Evidence map›Paper›PMID 24497638›Full record

ArticleThe Journal of biological chemistry2014

Candida albicans utilizes a modified β-oxidation pathway for the degradation of toxic propionyl-CoA.

Christian Otzen, Bettina Bardl, Ilse D Jacobsen, Markus Nett, Matthias Brock

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. 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
1.1field-weighted citation impact, top 24% 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

37 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  3. Metabolic engineering enablesSynthetic and systems biotechnology · 2026
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  5. mBio · 2026
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  6. Review
  7. Article
  8. Article
  9. Article
  10. Peroxisomes regulate virulence and cell density sensing inbioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Article
  13. Propionate metabolism inFrontiers in microbiology · 2025
    Article
  14. Central Carbon Metabolism inJournal of fungi (Basel, Switzerland) · 2024
    Article
  15. Article
  16. Article
  17. Creation of Environmentally Friendly Super "Dinitrotoluene Scavenger" Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  18. Review
  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

5 authors at 3 institutions in 4 countries.

Christian OtzenFrom Microbial Biochemistry and Physiology.
Bettina Bardl
Ilse D Jacobsen
Markus Nett
Matthias Brock
Ecologie Microbienne Lyon · FRLeibniz-Institut für Naturstoff-Forschung und Infektionsbiologie e. V. - Hans-Knöll-Institut (HKI) · DEBio Base Europe · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Propionyl-CoA arises as a metabolic intermediate from the degradation of propionate, odd-chain fatty acids, and some amino acids. Thus, pathways for catabolism of this intermediate have evolved in all kingdoms of life, preventing the accumulation of toxic propionyl-CoA concentrations. Previous studies have shown that fungi generally use the methyl citrate cycle for propionyl-CoA degradation. Here, we show that this is not the case for the pathogenic fungus Candida albicans despite its ability to use propionate and valerate as carbon sources. Comparative proteome analyses suggested the presence of a modified β-oxidation pathway with the key intermediate 3-hydroxypropionate. Gene deletion analyses confirmed that the enoyl-CoA hydratase/dehydrogenase Fox2p, the putative 3-hydroxypropionyl-CoA hydrolase Ehd3p, the 3-hydroxypropionate dehydrogenase Hpd1p, and the putative malonate semialdehyde dehydrogenase Ald6p essentially contribute to propionyl-CoA degradation and its conversion to acetyl-CoA. The function of Hpd1p was further supported by the detection of accumulating 3-hydroxypropionate in the hpd1 mutant on propionyl-CoA-generating nutrients. Substrate specificity of Hpd1p was determined from recombinant purified enzyme, which revealed a preference for 3-hydroxypropionate, although serine and 3-hydroxyisobutyrate could also serve as substrates. Finally, virulence studies in a murine sepsis model revealed attenuated virulence of the hpd1 mutant, which indicates generation of propionyl-CoA from host-provided nutrients during infection.

Indexed as

Acyl Coenzyme AAnimalsCandida albicansCandidiasisFatty AcidsFemaleFungal ProteinsMetabolic Networks and PathwaysMiceMice, Inbred BALB CMutationOxidation-ReductionPropionatesAcyl Coenzyme AFatty AcidsFungal ProteinsPropionatespropionyl-coenzyme AAmino AcidCandida albicansCUG cladeEnzyme KineticsFatty Acid MetabolismFatty Acid OxidationOdd-chain Fatty AcidsPathogenesisβ-Hydroxypropionate

Identifiers

PMID24497638
PMCPMC3961645
OpenAlexW2004054808

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.