Evidence map›Paper›PMID 17221359›Full record

ArticlePlant molecular biology2007

Putrescine N-methyltransferases--a structure-function analysis.

Michael Teuber, Mohammad E Azemi, Foroogh Namjoyan, Anna-Carolin Meier, Anja Wodak, Wolfgang Brandt, Birgit Dräger

Abstract read
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2007. 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
3.1field-weighted citation impact, top 8% 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, 59 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
  16. 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

7 authors at 2 institutions in 1 country.

Michael TeuberInstitute of Pharmacy, Faculty of Science I, Martin-Luther University Halle-Wittenberg, Halle, Saale, Germany.
Mohammad E Azemi
Foroogh Namjoyan
Anna-Carolin Meier
Anja Wodak
Wolfgang Brandt
Birgit Dräger
Martin Luther University Halle-Wittenberg · DELeibniz Institute of Plant Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Putrescine N-methyltransferase (PMT) is a key enzyme of plant secondary metabolism at the start of the specific biosynthesis of nicotine, of tropane alkaloids, and of calystegines that are glycosidase inhibitors with nortropane structure. PMT is assumed to have developed from spermidine synthases (SPDS) participating in ubiquitous polyamine metabolism. In this study decisive differences between both enzyme families are elucidated. PMT sequences were known from four Solanaceae genera only, therefore additional eight PMT cDNA sequences were cloned from five Solanaceae and a Convolvulaceae. The encoded polypeptides displayed between 76% and 97% identity and typical amino acids different from plant spermidine synthase protein sequences. Heterologous expression of all enzymes proved catalytic activity exclusively as PMT and K (cat) values between 0.16 s(-1) and 0.39 s(-1). The active site of PMT was initially inferred from a protein structure of spermidine synthase obtained by protein crystallisation. Those amino acids of the active site that were continuously different between PMTs and SPDS were mutated in one of the PMT sequences with the idea of changing PMT activity into spermidine synthase. Mutagenesis of active site residues unexpectedly resulted in a complete loss of catalytic activity. A protein model of PMT was based on the crystal structure of SPDS and suggests that overall protein folds are comparable. The respective cosubstrates S-adenosylmethionine and decarboxylated S-adenosylmethionine, however, appear to bind differentially to the active sites of both enzymes, and the substrate putrescine adopts a different position.

Indexed as

Gene Expression ProfilingAmino Acid SequenceBinding SitesBlotting, NorthernCloning, MolecularComputer SimulationConvolvulaceaeDNA, ComplementaryMethyltransferasesModels, MolecularMolecular Sequence DataMolecular StructurePhylogenyPlant ProteinsProtein Structure, TertiaryPutrescineDNA, ComplementaryMethyltransferasesPlant ProteinsPutrescineputrescine N-methyltransferaseSpermidine Synthase

Identifiers

PMID17221359
OpenAlexW2145985152

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.