Evidence map›Paper›PMID 21204864›Full record

ReviewFEMS microbiology reviews2011

Fatty acid biosynthesis in actinomycetes.

Gabriela Gago, Lautaro Diacovich, Ana Arabolaza, Shiou-Chuan Tsai, Hugo Gramajo

Open access · bronzeAbstract readReview
In one paragraph

Review in FEMS microbiology reviews, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
6.2field-weighted citation impact, top 4% 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

94 citing papers in PubMed, 175 citations in OpenAlex.

  1. Article
  2. Description ofInternational journal of systematic and evolutionary microbiology · 2026
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  3. Review
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  7. MarinePharmaceuticals (Basel, Switzerland) · 2026
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  8. Article
  9. Article
  10. Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026
    Review
  11. Article
  12. Article
  13. An extremophilicbioRxiv : the preprint server for biology · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. New Potent Sulfonamide-Based Inhibitors ofACS medicinal chemistry letters · 2024
    Article
  20. Review

34 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 2 countries.

Gabriela GagoMicrobiology Division, IBR (Instituto de Biología Molecular y Celular de Rosario), Consejo Nacional de Investigaciones Científicas y Técnicas, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.
Lautaro Diacovich
Ana Arabolaza
Shiou-Chuan Tsai
Hugo Gramajo
National University of Rosario · ARUniversity of California, Irvine · US

Funding

Characterization of two acyl-CoA carboxylase complexes of Mycobacterium tuberculoR03TW007982 · FIC · INSTITUTE OF MOLECULAR /CELLULAR BIOLOGY · PI GRAMAJO, HUGO · 2008 to 2010
$96k
FIC NIH HHS 1R03TW007982-02FIC NIH HHS R03 TW007982
6 · The paper itself

Abstract

All organisms that produce fatty acids do so via a repeated cycle of reactions. In mammals and other animals, these reactions are catalyzed by a type I fatty acid synthase (FAS), a large multifunctional protein to which the growing chain is covalently attached. In contrast, most bacteria (and plants) contain a type II system in which each reaction is catalyzed by a discrete protein. The pathway of fatty acid biosynthesis in Escherichia coli is well established and has provided a foundation for elucidating the type II FAS pathways in other bacteria (White et al., 2005). However, fatty acid biosynthesis is more diverse in the phylum Actinobacteria: Mycobacterium, possess both FAS systems while Streptomyces species have only the multienzyme FAS II system and Corynebacterium species exclusively FAS I. In this review, we present an overview of the genome organization, biochemical properties and physiological relevance of the two FAS systems in the three genera of actinomycetes mentioned above. We also address in detail the biochemical and structural properties of the acyl-CoA carboxylases (ACCases) that catalyzes the first committed step of fatty acid synthesis in actinomycetes, and discuss the molecular bases of their substrate specificity and the structure-based identification of new ACCase inhibitors with antimycobacterial properties.

Indexed as

ActinobacteriaBacterial ProteinsBinding SitesFatty AcidsFatty Acid Synthase, Type IIBacterial ProteinsFatty AcidsFatty Acid Synthase, Type II

Identifiers

PMID21204864
PMCPMC3079561
OpenAlexW1839672289

What OpenQuestion holds

Textmetadata
LicenceTDM
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.