catalytic pathway of the natural substrate using hybrid quantum mechanical/molecular mechanical (QM/MM) methods. The reaction profiles associated with three proposed general bases have been investigated, as well as the profile for two mutant enzymes, namely R92A and R82A. We identified R92 as the general base in the wildtype reaction. The predicted barriers are in good agreement with the observed experimental kcat values obtained for wildtype and mutant proteins.
