Evidence map›Paper›PMID 24096172›Full record

ReviewArchives of biochemistry and biophysics2014

Structure, mechanism, and dynamics of UDP-galactopyranose mutase.

John J Tanner, Leonardo Boechi, J Andrew McCammon, Pablo Sobrado

Open access · bronzeAbstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. The Glycan Structure ofMolecules (Basel, Switzerland) · 2020
    Review
  10. Galactofuranose-Related Enzymes: Challenges and Hopes.International journal of molecular sciences · 2020
    Review
  11. Biosynthesis of Galactan inAntibiotics (Basel, Switzerland) · 2020
    Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 4 institutions in 1 country.

John J TannerDepartments of Chemistry and Biochemistry, University of Missouri, Columbia, MO, United States. Electronic address: tannerjj@missouri.edu.
Leonardo BoechiDepartments of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, United States.
J Andrew McCammonDepartments of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, United States; Howard Hughes Medical Institute, Department of Pharmacology, University of California San Diego, La Jolla, CA, United States.
Pablo SobradoDepartment of Biochemistry, Virginia Tech, Blacksburg, VA, United States; Virginia Tech Center for Drug Discovery, Virginia Tech, Blacksburg, VA, United States. Electronic address: psobrado@vt.edu.
Howard Hughes Medical Institute · USUniversity of California, San Diego · USUniversity of Missouri · USVirginia Tech · US

Funding

Mechanistic and structural studies of eukaryotic UDP-galactopyranose mutasesR01GM094469 · NIGMS · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI SOBRADO, PABLO, TANNER, JOHN J · 2010 to 2019
$2.0M
Howard Hughes Medical InstituteNIGMS NIH HHS GM094469NIGMS NIH HHS R01 GM094469
6 · The paper itself

Abstract

The flavoenzyme UDP-galactopyranose mutase (UGM) is a key enzyme in galactofuranose biosynthesis. The enzyme catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose. Galactofuranose is absent in humans yet is an essential component of bacterial and fungal cell walls and a cell surface virulence factor in protozoan parasites. Thus, inhibition of galactofuranose biosynthesis is a valid strategy for developing new antimicrobials. UGM is an excellent target in this effort because the product of the UGM reaction represents the first appearance of galactofuranose in the biosynthetic pathway. The UGM reaction is redox neutral, which is atypical for flavoenzymes, motivating intense examination of the chemical mechanism and structural features that tune the flavin for its unique role in catalysis. These studies show that the flavin functions as nucleophile, forming a flavin-sugar adduct that facilitates galactose-ring opening and contraction. The 3-dimensional fold is novel and conserved among all UGMs, however the larger eukaryotic enzymes have additional secondary structure elements that lead to significant differences in quaternary structure, substrate conformation, and conformational flexibility. Here we present a comprehensive review of UGM three-dimensional structure, provide an update on recent developments in understanding the mechanism of the enzyme, and summarize computational studies of active site flexibility.

Indexed as

AnimalsBacteriaEnzyme ActivationFlavinsHumansIntramolecular TransferasesModels, MolecularProtein ConformationSubstrate SpecificityFlavinsIntramolecular TransferasesUDP-galactopyranose mutaseConformational changesFlavin-dependent reactionGalactofuranoseNeglected diseasesNon-redox reactionProtein dynamicsRedox-switchTuberculosis

Identifiers

PMID24096172
PMCPMC3946560
OpenAlexW2072296038

What OpenQuestion holds

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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.