Evidence map›Paper›PMID 28068311›Full record

ArticleNature chemical biology2017

Structural and functional insights into asymmetric enzymatic dehydration of alkenols.

Bettina M Nestl, Christopher Geinitz, Stephanie Popa, Sari Rizek, Robert J Haselbeck, Rosary Stephen, Michael A Noble, Max-Philipp Fischer, Erik C Ralph, Hoi Ting Hau and 7 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

8 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. ExploringMolecules (Basel, Switzerland) · 2019
    Article
  6. Asymmetric Enzymatic Hydration of Unactivated, Aliphatic Alkenes.Angewandte Chemie (International ed. in English) · 2019
    Article
  7. On the current role of hydratases in biocatalysis.Applied microbiology and biotechnology · 2018
    Review
  8. 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

17 authors at 3 institutions in 3 countries.

Bettina M NestlInstitute of Technical Biochemistry, Universitaet Stuttgart, Stuttgart, Germany.
Christopher GeinitzInstitute of Technical Biochemistry, Universitaet Stuttgart, Stuttgart, Germany.
Stephanie PopaYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, UK.
Sari RizekGenomatica, Inc., San Diego, California, USA.
Robert J HaselbeckGenomatica, Inc., San Diego, California, USA.
Rosary StephenGenomatica, Inc., San Diego, California, USA.
Michael A NobleGenomatica, Inc., San Diego, California, USA.
Max-Philipp FischerInstitute of Technical Biochemistry, Universitaet Stuttgart, Stuttgart, Germany.
Erik C RalphGenomatica, Inc., San Diego, California, USA.
Hoi Ting HauYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, UK.
Henry ManYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, UK.
Muhiadin OmarYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, UK.
Johan P TurkenburgYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, UK.ORCID 0000-0001-6992-6838
Stephen van DienGenomatica, Inc., San Diego, California, USA.
Stephanie J CullerGenomatica, Inc., San Diego, California, USA.
Gideon GroganYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, UK.
Bernhard HauerInstitute of Technical Biochemistry, Universitaet Stuttgart, Stuttgart, Germany.
Genomatica (United States) · USUniversity of York · GBUniversity of Stuttgart · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The asymmetric dehydration of alcohols is an important process for the direct synthesis of alkenes. We report the structure and substrate specificity of the bifunctional linalool dehydratase isomerase (LinD) from the bacterium Castellaniella defragrans that catalyzes in nature the hydration of β-myrcene to linalool and the subsequent isomerization to geraniol. Enzymatic kinetic resolutions of truncated and elongated aromatic and aliphatic tertiary alcohols (C5-C15) that contain a specific signature motif demonstrate the broad substrate specificity of LinD. The three-dimensional structure of LinD from Castellaniella defragrans revealed a pentamer with active sites at the protomer interfaces. Furthermore, the structure of LinD in complex with the product geraniol provides initial mechanistic insights into this bifunctional enzyme. Site-directed mutagenesis confirmed active site amino acid residues essential for its dehydration and isomerization activity. These structural and mechanistic insights facilitate the development of hydrating catalysts, enriching the toolbox for novel bond-forming biocatalysis.

Indexed as

AlcoholsBiocatalysisDehydrationHydro-LyasesMolecular StructureAlcoholsHydro-Lyaseslinalool dehydratase-isomerase, Castellaniella defragrans

Identifiers

PMID28068311
OpenAlexW2570412779

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.