Evidence map›Paper›PMID 10082381›Full record

ArticleProtein science : a publication of the Protein Society1998

A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases.

M Y Galperin, A Bairoch, E V Koonin

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
6.0field-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

60 citing papers in PubMed, 157 citations in OpenAlex.

  1. Article
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  4. Role ofMicroorganisms · 2023
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  13. Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.Advances in protein chemistry and structural biology · 2017
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Modeling catalytic promiscuity in the alkaline phosphatase superfamily.Physical chemistry chemical physics : PCCP · 2013
    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

3 authors at 2 institutions in 2 countries.

M Y GalperinNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894, USA. galperin@ncbi.nlm.nih.gov
A Bairoch
E V Koonin
National Institutes of Health · USHES-SO Genève · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sequence analysis of the probable archaeal phosphoglycerate mutase resulted in the identification of a superfamily of metalloenzymes with similar metal-binding sites and predicted conserved structural fold. This superfamily unites alkaline phosphatase, N-acetylgalactosamine-4-sulfatase, and cerebroside sulfatase, enzymes with known three-dimensional structures, with phosphopentomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglycerol transferase, phosphonate monoesterase, streptomycin-6-phosphate phosphatase, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1, and several closely related sulfatases. In addition to the metal-binding motifs, all these enzymes contain a set of conserved amino acid residues that are likely to be required for the enzymatic activity. Mutational changes in the vicinity of these residues in several sulfatases cause mucopolysaccharidosis (Hunter, Maroteaux-Lamy, Morquio, and Sanfilippo syndromes) and metachromatic leucodystrophy.

Indexed as

Alkaline PhosphataseAmino Acid SequenceComputer SimulationDatabases, FactualHumansHydrogen-Ion ConcentrationMetalloendopeptidasesModels, MolecularMolecular Sequence DataPhosphoglycerate MutasePhosphotransferasesPhylogenySequence Homology, Amino AcidSulfatasesAlkaline PhosphataseMetalloendopeptidasesPhosphoglycerate MutasephosphopentomutasePhosphotransferasesSulfatases

Identifiers

PMID10082381
PMCPMC2144072
OpenAlexW2060576889

What OpenQuestion holds

Texttitle and abstract
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.