Evidence map›Paper›PMID 27252380›Full record

ArticleThe Journal of biological chemistry2016

1,2-Propanediol Dehydration in Roseburia inulinivorans: STRUCTURAL BASIS FOR SUBSTRATE AND ENANTIOMER SELECTIVITY.

Joseph W LaMattina, Nicholas D Keul, Pierre Reitzer, Suraj Kapoor, Felipe Galzerani, Daniel J Koch, Iuri E Gouvea, William N Lanzilotta

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Advances in the World of Bacterial Microcompartments.Trends in biochemical sciences · 2021
    Review
  7. Review
  8. Article
  9. Review
  10. A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacteriumProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Review
  12. Bacterial microcompartments.Nature reviews. Microbiology · 2018
    Review
  13. New tricks for the glycyl radical enzyme family.Critical reviews in biochemistry and molecular biology · 2017
    Review
  14. Article
  15. 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

8 authors at 1 institution in 1 country.

Joseph W LaMattinaFrom the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602 and.
Nicholas D KeulFrom the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602 and.
Pierre ReitzerFrom the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602 and.
Suraj KapoorFrom the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602 and.
Felipe GalzeraniBRASKEM S.A., Rua Lemos Moonteiro, 120 Edifício Odebrecht São Paulo, Butantã 05501-050-São Paulo, SP Brasil.
Daniel J KochBRASKEM S.A., Rua Lemos Moonteiro, 120 Edifício Odebrecht São Paulo, Butantã 05501-050-São Paulo, SP Brasil.
Iuri E GouveaBRASKEM S.A., Rua Lemos Moonteiro, 120 Edifício Odebrecht São Paulo, Butantã 05501-050-São Paulo, SP Brasil.
William N LanzilottaFrom the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602 and wlanzilo@bmb.uga.edu.
University of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycyl radical enzymes (GREs) represent a diverse superfamily of enzymes that utilize a radical mechanism to catalyze difficult, but often essential, chemical reactions. In this work we present the first biochemical and structural data for a GRE-type diol dehydratase from the organism Roseburia inulinivorans (RiDD). Despite high sequence (48% identity) and structural similarity to the GRE-type glycerol dehydratase from Clostridium butyricum, we demonstrate that the RiDD is in fact a diol dehydratase. In addition, the RiDD will utilize both (S)-1,2-propanediol and (R)-1,2-propanediol as a substrate, with an observed preference for the S enantiomer. Based on the new structural information we developed and successfully tested a hypothesis that explains the functional differences we observe.

Indexed as

Bacterial ProteinsEubacterialesPropanediol DehydratasePropylene GlycolSubstrate SpecificityBacterial ProteinsPropanediol DehydratasePropylene Glycolchemical biologydiol dehydrataseenzyme structureglycerol dehydrataseglycyl radical enzymeintestinal metabolismmetabolic engineeringradicalradical dehydration

Identifiers

PMID27252380
PMCPMC4957038
OpenAlexW2412909664

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.