Human Metabolome Database: Showing metabocard for Phosphoribosyl pyrophosphate (HMDB0000280)

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Identification Taxonomy Ontology Physical properties Spectra Biological properties Concentrations Links References enzymes (11) Show 11 proteins XML

enzymes (11) Show 11 proteins

Record Information

Version

4.0

Status

Detected and Quantified

Creation Date

2005-11-16 15:48:42 UTC

Update Date

2020-03-12 18:26:04 UTC

HMDB ID

HMDB0000280

Secondary Accession Numbers

HMDB00280

Metabolite Identification

Common Name

Phosphoribosyl pyrophosphate

Description

Phosphoribosyl pyrophosphate, also known as PRPP or PRib-PP, belongs to the class of organic compounds known as pentose phosphates. These are carbohydrate derivatives containing a pentose substituted by one or more phosphate groups. Phosphoribosyl pyrophosphate is an extremely weak basic (essentially neutral) compound (based on its pKa). Phosphoribosyl pyrophosphate exists in all living species, ranging from bacteria to humans. Within humans, phosphoribosyl pyrophosphate participates in a number of enzymatic reactions. In particular, guanine and phosphoribosyl pyrophosphate can be biosynthesized from guanosine monophosphate through its interaction with the enzyme adenine phosphoribosyltransferase. In addition, guanine and phosphoribosyl pyrophosphate can be biosynthesized from guanosine monophosphate; which is catalyzed by the enzyme hypoxanthine-guanine phosphoribosyltransferase. In humans, phosphoribosyl pyrophosphate is involved in adenosine deaminase deficiency. Phosphoribosyl pyrophosphate is a pentosephosphate and it is the key substance in the biosynthesis of histidine, tryptophan, and purine and pyrimidine nucleotides. It is formed from ribose 5-phosphate by the enzyme ribose-phosphate diphosphokinase. It plays a role in transferring phosphate groups in several reactions.

Structure

MOL SDF PDB SMILES InChI

Synonyms

Value	Source
5-Phospho-alpha-D-ribose 1-diphosphate	ChEBI
5-Phosphoribosyl 1-pyrophosphate	ChEBI
5-Phosphoribosyl diphosphate	ChEBI
alpha-D-Ribofuranose 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)	ChEBI
alpha-Phosphoribosylpyrophosphoric acid	ChEBI
Phosphoribosylpyrophosphate	ChEBI
PRib-PP	ChEBI
PRPP	ChEBI
5-Phospho-a-D-ribose 1-diphosphate	Generator
5-Phospho-a-D-ribose 1-diphosphoric acid	Generator
5-Phospho-alpha-D-ribose 1-diphosphoric acid	Generator
5-Phospho-α-D-ribose 1-diphosphate	Generator
5-Phospho-α-D-ribose 1-diphosphoric acid	Generator
Phosphoribosyl pyrophosphoric acid	Generator
5-Phosphoribosyl 1-pyrophosphoric acid	Generator
5-Phosphoribosyl diphosphoric acid	Generator
a-D-Ribofuranose 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)	Generator
a-D-Ribofuranose 5-(dihydrogen phosphoric acid) 1-(trihydrogen diphosphoric acid)	Generator
alpha-D-Ribofuranose 5-(dihydrogen phosphoric acid) 1-(trihydrogen diphosphoric acid)	Generator
α-D-Ribofuranose 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)	Generator
α-D-Ribofuranose 5-(dihydrogen phosphoric acid) 1-(trihydrogen diphosphoric acid)	Generator
a-Phosphoribosylpyrophosphate	Generator
a-Phosphoribosylpyrophosphoric acid	Generator
alpha-Phosphoribosylpyrophosphate	Generator
α-Phosphoribosylpyrophosphate	Generator
α-Phosphoribosylpyrophosphoric acid	Generator
Phosphoribosylpyrophosphoric acid	Generator
5-Phospho-a-D-ribose-1-diphosphate	HMDB
5-Phospho-a-D-ribosyl pyrophosphate	HMDB
5-Phospho-alpha-D-ribose-1-diphosphate	HMDB
5-Phospho-alpha-D-ribosyl pyrophosphate	HMDB
5-Phosphoribose 1-pyrophosphate	HMDB
5-Phosphoribosyl 1-diphosphate	HMDB
5-Phosphoribosyl a-1-pyrophosphate	HMDB
5-Phosphoribosyl-1-pyrophosphate	HMDB
5-Phosphorylribose 1-a-diphosphate	HMDB
5-Phosphorylribose 1-alpha-diphosphate	HMDB
5-Phosphorylribose 1-pyrophosphate	HMDB
5-Phosphorylribosyl 1-pyrophosphate	HMDB
a-D-5-(Dihydrogen phosphate) 1-(trihydrogen pyrophosphate) ribofuranose	HMDB
a-D-5-Phosphoribosyl 1-pyrophosphate	HMDB
a-D-Ribofuranose 5-phosphate 1-pyrophosphate	HMDB
a-D-Ribofuranose, 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)	HMDB
alpha-D-5-(Dihydrogen phosphate) 1-(trihydrogen pyrophosphate) ribofuranose	HMDB
alpha-D-5-Phosphoribosyl 1-pyrophosphate	HMDB
alpha-D-Ribofuranose 5-phosphate 1-pyrophosphate	HMDB
alpha-D-Ribofuranose, 5-(dihydrogen phosphate) 1-(trihydrogen diphosphate)	HMDB
Phosphoribosyl-1-pyrophosphate	HMDB
Phosphoribosyl-pyrophosphate	HMDB
Phosphoribosylpyrophosphorate	HMDB
PP-Ribose-P	HMDB
Pyrophosphate, phosphoribosyl	MeSH, HMDB
5-Phospho-α-D-ribose-1-diphosphate	HMDB
5-Phospho-α-D-ribosyl pyrophosphate	HMDB
5-Phosphoribosyl alpha-1-pyrophosphate	HMDB
5-Phosphoribosyl pyrophosphate	HMDB
5-Phosphoribosyl α-1-pyrophosphate	HMDB
5-Phosphorylribose 1-α-diphosphate	HMDB
Phosphoribosyl pyrophosphate	HMDB
α-D-5-Phosphoribosyl 1-pyrophosphate	HMDB

Chemical Formula

C₅H₁₃O₁₄P₃

Average Molecular Weight

390.0696

Monoisotopic Molecular Weight

389.95181466

IUPAC Name

[({[(2R,3R,4S,5R)-3,4-dihydroxy-5-[(phosphonooxy)methyl]oxolan-2-yl]oxy}(hydroxy)phosphoryl)oxy]phosphonic acid

Traditional Name

phosphoribosylpyrophosphate

CAS Registry Number

7540-64-9

SMILES

O[C@H]1[C@@H](O)[C@@H](OP(O)(=O)OP(O)(O)=O)O[C@@H]1COP(O)(O)=O

InChI Identifier

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

InChI Key

PQGCEDQWHSBAJP-TXICZTDVSA-N

Chemical Taxonomy

Description

belongs to the class of organic compounds known as pentose phosphates. These are carbohydrate derivatives containing a pentose substituted by one or more phosphate groups.

Kingdom

Organic compounds

Super Class

Organic oxygen compounds

Class

Organooxygen compounds

Sub Class

Carbohydrates and carbohydrate conjugates

Direct Parent

Pentose phosphates

Alternative Parents

Substituents

Pentose phosphate
Pentose-5-phosphate
Monosaccharide phosphate
Organic pyrophosphate
Monoalkyl phosphate
Organic phosphoric acid derivative
Phosphoric acid ester
Alkyl phosphate
Tetrahydrofuran
1,2-diol
Secondary alcohol
Organoheterocyclic compound
Oxacycle
Alcohol
Hydrocarbon derivative
Organic oxide
Aliphatic heteromonocyclic compound

Molecular Framework

Aliphatic heteromonocyclic compounds

External Descriptors

5-O-phosphono-D-ribofuranosyl diphosphate (CHEBI:17111 )

Ontology

Disposition

Source:

Endogenous

Biological location:

Cell and elements:

Cell:

Fibroblast

Biofluid and excreta:

Blood

Subcellular:

Cytoplasm

Process

Naturally occurring process:

Biological process:

Biochemical pathway:

Role

Industrial application:

Pharmaceutical industry:

Pharmaceutical

Physical Properties

State

Solid

Experimental Properties

Property	Value	Reference
Melting Point	Not Available	Not Available
Boiling Point	Not Available	Not Available
Water Solubility	Not Available	Not Available
LogP	Not Available	Not Available

Predicted Properties

Property	Value	Source
Water Solubility	11.6 g/L	ALOGPS
logP	-0.74	ALOGPS
logP	-3	ChemAxon
logS	-1.5	ALOGPS
pKa (Strongest Acidic)	1.09	ChemAxon
pKa (Strongest Basic)	-3.7	ChemAxon
Physiological Charge	-4	ChemAxon
Hydrogen Acceptor Count	11	ChemAxon
Hydrogen Donor Count	7	ChemAxon
Polar Surface Area	229.74 Å²	ChemAxon
Rotatable Bond Count	7	ChemAxon
Refractivity	62.58 m³·mol⁻¹	ChemAxon
Polarizability	27.46 Å³	ChemAxon
Number of Rings	1	ChemAxon
Bioavailability	No	ChemAxon
Rule of Five	No	ChemAxon
Ghose Filter	No	ChemAxon
Veber's Rule	No	ChemAxon
MDDR-like Rule	No	ChemAxon

Spectra

Spectrum Type	Description	Splash Key	View
Predicted GC-MS	Predicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positive	splash10-004j-7902000000-513a0a03122b76d768d9	Spectrum
Predicted GC-MS	Predicted GC-MS Spectrum - GC-MS (2 TMS) - 70eV, Positive	splash10-004i-6952010000-eac4b7259ac1081ff665	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Positive	splash10-01tc-2934000000-e0fcfd13254fd3781439	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Positive	splash10-03dm-6593000000-b295e74d43b0dc625e47	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Positive	splash10-01r2-7920000000-a021603f22f19c083511	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Negative	splash10-000i-0509000000-54231bd8f000ab2dd4a0	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Negative	splash10-004i-9301000000-447b996f7510c6ae354b	Spectrum
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Negative	splash10-004i-9000000000-54f70df2270a3e4f67d2	Spectrum

Biological Properties

Cellular Locations

Cytoplasm

Biospecimen Locations

Blood

Tissue Locations

Erythrocyte
Fibroblasts

Pathways

Name	SMPDB/Pathwhiz	KEGG
Pyrimidine Metabolism
Purine Metabolism
Pentose Phosphate Pathway
Glucose-6-phosphate dehydrogenase deficiency		Not Available
Ribose-5-phosphate isomerase deficiency		Not Available

Normal Concentrations

Biospecimen	Status	Value	Age	Sex	Condition	Reference	Details
Blood	Detected and Quantified	5.72 +/- 0.86 uM	Children (1-13 years old)	Both	Normal	Geigy Scientific ...	details
Blood	Detected and Quantified	4.9 +/- 2.1 uM	Adult (>18 years old)	Both	Normal	Geigy Scientific ...	details

Abnormal Concentrations

Not Available

Associated Disorders and Diseases

Disease References

None

Associated OMIM IDs

None

External Links

DrugBank ID

DB01632

Phenol Explorer Compound ID

Not Available

FoodDB ID

KNApSAcK ID

Chemspider ID

KEGG Compound ID

BioCyc ID

BiGG ID

Wikipedia Link

Phosphoribosyl pyrophosphate

METLIN ID

5274

PubChem Compound

7339

PDB ID

Not Available

ChEBI ID

17111

Food Biomarker Ontology

Not Available

VMH ID

PRPP

References

Synthesis Reference

Gross, Akiva; Abril, Obsidiana; Lewis, Jerome M.; Geresh, Shimona; Whitesides, George M. Practical synthesis of 5-phospho-D-ribosyl a-1-pyrophosphate (PRPP): enzymatic routes from ribose 5-phosphate or ribose. Journal of the American Chemical Society (1983), 105(25), 7428-35.

Material Safety Data Sheet (MSDS)

Not Available

General References

Snyder FF, Dyer C, Seegmiller JE, Goldblum RM, Mills GC, Schmalstieg FC: Substrate inhibition of adenosine phosphorylation in adenosine deaminase deficiency and adenosine-mediated inhibition of PP-ribose-P dependent nucleotide synthesis in hypoxanthine phosphoribosyltransferase deficient erythrocytes. J Inherit Metab Dis. 1988;11(2):174-83. [PubMed:2459496 ]
Gordon RB, Keough DT, Emmerson BT: HPRT-deficiency associated with normal PRPP concentration and APRT activity. J Inherit Metab Dis. 1987;10(1):82-8. [PubMed:2437388 ]
Nishida Y, Akaoka I, Nishizawa T, Maruki M, Maruki K: Synthesis and concentration of 5-phosphoribosyl-1-pyrophosphate in erythrocytes from patients with Down's syndrome. Ann Rheum Dis. 1977 Jun;36(3):261-3. [PubMed:141914 ]
Ghitis J, Schreiber C, Waxman S: Phosphate-induced phosphoribosylpyrophosphate elevations to assess deranged folate and purine nucleotide metabolism. Proc Soc Exp Biol Med. 1987 Oct;186(1):90-5. [PubMed:2442765 ]
Yamaoka T, Yano M, Kondo M, Sasaki H, Hino S, Katashima R, Moritani M, Itakura M: Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses. J Biol Chem. 2001 Jun 15;276(24):21285-91. Epub 2001 Apr 4. [PubMed:11290738 ]
Blinov MN, Kamyshentsev MV, Luganova IS, Filanovskaia LI, Filippova VN: [Phosphoribosyl pyrophosphate and its metabolic enzymes in the erythrocytes in certain forms of anemia]. Vopr Med Khim. 1976 Jul-Aug;22(4):456-62. [PubMed:194412 ]
Micheli V, Taddeo A: [Spectrophotometric assay of 5-phosphoribosyl-1-pyrophosphate synthetase (PRPP) in erythrocyte lysate (author's transl)]. Quad Sclavo Diagn. 1981 Jun;17(2):209-15. [PubMed:6267652 ]
Sakuma R, Nishina T, Yamanaka H, Kamatani N, Nishioka K, Maeda M, Tsuji A: Phosphoribosylpyrophosphate synthetase in human erythrocytes: assay and kinetic studies using high-performance liquid chromatography. Clin Chim Acta. 1991 Dec 16;203(2-3):143-52. [PubMed:1663846 ]
Zoref-Shani E, Feinstein S, Frishberg Y, Bromberg Y, Sperling O: Kelley-Seegmiller syndrome due to a unique variant of hypoxanthine-guanine phosphoribosyltransferase: reduced affinity for 5-phosphoribosyl-1-pyrophosphate manifested only at low, physiological substrate concentrations. Biochim Biophys Acta. 2000 Feb 21;1500(2):197-203. [PubMed:10657589 ]
Sperling O, Boer P, Brosh S, Elazar E, Szeinberg A, de Vries A: Normal activity of metabolic pathways involved in the formation and utilization of phosphoribosylpyrophosphate in erythrocytes of patients with primary metabolic gout. Nutr Metab. 1975;18(4):217-23. [PubMed:172821 ]
Gorbach ZV: [Determination of phosphoribosyl pyrophosphate in the erythrocytes]. Lab Delo. 1977;(12):724-5. [PubMed:75318 ]
Marcolongo R, Pompucci G, Micheli V: Familial distribution of increased erythrocyte PP-ribose-P levels. Adv Exp Med Biol. 1977;76A:280-6. [PubMed:193371 ]
Becker MA, Losman MJ, Itkin P, Simkin PA: Gout with superactive phosphoribosylpyrophosphate synthetase due to increased enzyme catalytic rate. J Lab Clin Med. 1982 Apr;99(4):495-511. [PubMed:6174658 ]
Tax WJ, Veerkamp JH: A simple and sensitive method for estimating the concentration and synthesis of 5-phosphoribosyl 1-pyrophosphate in red blood cells. Clin Chim Acta. 1977 Jul 15;78(2):209-16. [PubMed:195752 ]
MacDermot KD, Allsop J, Watts RW: The rate of purine synthesis de nova in blood mononuclear cells in vitro from patients with familial hyperuricaemic nephropathy. Clin Sci (Lond). 1984 Aug;67(2):249-58. [PubMed:6744792 ]
Emmerson BT, Gordon RB, Thompson L: Adenine phosphoribosyltransferase deficiency: its inheritance and occurrence in a female with gout and renal disease. Aust N Z J Med. 1975 Oct;5(5):440-6. [PubMed:1061547 ]
Zerez CR, Lachant NA, Tanaka KR: Decreased erythrocyte phosphoribosylpyrophosphate synthetase activity and impaired formation in thalassemia minor: a mechanism for decreased adenine nucleotide content. J Lab Clin Med. 1989 Jul;114(1):43-50. [PubMed:2544652 ]
Rylance HJ, Wallace RC, Nuki G: A method for the determination of 5-phosphoribosyl 1-pyrophosphate concentrations in erythrocytes using high-performance liquid chromatography. Anal Biochem. 1987 Feb 1;160(2):337-41. [PubMed:2437821 ]
Kane MA, Roth E, Raptis G, Schreiber C, Waxman S: Effect of intracellular folate concentration on the modulation of 5-fluorouracil cytotoxicity by the elevation of phosphoribosylpyrophosphate in cultured human KB cells. Cancer Res. 1987 Dec 15;47(24 Pt 1):6444-50. [PubMed:2445472 ]
Lachant NA, Zerez CR, Tanaka KR: Pyrimidine nucleotides impair phosphoribosylpyrophosphate (PRPP) synthetase subunit aggregation by sequestering magnesium. A mechanism for the decreased PRPP synthetase activity in hereditary erythrocyte pyrimidine 5'-nucleotidase deficiency. Biochim Biophys Acta. 1989 Jan 19;994(1):81-8. [PubMed:2535789 ]

Only showing the first 10 proteins. There are 11 proteins in total.

Show all enzymes and transporters

Enzymes

Enzyme Details

1. Amidophosphoribosyltransferase

General function:: Involved in amidophosphoribosyltransferase activity
Specific function:: Not Available
Gene Name:: PPAT
Uniprot ID:: Q06203
Molecular weight:: 57398.52

Reactions

5-Phosphoribosylamine + Pyrophosphate + L-Glutamic acid → L-Glutamine + Phosphoribosyl pyrophosphate + Water	details

Enzyme Details

2. Nicotinate-nucleotide pyrophosphorylase [carboxylating]

General function:: Involved in catalytic activity
Specific function:: Involved in the catabolism of quinolinic acid (QA).
Gene Name:: QPRT
Uniprot ID:: Q15274
Molecular weight:: 30815.28

Reactions

nicotinate beta-D-ribonucleotide + Pyrophosphate + CO(2) → Quinolinic acid + Phosphoribosyl pyrophosphate	details
nicotinate beta-D-ribonucleotide + Pyrophosphate + Carbon dioxide → Quinolinic acid + Phosphoribosyl pyrophosphate	details

Enzyme Details

3. Adenine phosphoribosyltransferase

General function:: Involved in adenine phosphoribosyltransferase activity
Specific function:: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Gene Name:: APRT
Uniprot ID:: P07741
Molecular weight:: 19607.535

Reactions

Adenosine monophosphate + Pyrophosphate → Adenine + Phosphoribosyl pyrophosphate	details
Guanosine monophosphate + Pyrophosphate → Guanine + Phosphoribosyl pyrophosphate	details
AICAR + Pyrophosphate → 5-Aminoimidazole-4-carboxamide + Phosphoribosyl pyrophosphate	details

Enzyme Details

4. Hypoxanthine-guanine phosphoribosyltransferase

General function:: Involved in hypoxanthine phosphoribosyltransferase activity
Specific function:: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.
Gene Name:: HPRT1
Uniprot ID:: P00492
Molecular weight:: 24579.155

Reactions

Inosinic acid + Pyrophosphate → Hypoxanthine + Phosphoribosyl pyrophosphate	details
Guanosine monophosphate + Pyrophosphate → Guanine + Phosphoribosyl pyrophosphate	details
Adenosine monophosphate + Pyrophosphate → Adenine + Phosphoribosyl pyrophosphate	details
Xanthylic acid + Pyrophosphate → Xanthine + Phosphoribosyl pyrophosphate	details
Mercaptopurine + Phosphoribosyl pyrophosphate → 6-Thioinosine-5'-monophosphate + Pyrophosphate	details
6-Methylmercaptopurine + Phosphoribosyl pyrophosphate → 6-Methylthiopurine 5'-monophosphate ribonucleotide + Pyrophosphate	details
Thioguanine + Phosphoribosyl pyrophosphate → 6-Thioguanosine monophosphate + Pyrophosphate	details

Enzyme Details

5. Ribose-phosphate pyrophosphokinase 3

General function:: Involved in magnesium ion binding
Specific function:: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Gene Name:: PRPS1L1
Uniprot ID:: P21108
Molecular weight:: 34838.915

Reactions

Adenosine triphosphate + D-Ribose 5-phosphate → Adenosine monophosphate + Phosphoribosyl pyrophosphate	details

Enzyme Details

6. Ribose-phosphate pyrophosphokinase 1

General function:: Involved in magnesium ion binding
Specific function:: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Gene Name:: PRPS1
Uniprot ID:: P60891
Molecular weight:: 12324.195

Reactions

Adenosine triphosphate + D-Ribose 5-phosphate → Adenosine monophosphate + Phosphoribosyl pyrophosphate	details

Enzyme Details

7. Ribose-phosphate pyrophosphokinase 2

General function:: Involved in magnesium ion binding
Specific function:: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Gene Name:: PRPS2
Uniprot ID:: P11908
Molecular weight:: 35054.06

Reactions

Adenosine triphosphate + D-Ribose 5-phosphate → Adenosine monophosphate + Phosphoribosyl pyrophosphate	details

Enzyme Details

8. Uridine 5'-monophosphate synthase

General function:: Involved in catalytic activity
Specific function:: Not Available
Gene Name:: UMPS
Uniprot ID:: P11172
Molecular weight:: 52221.075

Reactions

Orotidylic acid + Pyrophosphate → Orotic acid + Phosphoribosyl pyrophosphate	details
Fluorouracil + Phosphoribosyl pyrophosphate → 5-Fluorouridine monophosphate + Pyrophosphate	details

Enzyme Details

9. Nicotinamide phosphoribosyltransferase

General function:: Involved in nicotinate phosphoribosyltransferase activity
Specific function:: Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity).
Gene Name:: NAMPT
Uniprot ID:: P43490
Molecular weight:: 55520.8

Reactions

beta-nicotinamide D-ribonucleotide + Pyrophosphate → Niacinamide + Phosphoribosyl pyrophosphate	details

Enzyme Details

10. Nicotinate phosphoribosyltransferase

General function:: Involved in nicotinate phosphoribosyltransferase activity
Specific function:: Catalyzes the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). Essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells.
Gene Name:: NAPRT1
Uniprot ID:: Q6XQN6
Molecular weight:: 57577.575

Reactions

nicotinate beta-D-ribonucleotide + Pyrophosphate → Nicotinic acid + Phosphoribosyl pyrophosphate	details

Only showing the first 10 proteins. There are 11 proteins in total.

Show all enzymes and transporters

Showing metabocard for Phosphoribosyl pyrophosphate (HMDB0000280)

Structure for HMDB0000280 (Phosphoribosyl pyrophosphate)

Enzymes

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