529-69-1 Usage
Uses
Used in Pharmaceutical Industry:
Isoxanthopterin is used as a biochemical marker for the diagnosis and monitoring of certain diseases. Its interaction with the enzyme isoxanthopterin deaminase helps in understanding the metabolic pathways and identifying potential therapeutic targets.
Used in Research and Development:
In the field of research, isoxanthopterin is utilized as a key compound for studying the mechanisms of enzyme-catalyzed reactions and the role of isoxanthopterin deaminase in various biological processes. This knowledge can contribute to the development of novel therapeutic strategies and drug candidates.
Used in Diagnostic Applications:
Isoxanthopterin can be employed as a diagnostic tool to measure the activity of isoxanthopterin deaminase in patients, which may be indicative of specific health conditions or genetic disorders. This information can aid in the early detection and treatment of these conditions.
Used in Enzyme Assays:
Isoxanthopterin is used as a substrate in enzyme assays to study the activity and specificity of isoxanthopterin deaminase. This application is crucial for understanding the enzyme's function and its potential role in disease pathology.
Used in Drug Design and Development:
The knowledge of isoxanthopterin's interaction with isoxanthopterin deaminase can be applied in the design and development of new drugs targeting this enzyme. This may lead to the creation of novel therapeutic agents for the treatment of various diseases and conditions.
Synthesis Reference(s)
Journal of the American Chemical Society, 75, p. 4450, 1953 DOI: 10.1021/ja01114a016
Biological Activity
isoxanthopterin interferes with rna and dna synthesis.isoxanthopterin, a natural intermediate in the pteridine pathway, plays critical roles in pigmentation and cell division.
in vitro
isoxanthopterin was identified as a pteridine of wide natural occurrence and was reported to exerts an inhibitory action on the synthesis of ribosomal rna, possibly soluble rna and on dna in developing eggs of the milkweed bug oncopeltus fasciatus. such effects were measured by partially incubating dechorionated eggs in a solution containing isoxanthopterin and radioactive uridine or thymidine, and then testing the incorporation of the isotope into ribosomal rna or dna. the detailed mechanism of this inhibition had been discussed, and the tentative conclusion was agreed that it was due to an interaction between the pteridine and the nucleic acid (most probably dna) [1].
in vivo
previous animal study showed that rats with inherited retinal dystrophy appeared to differ from healthy rats by an elevated isoxanthopterin excretion in urine. rcs rats responded to feeding of monapterin with an increase of isoxanthopterin excretion. this phenomenon supported the idea that the rcs rat had an increased xanthinoxidase activity compared with healthy rats [2].
Purification Methods
Purify it by repeated precipitation from alkaline solution with acid (preferably AcOH or formic acid), filter, wash well with H2O, then EtOH and dry at 100o. The purity is checked by paper chromatography [RF 0.15 (n-BuOH/AcOH/H2O, 4:1:1); 0.33 (3% aqueous NH4OH). [Goto et al. Arch Biochem Biophys 111 8 1965.] [For biochemistry see Blakley Biochemistry of Folic Acid and Related Pteridines North Holland Publ Co, Amsterdam 1969.] [Beilstein 26 III/IV 3999.]
references
[1] lagowski, j. m. and forrest, h.s. interaction in vitro between isoxanthopterin and dna. proceedings of the national academy of sciences of the united states of america 58(4), 1541-1547 (1967).[2] g. cremer-bartels, h. gerding, l. hanneken and k. krause. isoxanthopterin excretion of rats with inherited retinal dystrophy. pteridines vol. 2, 1990, pp. 103 -105.
Check Digit Verification of cas no
The CAS Registry Mumber 529-69-1 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 5,2 and 9 respectively; the second part has 2 digits, 6 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 529-69:
(5*5)+(4*2)+(3*9)+(2*6)+(1*9)=81
81 % 10 = 1
So 529-69-1 is a valid CAS Registry Number.
InChI:InChI=1/C6H5N5O2/c7-6-10-4-3(5(13)11-6)8-1-2(12)9-4/h1H,(H4,7,9,10,11,12,13)
529-69-1Relevant academic research and scientific papers
Regulation of xanthine oxidase activity by substrates at active sites via cooperative interactions between catalytic subunits: Implication to drug pharmacokinetics
Tai,Hwang
experimental part, p. 69 - 78 (2012/01/05)
Three xanthine oxidase substrates (i.e., xanthine, adenine, and 2-amino-4-hydroxypterin) show a "substrate inhibition" pattern (i.e., slower turnover rates at higher substrate concentrations), whereas another two substrates (i.e., xanthopterin and lumazine) show a "substrate activation" pattern (i.e., higher turnover rates at higher substrate concentrations). Binding of a 6-formylpterin at one of the two xanthine oxidase active sites slows down the turnover rate of xanthine at the adjacent active site from 17.0 s-1 to 10.5 s-1, and converts the V-[S] plot from "substrate inhibition" pattern to a classical Michaelis-Menten hyperbolic saturation pattern. In contrast, binding of xanthine at an active site accelerates the turnover rate of 6-formylpterin at the neighboring active site. The experimental results demonstrate that a substrate can regulate the activity of xanthine oxidase via binding at the active sites; or a xanthine oxidase catalytic subunit can simultaneously serve as a regulatory unit. Theoretical simulation based on the velocity equation derived from the extended Michaelis-Menten model shows that the substrate inhibition and the substrate activation behavior in the V-[S] plots could be obtained by introducing cooperative interactions between two catalytic subunits in homodimeric enzymes. The current work confirms that there exist very strong cooperative interactions between the two catalytic subunits of xanthine oxidase.
Enzymatic inhibition assay for fluorometric determination of allopurinol and oxipurinol in serum and urine
Neubert,Besenfelder,Koch
, p. 1857 - 1859 (2007/10/02)
An enzymatic inhibition assay for the xanthine oxidase (XOD) inhibitors allopurinol and oxipurinol is described. 2-Amino-4-hydroxypteridine is used as sensitive fluorogenic substrate, which is oxidized to highly fluorescent isoxanthopterin by XOD. Increasing concentrations of allopurinol (Ap) or oxipurinol (Ox) prevent conversion of 2-amino-4-hydroxypterdine to isoxanthopterin. Assay conditions of XOD-inhibition are different for Ap and Ox. In the presence of xanthine both Ap and Ox inhibit XOD to the same degree; absence of xanthine results in inactivation by Ap only. Thus rapid and convenient determination of Ap and Ox is possible without prior separation of the substances. The limit of detection is about 0.5 nmol/ml (50 μg/ml) in serum and 25 nmol/ml (2.5 μg/ml) in urine.
