Evidence map›Paper›PMID 24189065›Full record

ArticleThe Journal of biological chemistry2013

Plant acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have different specificities in their forward and reverse reactions.

Ida Lager, Jenny Lindberg Yilmaz, Xue-Rong Zhou, Katarzyna Jasieniecka, Michael Kazachkov, Peng Wang, Jitao Zou, Randall Weselake, Mark A Smith, Shen Bayon and 6 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

83 citing papers in PubMed, 149 citations in OpenAlex.

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23 more citing papers are in PubMed but not listed here.

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

16 authors at 10 institutions in 6 countries.

Ida LagerFrom the Department of Plant Breeding, Swedish University of Agricultural Sciences, S-230 53 Alnarp, Sweden.
Jenny Lindberg Yilmaz
Xue-Rong Zhou
Katarzyna Jasieniecka
Michael Kazachkov
Peng Wang
Jitao Zou
Randall Weselake
Mark A Smith
Shen Bayon
John M Dyer
Jay M Shockey
Ernst Heinz
Allan Green
Antoni Banas
Sten Stymne
Saskatchewan Research Council (Canada) · CAACT GovernmentGdańsk Medical University · PLAgricultural Research Service · USSwedish University of Agricultural Sciences · SEUnited States Department of Agriculture · USUniversität Hamburg · DEUniversity of Alberta · CAUniversity of Nebraska–Lincoln · USWashington State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine (PC). Plant LPCAT genes were expressed in yeast and characterized biochemically in microsomal preparations of the cells. Specificities for different acyl-CoAs were similar for seven LPCATs from five different species, including species accumulating hydroxylated acyl groups in their seed oil, with a preference for C18-unsaturated acyl-CoA and low activity with palmitoyl-CoA and ricinoleoyl (12-hydroxyoctadec-9-enoyl)-CoA. We showed that Arabidopsis LPCAT1 and LPCAT2 enzymes catalyzed the acylation and de-acylation of both sn positions of PC, with a preference for the sn-2 position. When acyl specificities of the Arabidopsis LPCATs were measured in the reverse reaction, sn-2-bound oleoyl, linoleoyl, and linolenoyl groups from PC were transferred to acyl-CoA to a similar extent. However, a ricinoleoyl group at the sn-2-position of PC was removed 4-6-fold faster than an oleoyl group in the reverse reaction, despite poor utilization in the forward reaction. The data presented, taken together with earlier published reports on in vivo lipid metabolism, support the hypothesis that plant LPCAT enzymes play an important role in regulating the acyl-CoA composition in plant cells by transferring polyunsaturated and hydroxy fatty acids produced on PC directly to the acyl-CoA pool for further metabolism or catabolism.

Indexed as

1-Acylglycerophosphocholine O-AcyltransferaseAcylationAcyl Coenzyme AArabidopsisArabidopsis ProteinsBase SequenceCatalysisFatty Acids, UnsaturatedMolecular Sequence DataSpecies Specificity1-Acylglycerophosphocholine O-AcyltransferaseAcyl Coenzyme AArabidopsis ProteinsFatty Acids, UnsaturatedArabidopsisEnzymeEnzymesLipid MetabolismLysophosphatidylcholine AcyltransferasesPhosphatidylcholinePhosphatidylcholine MetabolismPlant BiochemistryPlant Lipid Biochemistry

Identifiers

PMID24189065
PMCPMC3873549
OpenAlexW2116232319

What OpenQuestion holds

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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.