Evidence map›Paper›PMID 11563694›Full record

ArticleJournal of protein chemistry2001

The effect of inorganic phosphate on the activity of bacterial ribokinase.

M C Maj, R S Gupta

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of protein chemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

7 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Cloning, purification, crystallization and preliminary crystallographic analysis of a ribokinase from Staphylococcus aureus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    Article
  6. Article
  7. Article
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

2 authors at 1 institution in 1 country.

M C MajDepartment of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
R S Gupta
McMaster University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribokinase and adenosine kinase are both members of the PfkB family of carbohydrate kinases. The activity of mammalian adenosine kinase was previously shown to be affected by pentavalent ions (PVI). We now present evidence that the catalytic activity of E. coli ribokinase is also affected by PVI, increasing both the velocity and affinity of the enzyme for D-ribose. The Km, for ribose decreased from 0.61 mM to 0.21, 0.25, and 0.33 mM in the presence of 20 mM phosphate, arsenate, and vanadate, respectively. The activity of ribokinase was stimulated in a hyperbolic fashion, with the maximum velocity increasing 23-fold, 13-fold, and 11-fold under the same conditions, respectively. Activity was also affected upon the addition of phosphoenolpyruvate, suggesting that phosphorylated metabolites could be involved in enzymatic control. The similar effect of PVI on distantly related enzymes suggests that a common mechanism for activity is shared among PfkB family members.

Indexed as

Adenosine KinaseAdenosine TriphosphateArsenatesEscherichia coliHydrogen-Ion ConcentrationIonsPhosphatesPhosphoenolpyruvatePhosphotransferases (Alcohol Group Acceptor)Recombinant ProteinsSubstrate SpecificityVanadatesAdenosine KinaseAdenosine TriphosphateArsenatesarsenic acidIonsPhosphatesPhosphoenolpyruvatePhosphotransferases (Alcohol Group Acceptor)Recombinant ProteinsribokinaseVanadates

Identifiers

PMID11563694
OpenAlexW1501431

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.