Evidence map›Paper›PMID 15651811›Full record

ArticleThe Journal of organic chemistry2005

Identification of the function of gene lndM2 encoding a bifunctional oxygenase-reductase involved in the biosynthesis of the antitumor antibiotic landomycin E by Streptomyces globisporus 1912 supports the originally assigned structure for landomycinone.

Lili Zhu, Bohdan Ostash, Uwe Rix, Mohammad Nur-E-Alam, Almuth Mayers, Andriy Luzhetskyy, Carmen Mendez, Jose A Salas, Andreas Bechthold, Victor Fedorenko and 1 more

Open access · greenAbstract read
In one paragraph

Article in The Journal of organic chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Bioactive compounds from marine actinomycetes.Indian journal of microbiology · 2008
    Article
  19. 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

11 authors at 1 institution in 1 country.

Lili ZhuDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 725 Rose Street, Lexington, Kentucky 40536-0082, USA.
Bohdan Ostash
Uwe Rix
Mohammad Nur-E-Alam
Almuth Mayers
Andriy Luzhetskyy
Carmen Mendez
Jose A Salas
Andreas Bechthold
Victor Fedorenko
Jürgen Rohr
University of Freiburg · DE

Funding

NOVEL AUREOLIC ACID TYPE ANTITUMOR AGENTSR01CA091901 · NCI · UNIVERSITY OF KENTUCKY · PI ROHR, JURGEN T · 2001 to 2017
$3.6M
BIOSYNTHETIC KEY STEPS OF ANGUCYCLINE ANTITUMOR DRUGSR01CA102102 · NCI · UNIVERSITY OF KENTUCKY · PI ROHR, JURGEN T · 2005 to 2009
$1.3M
NCI NIH HHS CA 91901NCI NIH HHS R01 CA091901NCI NIH HHS R01 CA102102
6 · The paper itself

Abstract

The angucycline antibiotic family of the landomycins displays potent antitumor activity. To elucidate early post polyketide synthase (PKS) tailoring steps of the landomycin E biosynthetic pathway in Streptomyces globisporus 1912, the mutant S. globisporus M12 was prepared through gene replacement experiment of lndM2. It encodes an enzyme with putative oxygenase and reductase domains, according to sequencing of the gene and its counterpart lanM2 from S. cyanogenus S136 landomycin A biosynthetic gene cluster. The isolation of the novel shunt products 11-hydroxytetrangomycin and 4-hydroxytetrangomycin along with the well-known angucyclines tetrangomycin and tetrangulol from the culture of S. globisporus M12 provides evidence for the involvement of lndM2 in the early biosynthetic pathway of the landomycins, in particular in the formation of the alicyclic 6-hydroxy function of the landomycin aglycon. We therefore propose LndM2 to be responsible for both hydroxylation of the 6-position and its subsequent reduction. These reactions are necessary before the glycosylation reactions can occur. The results are in agreement with the originally published structure of landomycin but do not support the recently suggested revised structure.

Indexed as

AminoglycosidesAntibiotics, AntineoplasticDNA, BacterialGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGenes, BacterialMolecular StructureMultigene FamilyMutationNaphthoquinonesOligosaccharidesOxidoreductasesStreptomycesAminoglycosidesAntibiotics, AntineoplasticDNA, Bacteriallandomycin ElandomycinoneNaphthoquinonesOligosaccharidesOxidoreductases

Identifiers

PMID15651811
PMCPMC2884283
OpenAlexW2068209092

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.