Evidence map›Paper›PMID 20406823›Full record

ArticleThe Journal of biological chemistry2010

Oxazolomycin biosynthesis in Streptomyces albus JA3453 featuring an "acyltransferase-less" type I polyketide synthase that incorporates two distinct extender units.

Chunhua Zhao, Jane M Coughlin, Jianhua Ju, Dongqing Zhu, Evelyn Wendt-Pienkowski, Xiufen Zhou, Zhijun Wang, Ben Shen, Zixin Deng

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
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

37 citing papers in PubMed.

  1. Article
  2. Spirocyclic β-lactone secondary metabolites modulate spliceosome function.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Biosynthesis in Streptomyces sp. NRRL S-1813 and regulation between oxazolomycin A and A2.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Oxazolomycins produced byRSC advances · 2021
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

9 authors.

Chunhua ZhaoLaboratory of Microbial Metabolism and School of Life Sciences and Biotechnology, Shanghai Jiaotong University, Shanghai 200030, China.
Jane M Coughlin
Jianhua Ju
Dongqing Zhu
Evelyn Wendt-Pienkowski
Xiufen Zhou
Zhijun Wang
Ben Shen
Zixin Deng

Funding

Zeeh Pharmaceutical Experimental StationU19CA113297 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI HOFFMANN, F. MICHAEL · 2005 to 2009
$5.4M
AT-less Type I Polyketide SynthasesR01CA106150 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI SHEN, BEN · 2004 to 2015
$3.3M
NCI NIH HHS CA113297NCI NIH HHS R01 CA106150NCI NIH HHS U19 CA113297
6 · The paper itself

Abstract

The oxazolomycins (OZMs) are a growing family of antibiotics produced by several Streptomyces species that show diverse and important antibacterial, antitumor, and anti-human immunodeficiency virus activity. Oxazolomycin A is a peptide-polyketide hybrid compound containing a unique spiro-linked beta-lactone/gamma-lactam, a 5-substituted oxazole ring. The oxazolomycin biosynthetic gene cluster (ozm) was identified from Streptomyces albus JA3453 and localized to 79.5-kb DNA, consisting of 20 open reading frames that encode non-ribosomal peptide synthases, polyketide synthases (PKSs), hybrid non-ribosomal peptide synthase-PKS, trans-acyltransferases (trans-ATs), enzymes for methoxymalonyl-acyl carrier protein (ACP) synthesis, putative resistance genes, and hypothetical regulation genes. In contrast to classical type I polyketide or fatty acid biosynthases, all 10 PKS modules in the gene cluster lack cognate ATs. Instead, discrete ATs OzmM (with tandem domains OzmM-AT1 and OzmM-AT2) and OzmC were equipped to carry out all of the loading functions of both malonyl-CoA and methoxymalonyl-ACP extender units. Strikingly, only OzmM-AT2 is required for OzmM activity for OZM biosynthesis, whereas OzmM-AT1 seemed to be a cryptic AT domain. The above findings, together with previous results using isotope-labeled precursor feeding assays, are assembled for the OZM biosynthesis model to be proposed. The incorporation of both malonyl-CoA (by OzmM-AT2) and methoxymalonyl-ACP (by OzmC) extender units seemed to be unprecedented for this class of trans-AT type I PKSs, which might be fruitfully manipulated to create structurally diverse novel compounds.

Indexed as

AcyltransferasesAmino Acid SequenceBacterial ProteinsBinding SitesBiosynthetic PathwaysGene DeletionGene OrderGenetic Complementation TestModels, BiologicalMultigene FamilyOpen Reading FramesOxazolesPolyketide SynthasesPyrrolidinonesSpiro CompoundsStreptomycesAcyltransferasesBacterial ProteinsdiffusomycinOxazolesPolyketide SynthasesPyrrolidinonesSpiro Compounds

Identifiers

PMID20406823
PMCPMC2888422

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.