Evidence map›Paper›PMID 16052321›Full record

ArticlePlanta2005

Biochemical properties of isoprene synthase in poplar (Populus x canescens).

J-P Schnitzler, I Zimmer, A Bachl, M Arend, J Fromm, R J Fischbach

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

39 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Cryptic isoprene emission of soybeans.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. De Novo Terpenes Emitted from Juvenile Leaves ofMolecules (Basel, Switzerland) · 2025
    Article
  5. Article
  6. Optimization of IspSApplied and environmental microbiology · 2023
    Article
  7. Emission Trade-Off between Isoprene and Other BVOC Components inInternational journal of molecular sciences · 2023
    Article
  8. Microbial Production Potential ofMicroorganisms · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Anaerobic Production of Isoprene by EngineeredApplied and environmental microbiology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. 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

6 authors at 1 institution in 1 country.

J-P SchnitzlerForschungszentrum Karlsruhe GmbH, Institut für Meteorologie und Klimaforschung, Atmosphärische Umweltforschung (IMK-IFU), Kreuzeckbahnstr. 19, 82467, Garmisch-Partenkirchen, Germany. joerg-peter.schnitzler@imk.fzk.de
I Zimmer
A Bachl
M Arend
J Fromm
R J Fischbach
Technical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Isoprene synthase (ISPS) catalyzes the elimination of pyrophosphate from dimethylallyl diphosphate (DMADP) forming isoprene, a volatile hydrocarbon emitted from many plant species to the atmosphere. In the present work, immunological techniques were applied to study and localize ISPS in poplar leaves (Populus x canescens). Immunogold labeling using polyclonal antibodies generated against His-tagged recombinant ISPS protein detected ca. 44% of ISPS in the stroma of the chloroplasts and ca. 56% of gold particles attached to the stromal-facing side of the thylakoid membranes. ISPS isolated from leaves exhibited the same biochemical properties as the recombinant ISPS without the plastid-targeting peptide heterologous expressed in E. coli, whereas an additional C- or N-terminal His-tag changed the biochemical features of the recombinant enzyme with regard to temperature, pH, and substrate dependence. In comparison to the closely related class of monoterpene synthases from angiosperms and ISPS of oaks, the most striking feature of the poplar ISPS is a cooperative substrate dependence which is characteristic to enzymes with positive substrate activation. The detection of four immunoreactive bands in poplar leaf extracts with isoelectric points from 5.0 to 5.5 and a native molecular weight of ca. 51 kDa give reason for future studies on post-translational modifications of ISPS.

Indexed as

Alkyl and Aryl TransferasesImmunochemistryKineticsPopulusRecombinant ProteinsSubstrate SpecificityTissue DistributionAlkyl and Aryl Transferasesisoprene synthaseRecombinant Proteins

Identifiers

PMID16052321
OpenAlexW2028397969

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.