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| 5-O-phosphono-α-D-ribofuranosyl diphosphate |
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| CHEBI:17111 |
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| 5-O-phosphono-alpha-D-ribofuranosyl diphosphate |
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| A derivative of α-D-ribose having a phosphate group at the 5-position and a diphosphate at the 1-position. |
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This entity has been manually annotated by the ChEBI Team.
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CHEBI:12160, CHEBI:12159, CHEBI:2121, CHEBI:45139, CHEBI:20625
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| ZINC000008215630 |
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Molfile
XML
SDF
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more structures >>
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call loadScript javascripts\jsmol\core\package.js call loadScript javascripts\jsmol\core\core.z.js -- required by ClazzNode call loadScript javascripts\jsmol\J\awtjs2d\WebOutputChannel.js
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InChI=1S/C5H13O14P3/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)/t2-,3-,4-,5-/m1/s1 |
| PQGCEDQWHSBAJP-TXICZTDVSA-N |
| O[C@H]1[C@@H](O)[C@H](O[C@@H]1COP(O)(O)=O)OP(O)(=O)OP(O)(O)=O |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Arabidopsis thaliana
(NCBI:txid3702)
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See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Homo sapiens
(NCBI:txid9606)
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See:
PubMed
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Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
plant metabolite
Any eukaryotic metabolite produced during a metabolic reaction in plants, the kingdom that include flowering plants, conifers and other gymnosperms.
mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
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View more via ChEBI Ontology
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Outgoing
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5-O-phosphono-α-D-ribofuranosyl diphosphate
(CHEBI:17111)
has functional parent
α-D-ribose
(CHEBI:45506)
5-O-phosphono-α-D-ribofuranosyl diphosphate
(CHEBI:17111)
has role
Escherichia coli metabolite
(CHEBI:76971)
5-O-phosphono-α-D-ribofuranosyl diphosphate
(CHEBI:17111)
has role
human metabolite
(CHEBI:77746)
5-O-phosphono-α-D-ribofuranosyl diphosphate
(CHEBI:17111)
has role
mouse metabolite
(CHEBI:75771)
5-O-phosphono-α-D-ribofuranosyl diphosphate
(CHEBI:17111)
has role
plant metabolite
(CHEBI:76924)
5-O-phosphono-α-D-ribofuranosyl diphosphate
(CHEBI:17111)
is a
5-O-phosphono-D-ribofuranosyl diphosphate
(CHEBI:48956)
5-O-phosphono-α-D-ribofuranosyl diphosphate
(CHEBI:17111)
is conjugate acid of
5-O-phosphonato-α-D-ribofuranosyl diphosphate(5−)
(CHEBI:58017)
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Incoming
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5-O-phosphonato-α-D-ribofuranosyl diphosphate(5−)
(CHEBI:58017)
is conjugate base of
5-O-phosphono-α-D-ribofuranosyl diphosphate
(CHEBI:17111)
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5-O-phosphono-α-D-ribofuranose 1-(trihydrogen diphosphate)
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5-Phospho-alpha-D-ribose 1-diphosphate
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KEGG COMPOUND
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5-Phosphoribosyl 1-pyrophosphate
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KEGG COMPOUND
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5-Phosphoribosyl diphosphate
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KEGG COMPOUND
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α-D-ribofuranose 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)
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ChemIDplus
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ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC ACID
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PDBeChem
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phosphoribosyl pyrophosphate
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ChemIDplus
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phosphoribosylpyrophosphate
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ChEBI
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PRib-PP
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CBN
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PRPP
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KEGG COMPOUND
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60403
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Reaxys Registry Number
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Reaxys
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7540-64-9
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CAS Registry Number
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ChemIDplus
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Chen P, Li J, Ma J, Teng M, Li X (2013)
A small disturbance, but a serious disease: the possible mechanism of D52H-mutant of human PRS1 that causes gout.
IUBMB life 65, 518-525 [PubMed:23509005]
[show Abstract]
Phosphoribosyl pyrophosphate synthetase isoform 1 (PRS1) has an essential role in the de novo and salvage synthesis of human purine and pyrimidine nucleotides. The dysfunction of PRS1 will dramatically influence nucleotides' concentration in patient's body and lead to different kinds of disorders (such as hyperuricemia, gout and deafness). The D52H missense mutation of PRS1 will lead to a conspicuous phosphoribosyl pyrophosphate content elevation in the erythrocyte of patients and finally induce hyperuricemia and serious gout. In this study, the enzyme activity analysis indicated that D52H-mutant possessed similar catalytic activity to the wild-type PRS1, and the 2.27 Å resolution D52H-mutant crystal structure revealed that the stable interaction network surrounding the 52 position of PRS1 would be completely destroyed by the substitution of histidine. These interaction variations would further influence the conformation of ADP-binding pocket of D52H-mutant and reduced the inhibitor sensitivity of PRS1 in patient's body. | Fridman A, Saha A, Chan A, Casteel DE, Pilz RB, Boss GR (2013)
Cell cycle regulation of purine synthesis by phosphoribosyl pyrophosphate and inorganic phosphate.
The Biochemical journal 454, 91-99 [PubMed:23734909]
[show Abstract]
Cells must increase synthesis of purine nucleotides/deoxynucleotides before or during S-phase. We found that rates of purine synthesis via the de novo and salvage pathways increased 5.0- and 3.3-fold respectively, as cells progressed from mid-G1-phase to early S-phase. The increased purine synthesis could be attributed to a 3.2-fold increase in intracellular PRPP (5-phosphoribosyl-α-1-pyrophosphate), a rate-limiting substrate for de novo and salvage purine synthesis. PRPP can be produced by the oxidative and non-oxidative pentose phosphate pathways, and we found a 3.1-fold increase in flow through the non-oxidative pathway, with no change in oxidative pathway activity. Non-oxidative pentose phosphate pathway enzymes showed no change in activity, but PRPP synthetase is regulated by phosphate, and we found that phosphate uptake and total intracellular phosphate concentration increased significantly between mid-G1-phase and early S-phase. Over the same time period, PRPP synthetase activity increased 2.5-fold when assayed in the absence of added phosphate, making enzyme activity dependent on cellular phosphate at the time of extraction. We conclude that purine synthesis increases as cells progress from G1- to S-phase, and that the increase is from heightened PRPP synthetase activity due to increased intracellular phosphate. | Kunjara S, Greenbaum AL, Sochor M, Ali M, Flyvbjerg A, Grønbaek H, McLean P (2012)
Effects of long-acting somatostatin analogues on adrenal growth and phosphoribosyl pyrophosphate formation in experimental diabetes.
International journal of experimental pathology 93, 56-69 [PubMed:22264286]
[show Abstract]
Adrenal growth and increased adrenal function occur in experimental diabetes. Previously, we have shown that phosphoribosyl pyrophosphate (PRPP) and PRPP synthetase increased rapidly between 3 and 7 days after induction of diabetes with streptozotocin (STZ), with less marked changes in enzymes of the pentose phosphate pathway. The present study examines the earlier phase of 1-3 days following induction of diabetes, seeking to elucidate whether control of PRPP production is a result of diabetic hyperglycaemia, or to a more general re-ordering of hormonal factors. To investigate this question, the role of insulin and two different long-acting somatostatin analogues, Angiopeptin and Sandostatin, were used in a well-established animal model. PRPP was chosen specifically as a target for these studies in view of its central role in nucleotide formation and nicotinamide mononucleotide synthesis via Nampt which is the rate-limiting step in the synthesis of NAD and which has been shown to have multiple roles in cell signalling in addition to its known function in glycolysis and energy production. Treatment with the somatostatin analogues ab initio effectively abolished the adrenal growth, the increase in PRPP formation and the rise of PRPP synthetase activity in the first 7 days of diabetes, without having any significant effect on blood glucose values. This suggests that elevated glucose per se is not responsible for the diabetic adrenal hypertrophy and implies that growth factors/hormones, regulated by somatostatin analogues, play a significant role in adrenal growth processes. |
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