Evidence map›Paper›PMID 29430657›Full record

ArticleFEBS letters2018

The role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates.

Matthew R Jensen, Brandon R Goblirsch, Morgan A Esler, James K Christenson, Fatuma A Mohamed, Lawrence P Wackett, Carrie M Wilmot

Open access · bronzeAbstract readLetter
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 51% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Computational and structural biotechnology journal · 2021
    Article
  2. mBio · 2020
    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

7 authors at 2 institutions in 1 country.

Matthew R JensenDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St Paul, MN, USA.
Brandon R GoblirschDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St Paul, MN, USA.
Morgan A EslerDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St Paul, MN, USA.
James K ChristensonDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St Paul, MN, USA.
Fatuma A MohamedDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St Paul, MN, USA.
Lawrence P WackettDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St Paul, MN, USA.
Carrie M WilmotDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St Paul, MN, USA.
University of Minnesota · USBiotechnology Institute · US

Funding

TRAINING FOR FUTURE BIOTECHNOLOGY DEVELOPMENTT32GM008347 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SCHMIDT-DANNERT, CLAUDIA · 1990 to 2021
$11.0M
Chemistry-Biology Interface Training GrantT32GM008700 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI DISTEFANO, MARK D · 1999 to 2018
$4.0M
NIGMS NIH HHS T32 GM008347NIGMS NIH HHS T32 GM008700
6 · The paper itself

Abstract

Renewable production of hydrocarbons is being pursued as a petroleum-independent source of commodity chemicals and replacement for biofuels. The bacterial biosynthesis of long-chain olefins represents one such platform. The process is initiated by OleA catalyzing the condensation of two fatty acyl-coenzyme A substrates to form a β-keto acid. Here, the mechanistic role of the conserved His285 is investigated through mutagenesis, activity assays, and X-ray crystallography. Our data demonstrate that His285 is required for product formation, influences the thiolase nucleophile Cys143 and the acyl-enzyme intermediate before and after transesterification, and orchestrates substrate coordination as a defining component of an oxyanion hole. As a consequence, His285 plays a key role in enabling a mechanistic strategy in OleA that is distinct from other thiolases.

Indexed as

Acyl Coenzyme ABacterial ProteinsCatalysisHistidineXanthomonas campestrisAcyl Coenzyme ABacterial ProteinsHistidineOleAthiolaseX-ray crystallography

Identifiers

PMID29430657
PMCPMC5869120
OpenAlexW2789291726

What OpenQuestion holds

Textmetadata
LicenceTDM
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.