Evidence map›Paper›PMID 19762471›Full record

ArticleThe Journal of biological chemistry2009

Biochemical characterization of two wheat phosphoethanolamine N-methyltransferase isoforms with different sensitivities to inhibition by phosphatidic acid.

Ricarda Jost, Oliver Berkowitz, John Shaw, Josette Masle

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. A Comprehensive Functional Analysis ofPlants (Basel, Switzerland) · 2025
    Article
  2. Review
  3. NMT1 and NMT3Plant physiology · 2018
    Article
  4. Article
  5. Conformational changes in the di-domain structure ofThe Journal of biological chemistry · 2017
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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 1 institution in 1 country.

Ricarda JostEnvironmental Biology Group, Research School of Biological Sciences, The Australian National University, G. P. O. Box 475, Canberra, Australian Capital Territory 0200, Australia.
Oliver Berkowitz
John Shaw
Josette Masle
Australian National University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants the triple methylation of phosphoethanolamine to phosphocholine catalyzed by phosphoethanolamine N-methyltransferase (PEAMT) is considered a rate-limiting step in the de novo synthesis of phosphatidylcholine. Besides being a major membrane phospholipid, phosphatidylcholine can be hydrolyzed into choline and phosphatidic acid. Phosphatidic acid is widely recognized as a second messenger in stress signaling, and choline can be oxidized within the chloroplast to yield the putative osmoprotectant glycine betaine. Here we describe the cloning and biochemical characterization of a second wheat PEAMT isoform that has a four times higher specific activity than the previously described WPEAMT/TaPEAMT1 enzyme and is less sensitive to product inhibition by S-adenosyl homocysteine, but more sensitive to inhibition by phosphocholine. Both enzymes follow a sequential random Bi Bi mechanism and show mixed-type product inhibition patterns with partial inhibition for TaPEAMT1 and a strong non-competitive component for TaPEAMT2. An induction of TaPEAMT protein expression and activity is observed after cold exposure, ahead of an increase in gene expression. Our results demonstrate direct repression of in vitro enzymatic activities by phosphatidic acid for both enzymes, with TaPEAMT1 being more sensitive than TaPEAMT2 in the physiological concentration range. Other lipid ligands identified in protein-lipid overlays are phosphoinositide mono- as well as some di-phosphates and cardiolipin. These results provide new insights into the complex regulatory circuits of phospholipid biosynthesis in plants and underline the importance of head group biosynthesis in adaptive stress responses.

Indexed as

AcclimatizationAnimalsBlotting, WesternCloning, MolecularCold TemperatureImmunoglobulin GIsoenzymesPhosphatidic AcidsPhosphatidylethanolamine N-MethyltransferasePhosphatidylinositolsPhylogenyRabbitsRecombinant ProteinsReverse Transcriptase Polymerase Chain ReactionRNA, MessengerS-AdenosylhomocysteineImmunoglobulin GIsoenzymesPhosphatidic AcidsPhosphatidylethanolamine N-MethyltransferasePhosphatidylinositolsRecombinant ProteinsRNA, MessengerS-Adenosylhomocysteine

Identifiers

PMID19762471
PMCPMC2797268
OpenAlexW2033263043

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.