Evidence map›Paper›PMID 29045784›Full record

ArticleBiochemistry2017

Metal Dependence of the Xylose Isomerase from Piromyces sp. E2 Explored by Activity Profiling and Protein Crystallography.

Misun Lee, Henriëtte J Rozeboom, Paul P de Waal, Rene M de Jong, Hanna M Dudek, Dick B Janssen

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Nucleation of glucose isomerase protein crystals in a nonclassical disguise: The role of crystalline precursors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Structure-based directed evolution improvesBiotechnology for biofuels · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Engineering of Pentose Transport inFrontiers in bioengineering and biotechnology · 2019
    Review
  13. Structural insight intoScientific reports · 2018
    Article
  14. 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

6 authors at 2 institutions in 1 country.

Misun LeeBiochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen , Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Henriëtte J RozeboomBiochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen , Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Paul P de WaalDSM Biotechnology Center , Alexander Fleminglaan 1, 2613 AX Delft, The Netherlands.
Rene M de JongDSM Biotechnology Center , Alexander Fleminglaan 1, 2613 AX Delft, The Netherlands.
Hanna M DudekBiochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen , Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Dick B JanssenBiochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen , Nijenborgh 4, 9747 AG Groningen, The Netherlands.ORCID 0000-0002-0834-2043
University of Groningen · NLDSM (Netherlands) · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xylose isomerase from Piromyces sp. E2 (PirXI) can be used to equip Saccharomyces cerevisiae with the capacity to ferment xylose to ethanol. The biochemical properties and structure of the enzyme have not been described even though its metal content, catalytic parameters, and expression level are critical for rapid xylose utilization. We have isolated the enzyme after high-level expression in Escherichia coli, analyzed the metal dependence of its catalytic properties, and determined 12 crystal structures in the presence of different metals, substrates, and substrate analogues. The activity assays revealed that various bivalent metals can activate PirXI for xylose isomerization. Among these metals, Mn

Indexed as

Aldose-Ketose IsomerasesBinding SitesCatalysisCrystallography, X-RayMetalsModels, MolecularPiromycesProtein ConformationXylitolXyloseAldose-Ketose IsomerasesMetalsXylitolXylosexylose isomerase

Identifiers

PMID29045784
PMCPMC5688467
OpenAlexW2765998021

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.