Evidence map›Paper›PMID 15703176›Full record

ArticleThe Journal of biological chemistry2005

31P NMR and genetic analysis establish hinT as the only Escherchia coli purine nucleoside phosphoramidase and as essential for growth under high salt conditions.

Tsui-Fen Chou, Pawel Bieganowski, Kara Shilinski, Jilin Cheng, Charles Brenner, Carston R Wagner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

25 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. The Many Faces of Histidine Triad Nucleotide Binding Protein 1 (HINT1).ACS pharmacology & translational science · 2023
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Anchimerically Activatable Antiviral ProTides.ACS medicinal chemistry letters · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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 2 institutions in 1 country.

Tsui-Fen ChouDepartment of Medicinal Chemistry, College of Pharmacy, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Pawel Bieganowski
Kara Shilinski
Jilin Cheng
Charles Brenner
Carston R Wagner
Dartmouth College · USUniversity of Minnesota · US

Funding

Mechanism of Dnmt1 Up-regulation by Fhit LossR01CA075954 · NCI · UNIVERSITY OF IOWA · PI BRENNER, CHARLES M · 1997 to 2012
$3.0M
CARCINOGEN-ACTIVATING TRANSACETYLASESR01CA055334 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HANNA, PATRICK E · 1993 to 2001
$367k
STUDIES ON CARCINOGEN-ACTIVATING TRANSACETYLASESR55CA055334 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HANNA, PATRICK E · 1991 to 1991
–
NCI NIH HHS CA075954NCI NIH HHS CA55334NCI NIH HHS R01 CA075954
6 · The paper itself

Abstract

Eukaryotic cells encode AMP-lysine (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester) 5'-phosphoramidate) hydrolases related to the rabbit histidine triad nucleotide-binding protein 1 (Hint1) sequence. Bacterial and archaeal cells have Hint homologs annotated in a variety of ways, but the enzymes have not been characterized, nor have phenotypes been described due to loss of enzymatic activity. We developed a quantitative (31)P NMR assay to determine whether Escherichia coli possesses an adenosine phosphoramidase activity. Indeed, soluble lysates prepared from wild-type laboratory E. coli exhibited activity on the model substrate adenosine 5'-monophosphoramidate (AMP-NH(2)). The E. coli Hint homolog, which had been comprehensively designated ycfF and is here named hinT, was cloned, overexpressed, purified, and characterized with respect to purine nucleoside phosphoramidate substrates. Bacterial hinT was several times more active than human or rabbit Hint1 on five model substrates. In addition, bacterial and mammalian enzymes preferred guanosine versus adenosine phosphoramidates as substrates. Analysis of the lysates from a constructed hinT knock-out strain of E. coli demonstrated that all of the cellular purine nucleoside phosphoramidase activity is due to hinT. Physiological analysis of this mutant revealed that the loss of hinT results in failure to grow in media containing 0.75 m KCl, 0.9 m NaCl, 0.5 m NaOAc, or 10 mm MnCl(2). Thus, cation-resistant bacterial cell growth may be dependent on the hydrolysis of adenylylated and/or guanylylated phosphoramidate substrates by hinT.

Indexed as

Adenosine MonophosphateAnimalsCell ProliferationEscherichia coliGuanosineGuanosine MonophosphateHumansHydrolasesHydrolysisLysineMagnetic Resonance SpectroscopyModels, ChemicalMutationPlasmidsProtein ConformationPurine NucleosidesAdenosine MonophosphateGuanosineGuanosine Monophosphatehistidine triad proteinHydrolasesLysinepurinePurine NucleosidesPurinesRecombinant ProteinsSalts

Identifiers

PMID15703176
PMCPMC2556068
OpenAlexW2166695812

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.