Evidence map›Paper›PMID 28031352›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2017

Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.

Bjarne Hove-Jensen, Kasper R Andersen, Mogens Kilstrup, Jan Martinussen, Robert L Switzer, Martin Willemoës

Open access · bronzeAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.

0numbers the graph read from it
0cells of the map it votes in
151citing papers in PubMed
6.8field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

151 citing papers in PubMed, 252 citations in OpenAlex.

  1. Systems metabolic engineering of a plasmid-freeSynthetic and systems biotechnology · 2027
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Divergent evolution of the PRPS enzymes across the tree of life.bioRxiv : the preprint server for biology · 2026
    Article
  13. International journal of stem cells · 2026
    Article
  14. Review
  15. Article
  16. High-Level Production of NMN inMicroorganisms · 2026
    Article
  17. Review
  18. Review
  19. Article
  20. Article

91 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Bjarne Hove-JensenDTU Systems Biology, Technical University of Denmark, Kongens Lyngby, Denmark hove@mbg.au.dk.ORCID 0000-0001-8119-9477
Kasper R AndersenDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Mogens KilstrupDTU Systems Biology, Technical University of Denmark, Kongens Lyngby, Denmark.
Jan MartinussenDTU Systems Biology, Technical University of Denmark, Kongens Lyngby, Denmark.
Robert L SwitzerDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Illinois, USA.
Martin WillemoësDepartment of Biology, University of Copenhagen, Copenhagen, Denmark.
Aarhus University · DKTechnical University of Denmark · DKUniversity of Copenhagen · DKUniversity of Illinois Urbana-Champaign · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphoribosyl diphosphate (PRPP) 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. The participation of PRPP in each of these metabolic pathways is reviewed. Central to the metabolism of PRPP is PRPP synthase, which has been studied from all kingdoms of life by classical mechanistic procedures. The results of these analyses are unified with recent progress in molecular enzymology and the elucidation of the three-dimensional structures of PRPP synthases from eubacteria, archaea, and humans. The structures and mechanisms of catalysis of the five diphosphoryltransferases are compared, as are those of selected enzymes of diphosphoryl transfer, phosphoryl transfer, and nucleotidyl transfer reactions. PRPP is used as a substrate by a large number phosphoribosyltransferases. The protein structures and reaction mechanisms of these phosphoribosyltransferases vary and demonstrate the versatility of PRPP as an intermediate in cellular physiology. PRPP synthases appear to have originated from a phosphoribosyltransferase during evolution, as demonstrated by phylogenetic analysis. PRPP, furthermore, is an effector molecule of purine and pyrimidine nucleotide biosynthesis, either by binding to PurR or PyrR regulatory proteins or as an allosteric activator of carbamoylphosphate synthetase. Genetic analyses have disclosed a number of mutants altered in the PRPP synthase-specifying genes in humans as well as bacterial species.

Indexed as

Amino Acid SequenceArchaeaBacteriaEnergy MetabolismFungiHumansPeptide SynthasesPhosphoribosyl PyrophosphatePhosphotransferases (Phosphate Group Acceptor)Protein Structure, SecondaryRibosemonophosphateslipoate-protein ligasePeptide SynthasesPhosphoribosyl PyrophosphatePhosphotransferases (Phosphate Group Acceptor)ribose-5-phosphateRibosemonophosphatesamino acid metabolismdiphosphoryl transfernucleotide metabolismphosphoribosyl pyrophosphateprotein structure-function

Identifiers

PMID28031352
PMCPMC5312242
OpenAlexW2565616863

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.