Evidence map›Paper›PMID 30287897›Full record

ArticleScientific reports2018

A multisubstrate reductase from Plantago major: structure-function in the short chain reductase superfamily.

Rachel Fellows, Christopher M Russo, Catarina S Silva, Soon Goo Lee, Joseph M Jez, John D Chisholm, Chloe Zubieta, Max H Nanao

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Applications of Ene-Reductases in the Synthesis of Flavors and Fragrances.Journal of agricultural and food chemistry · 2024
    Review
  8. Article
  9. Article
  10. Article
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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

8 authors at 4 institutions in 3 countries.

Rachel FellowsEuropean Synchrotron Radiation Facility, Structural Biology Group, 71 Avenue des Martyrs, F-38000, Grenoble, France.
Christopher M RussoDepartment of Chemistry, Syracuse University, Syracuse, NY, 13244, USA.
Catarina S SilvaEuropean Synchrotron Radiation Facility, Structural Biology Group, 71 Avenue des Martyrs, F-38000, Grenoble, France.
Soon Goo LeeDepartment of Biology, Washington University in St. Louis, One Brookings Drive, Campus Box 1137, St. Louis, MO, 63130, USA.
Joseph M JezDepartment of Biology, Washington University in St. Louis, One Brookings Drive, Campus Box 1137, St. Louis, MO, 63130, USA.
John D ChisholmDepartment of Chemistry, Syracuse University, Syracuse, NY, 13244, USA.ORCID http://orcid.org/0000-0001-9518-2393
Chloe ZubietaLaboratoire de Physiologie Cellulaire & Végétale, Univ. Grenoble Alpes, CNRS, CEA, INRA, BIG, Grenoble, USA. chloe.zubieta@cea.fr.ORCID http://orcid.org/0000-0003-4558-9333
Max H NanaoEuropean Synchrotron Radiation Facility, Structural Biology Group, 71 Avenue des Martyrs, F-38000, Grenoble, France. max.nanao@esrf.fr.
Centre National de la Recherche Scientifique · FREuropean Synchrotron Radiation Facility · FRSyracuse University · USWashington University in St. Louis · US

Funding

Agence Nationale de la Recherche (French National Research Agency) ANR-10-LABX-49-01
6 · The paper itself

Abstract

The short chain dehydrogenase/reductase superfamily (SDR) is a large family of NAD(P)H-dependent enzymes found in all kingdoms of life. SDRs are particularly well-represented in plants, playing diverse roles in both primary and secondary metabolism. In addition, some plant SDRs are also able to catalyse a reductive cyclisation reaction critical for the biosynthesis of the iridoid backbone that contains a fused 5 and 6-membered ring scaffold. Mining the EST database of Plantago major, a medicinal plant that makes iridoids, we identified a putative 5β-progesterone reductase gene, PmMOR (P. major multisubstrate oxido-reductase), that is 60% identical to the iridoid synthase gene from Catharanthus roseus. The PmMOR protein was recombinantly expressed and its enzymatic activity assayed against three putative substrates, 8-oxogeranial, citral and progesterone. The enzyme demonstrated promiscuous enzymatic activity and was able to not only reduce progesterone and citral, but also to catalyse the reductive cyclisation of 8-oxogeranial. The crystal structures of PmMOR wild type and PmMOR mutants in complex with NADP

Indexed as

Catalytic DomainCrystallography, X-RayDNA Mutational AnalysisFatty Acid SynthasesModels, MolecularMutagenesis, Site-DirectedNADH, NADPH OxidoreductasesPlantagoProtein ConformationRecombinant ProteinsSequence HomologySubstrate SpecificityFatty Acid SynthasesNADH, NADPH OxidoreductasesRecombinant Proteinsshort chain trans-2-enoyl-CoA reductase

Identifiers

PMID30287897
PMCPMC6172241
OpenAlexW2894442776

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.