Evidence map›Paper›PMID 23066817›Full record

ArticleBiochemistry2012

Pseudouridine monophosphate glycosidase: a new glycosidase mechanism.

Siyu Huang, Nilkamal Mahanta, Tadhg P Begley, Steven E Ealick

Abstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Integrated Chemoenzymatic Synthesis of the mRNA Vaccine Building Block NAngewandte Chemie (International ed. in English) · 2025
    Article
  2. Reinvestigation of theJournal of the American Chemical Society · 2025
    Article
  3. microPublication biology · 2025
    Article
  4. Article
  5. Review
  6. Article
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  8. Article
  9. Article
  10. Structure Characterization ofFrontiers in microbiology · 2022
    Article
  11. Article
  12. Article
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  16. Article
  17. 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

4 authors at 2 institutions in 1 country.

Siyu HuangDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.
Nilkamal Mahanta
Tadhg P Begley
Steven E Ealick
Cornell University · USTexas A&M University · US

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structural Biology of Purine and Pyrimidine Biosynthesis and MetabolismR01GM073220 · NIGMS · CORNELL UNIVERSITY ITHACA · PI EALICK, STEVEN E · 2005 to 2012
$2.4M
NCRR NIH HHS P41 RR001646NCRR NIH HHS RR01646NIGMS NIH HHS GM103403NIGMS NIH HHS GM73220NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM073220
6 · The paper itself

Abstract

Pseudouridine (Ψ), the most abundant modification in RNA, is synthesized in situ using Ψ synthase. Recently, a pathway for the degradation of Ψ was described [Preumont, A., Snoussi, K., Stroobant, V., Collet, J. F., and Van Schaftingen, E. (2008) J. Biol. Chem. 283, 25238-25246]. In this pathway, Ψ is first converted to Ψ 5'-monophosphate (ΨMP) by Ψ kinase and then ΨMP is degraded by ΨMP glycosidase to uracil and ribose 5-phosphate. ΨMP glycosidase is the first example of a mechanistically characterized enzyme that cleaves a C-C glycosidic bond. Here we report X-ray crystal structures of Escherichia coli ΨMP glycosidase and a complex of the K166A mutant with ΨMP. We also report the structures of a ring-opened ribose 5-phosphate adduct and a ring-opened ribose ΨMP adduct. These structures provide four snapshots along the reaction coordinate. The structural studies suggested that the reaction utilizes a Lys166 adduct during catalysis. Biochemical and mass spectrometry data further confirmed the existence of a lysine adduct. We used site-directed mutagenesis combined with kinetic analysis to identify roles for specific active site residues. Together, these data suggest that ΨMP glycosidase catalyzes the cleavage of the C-C glycosidic bond through a novel ribose ring-opening mechanism.

Indexed as

Catalytic DomainCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGlycoside HydrolasesKineticsLysineMolecular ConformationMutagenesis, Site-DirectedSubstrate SpecificityEscherichia coli ProteinsGlycoside HydrolasesLysinepseudouridine monophosphate glycosidase, E coli

Identifiers

PMID23066817
PMCPMC3526674
OpenAlexW1996296527

What OpenQuestion holds

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LicenceTDM
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.