Evidence map›Paper›PMID 8692906›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Identifying functional domains within terpene cyclases using a domain-swapping strategy.

K Back, J Chappell

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

31 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Review
  3. Germacrene A-A Central Intermediate in Sesquiterpene Biosynthesis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. 3DSwap: curated knowledgebase of proteins involved in 3D domain swapping.Database : the journal of biological databases and curation · 2011
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Elucidation of the biosynthetic origin of the anti-inflammatory pseudopterosins.Journal of industrial microbiology & biotechnology · 2006
    Review
  19. Identifying and manipulating structural determinates linking catalytic specificities in terpene synthases.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  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

2 authors at 1 institution in 1 country.

K BackPlant Physiology/Biochemistry/Molecular Biology Program, University of Kentucky, Lexington 40546-0091, USA.
J Chappell
University of Kentucky · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic terpenes and terpenoids are found throughout nature. They comprise an especially important class of compounds from plants that mediate plant- environment interactions, and they serve as pharmaceutical agents with antimicrobial and anti-tumor activities. Molecular comparisons of several terpene cyclases, the key enzymes responsible for the multistep cyclization of C10, C15, and C20 allylic diphosphate substrates, have revealed a striking level of sequence similarity and conservation of exon position and size within the genes. Functional domains responsible for a terminal enzymatic step were identified by swapping regions approximating exons between a Nicotiana tabacum 5-epi-aristolochene synthase (TEAS) gene and a Hyoscyamus muticus vetispiradiene synthase (HVS) gene and by characterization of the resulting chimeric enzymes expressed in bacteria. While exon 4 of the TEAS gene conferred specificity for the predominant reaction products of the tobacco enzyme, exon 6 of the HVS gene conferred specificity for the predominant reaction products of the Hyoscyamus enzyme. Combining these two functional domains of the TEAS and HVS genes resulted in a novel enzyme capable of synthesizing reaction products reflective of both parent enzymes. The relative ratio of the TEAS and HVS reaction products was also influenced by the source of exon 5 present in the new chimeric enzymes. The association of catalytic activities with conserved but separate exonic domains suggests a general means for generating additional novel terpene cyclases.

Indexed as

Alkyl and Aryl TransferasesBase SequenceCloning, MolecularDNA, ComplementaryEscherichia coliMolecular Sequence DataTerpenesTransferases5-epi-aristolochene synthaseAlkyl and Aryl TransferasesDNA, ComplementaryTerpenesTransferasesvetispiradiene synthase

Identifiers

PMID8692906
PMCPMC39115
OpenAlexW2076953277

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.