Evidence map›Paper›PMID 24411456›Full record

ArticleEnzyme and microbial technology2014

Expression of dehydratase domains from a polyunsaturated fatty acid synthase increases the production of fatty acids in Escherichia coli.

Delise Oyola-Robles, Carlos Rullán-Lind, Néstor M Carballeira, Abel Baerga-Ortiz

Open access · greenAbstract read
In one paragraph

Article in Enzyme and microbial technology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

5 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  4. Review
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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

4 authors at 2 institutions in 1 country.

Delise Oyola-RoblesDepartment of Biochemistry, University of Puerto Rico School of Medicine, P.O. Box 365067, San Juan, 00936-5067, Puerto Rico. Electronic address: delise.oyola@upr.edu.
Carlos Rullán-LindDepartment of Biochemistry, University of Puerto Rico School of Medicine, P.O. Box 365067, San Juan, 00936-5067, Puerto Rico. Electronic address: carlos.rullan@upr.edu.
Néstor M CarballeiraDepartment of Chemistry, University of Puerto Rico, Rio Piedras Campus, PO Box 23346, San Juan, 00931-3346, Puerto Rico. Electronic address: nestor.carballeira1@upr.edu.
Abel Baerga-OrtizDepartment of Biochemistry, University of Puerto Rico School of Medicine, P.O. Box 365067, San Juan, 00936-5067, Puerto Rico; Molecular Sciences Building, University of Puerto Rico, San Juan, 00926, Puerto Rico. Electronic address: abel.baerga@upr.edu.
University of Puerto Rico System · PRUniversity of Puerto Rico at Río Piedras · PR

Funding

SUPPLEMENT FOR RENOVATION OF ANIMAL FACILITIES AT INSTITUTE OF NEUROBIOLOGYG12RR003051 · NCRR · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI ESPINO, ANA M · 1986 to 2011
$28.1M
RISE Option III: MBRS RISE at the UPR Medical Sciences CampusR25GM061838 · NIGMS · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI CADILLA, CARMEN LYDIA · 2000 to 2021
$25.5M
TRANSLATIONAL PROTEOMICS CENTERG12MD007600 · NIMHD · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI FERNANDEZ-REPOLLET, EMMA · 2012 to 2016
$11.0M
NCRR NIH HHS G12 RR003051NCRR NIH HHS G12RR03051NIGMS NIH HHS R25 GM061838NIGMS NIH HHS R25GM061838NIMHD NIH HHS G12 MD007600
6 · The paper itself

Abstract

Increasing the production of fatty acids by microbial fermentation remains an important step toward the generation of biodiesel and other portable liquid fuels. In this work, we report an Escherichia coli strain engineered to overexpress a fragment consisting of four dehydratase domains from the polyunsaturated fatty acid (PUFA) synthase enzyme complex from the deep-sea bacterium, Photobacterium profundum. The DH1-DH2-UMA enzyme fragment was excised from its natural context within a multi-enzyme PKS and expressed as a stand-alone protein. Fatty acids were extracted from the cell pellet, esterified with methanol and quantified by GC-MS analysis. Results show that the E. coli strain expressing the DH tetradomain fragment was capable of producing up to a 5-fold increase (80.31 mg total FA/L culture) in total fatty acids over the negative control strain lacking the recombinant enzyme. The enhancement in production was observed across the board for all the fatty acids that are typically made by E. coli. The overexpression of the DH tetradomain did not affect E. coli cell growth, thus showing that the observed enhancement in fatty acid production was not a result of effects associated with cell density. The observed enhancement was more pronounced at lower temperatures (3.8-fold at 16 °C, 3.5-fold at 22 °C and 1.5-fold at 30 °C) and supplementation of the media with 0.4% glycerol did not result in an increase in fatty acid production. All these results taken together suggest that either the dehydration of fatty acid intermediates are a limiting step in the E. coli fatty acid biosynthesis machinery, or that the recombinant dehydratase domains used in this study are also capable of catalyzing thioester hydrolysis of the final products. The enzyme in this report is a new tool which could be incorporated into other existing strategies aimed at improving fatty acid production in bacterial fermentations toward accessible biodiesel precursors.

Indexed as

Bacterial ProteinsBiocatalysisBiofuelsCarbonCulture MediaEscherichia coliFatty AcidsFatty Acids, UnsaturatedFatty Acid SynthasesFermentationGlycerolPeptide FragmentsPhotobacteriumProtein Structure, TertiaryRecombinant Fusion ProteinsTemperatureBacterial ProteinsBiofuelsCarbonCulture MediaFatty AcidsFatty Acids, UnsaturatedFatty Acid SynthasesGlycerolPeptide FragmentsRecombinant Fusion ProteinsACPacyl carrier proteinacyl tranferasesATBiodieselBioengineeringBiofueldehydrataseDehydratase domainDHenoyl reductaseEREscherichia coli.FAFAMEfatty acidfatty acid methyl esterFatty acids overproductiongas chromatographyGCketo-acyl reductaseketo-acyl synthaseKRKSmass spectrometryMSpolyunsaturated fatty acidsPUFAsaturated fatty acidSFAUFAunsaturated fatty acid

Identifiers

PMID24411456
PMCPMC3894691
OpenAlexW2017710964

What OpenQuestion holds

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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.