Evidence map›Paper›PMID 12093726›Full record

ArticleThe EMBO journal2002

Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.

Olga Mayans, Andreas Ivens, L Johan Nissen, Kasper Kirschner, Matthias Wilmanns

Abstract readComparative Study
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Structure, mechanism and inhibition of anthranilate phosphoribosyltransferase.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  2. Article
  3. Crystal structures of anthranilate phosphoribosyltransferase from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Ancient origin of the tryptophan operon and the dynamics of evolutionary change.Microbiology and molecular biology reviews : MMBR · 2003
    Review
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

5 authors.

Olga MayansEMBL Hamburg Outstation c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
Andreas Ivens
L Johan Nissen
Kasper Kirschner
Matthias Wilmanns

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism.

Indexed as

Evolution, MolecularAmino Acid SequenceAnthranilate PhosphoribosyltransferaseArchaeal ProteinsBacterial ProteinsBinding SitesEscherichia coliEscherichia coli ProteinsGeobacillus stearothermophilusMagnesiumMolecular Sequence DataPentosyltransferasesProtein Structure, TertiaryPyrimidine PhosphorylasesSequence AlignmentSpecies SpecificityAnthranilate PhosphoribosyltransferaseArchaeal ProteinsBacterial ProteinsEscherichia coli ProteinsMagnesiumPentosyltransferasesPyrimidine PhosphorylasesThymidine PhosphorylaseTryptophan

Identifiers

PMID12093726
PMCPMC126076

What OpenQuestion holds

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Registered trials

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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.