Phosphoribosyl pyrophosphate pentasodium

Names

[ Name ]:
Phosphoribosyl pyrophosphate pentasodium

[Synonym ]:
5-Phospho-a-d-ribosyl-diphosphate sodiuM salt
α-D-Ribofuranose, 1-O-[hydroxy(phosphonooxy)phosphinyl]-, 5-(dihydrogen phosphate), sodium salt (1:4)
5-PHOSPHO-D-RIBOSE 1-DIPHOSPHAT
P-RIB-PP
5-PHOSPHORYLRIBOSE 1-PYROPHOSPHATE SODIUM SALT
5-PHOSPHO-D-RIBOSE 1-DIPHOSPHATE SODIUM SALT
5-Phospho-D-ribose 1-diphosphate pentasodium salt
PRPP pentasodium salt
5-phosphorylribose 1-pyrophosphate*sodium
P-RIB-PP,PRPP SODIUM SALT

Biological Activity

[Description]:

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].

[Related Catalog]:

Research Areas >> Others

[Target]

Human Endogenous Metabolite

[In Vitro]

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].

[References]

[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.

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

Chemical & Physical Properties

[ Molecular Formula ]:
C₅H₈Na₅O₁₄P₃

[ Molecular Weight ]:
499.98

[ Exact Mass ]:
477.879608

[ PSA ]:
270.49000

[ Storage condition ]:
−20°C

[ Water Solubility ]:
H2O: 50 mg/mL, clear, colorless to very faintly yellow

Safety Information

[ Symbol ]:

GHS08

[ Signal Word ]:
Warning

[ Hazard Statements ]:
H371

[ Precautionary Statements ]:
P260

[ Personal Protective Equipment ]:
dust mask type N95 (US);Eyeshields;Faceshields;Gloves

[ Hazard Codes ]:
Xn: Harmful;

[ Risk Phrases ]:
20/21/22-68/20/21/22

[ Safety Phrases ]:
36/37

[ RIDADR ]:
NONH for all modes of transport

[ WGK Germany ]:
3

Articles

Relation between muscarinic receptor cationic current and internal calcium in guinea-pig jejunal smooth muscle cells.

J. Physiol. 441 , 477-99, (1991)

1. The action of carbachol, which activates muscarinic receptors, was studied in single patch-clamped cells where free internal calcium concentration in the cell (Cai2+) was estimated using the emissi...

Inhibitors of the bacterial cell wall biosynthesis enzyme MurD.

Bioorg. Med. Chem. Lett. 8 , 1643-8, (1998)

A series of transition-state analog inhibitors of the D-glutamic acid-adding enzyme (MurD) of bacterial peptidoglycan biosynthesis has been synthesized and evaluated for inhibition of the E. coli enzy...