Phosphoribosyl pyrophosphate pentasodium

For research use only. Not for therapeutic Use.

  • CAT Number: M008105
  • CAS Number: 108321-05-7
  • Molecular Formula: C5H8Na5O14P3
  • Molecular Weight: 499.98
  • Purity: ≥95%
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Phosphoribosyl pyrophosphate (PRPP) pentasodium is an important metabolite required in the biosynthesis of purine and pyrimidine nucleotides, the amino acids histidine and tryptophan, and the cofactors NAD and NADP[1].
Phosphoribosyl diphosphate (PRPP) pentasodium is an important intermediate in cellular metabolism. PRPP is synthesized by PRPP synthase, as follows: ribose 5-phosphate + ATP → PRPP + AMP. PRPP is ubiquitously found in living organisms and is used in substitution reactions with the formation of glycosidic bonds. PRPP is utilized in the biosynthesis of purine and pyrimidine nucleotides, the amino acids histidine and tryptophan, the cofactors NAD and tetrahydromethanopterin, arabinosyl monophosphodecaprenol, and certain aminoglycoside antibiotics[1].
Phosphoribosyl diphosphate (5-Phosphoribosyl-l-pyrophosphate) pentasodium, a substrate shared by adenine phosphoribosyltransferase and hypoxanthine-guanine phosphoribosyltransferase, accumulates in human erythrocytes lacking hypoxanthine-guanine phosphoribosyltransferase. 5-Phosphoribosyl-l-pyrophosphate added to purified adenine phosphoribosyltransferase stabilizes it against heat inactivation[2].


Catalog Number M008105
CAS Number 108321-05-7
Synonyms

pentasodium;[(2R,3S,4R,5R)-3,4-dihydroxy-5-[oxido(phosphonatooxy)phosphoryl]oxyoxolan-2-yl]methyl phosphate

Molecular Formula C5H8Na5O14P3
Purity ≥95%
InChI InChI=1S/C5H13O14P3.5Na/c6-3-2(1-16-20(8,9)10)17-5(4(3)7)18-22(14,15)19-21(11,12)13;;;;;/h2-7H,1H2,(H,14,15)(H2,8,9,10)(H2,11,12,13);;;;;/q;5*+1/p-5/t2-,3-,4-,5-;;;;;/m1...../s1
InChIKey UJNGSXHPBPBVKF-LVGJVSMDSA-I
SMILES C(C1C(C(C(O1)OP(=O)([O-])OP(=O)([O-])[O-])O)O)OP(=O)([O-])[O-].[Na+].[Na+].[Na+].[Na+].[Na+]
Reference

[1]. Schneiter R, et al. The importance of the five phosphoribosyl-pyrophosphate synthetase (Prs) gene products of Saccharomyces cerevisiae in the maintenance of cell integrity and the subcellular localization of Prs1p. Microbiology (Reading). 2000;146 Pt 12:3269-3278.
 [Content Brief]

[2]. Greene ML, et al. Substrate stabilization: genetically controlled reciprocal relationship of two human enzymes. Science. 1970;167(3919):887-889.
 [Content Brief]

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