Evidence map›Paper›PMID 25880760›Full record

ArticleMicrobial cell factories2015

Fungal cytochrome P450 monooxygenases of Fusarium oxysporum for the synthesis of ω-hydroxy fatty acids in engineered Saccharomyces cerevisiae.

Pradeepraj Durairaj, Sailesh Malla, Saravanan Prabhu Nadarajan, Pyung-Gang Lee, Eunok Jung, Hyun Ho Park, Byung-Gee Kim, Hyungdon Yun

Abstract read
In one paragraph

Article in Microbial cell factories, 2015. 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
–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

21 citing papers in PubMed.

  1. Virulence · 2025
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  7. Biodegradation of Petroleum Hydrocarbons byMolecules (Basel, Switzerland) · 2022
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  11. Application of Random Mutagenesis and Synthetic FadR Promoter forFrontiers in bioengineering and biotechnology · 2021
    Article
  12. Metabolic engineering communications · 2020
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  17. Review
  18. Article
  19. Diverse Metabolic Capacities of Fungi for Bioremediation.Indian journal of microbiology · 2016
    Review
  20. Review
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

8 authors.

Pradeepraj DurairajSchool of Biotechnology, Yeungnam University, Gyeongsan, South Korea. deeprajbiotech@gmail.com.
Sailesh MallaSchool of Chemical and Biological Engineering, Seoul National University, Seoul, South Korea. sailesh.malla@gmail.com.
Saravanan Prabhu NadarajanDepartment of Bioscience and Biotechnology, Konkuk University, Seoul, South Korea. saravananprabhu@gmail.com.
Pyung-Gang LeeSchool of Chemical and Biological Engineering, Seoul National University, Seoul, South Korea. lpg9456@hanmail.net.
Eunok JungSchool of Chemical and Biological Engineering, Seoul National University, Seoul, South Korea. lovetm22@snu.ac.kr.
Hyun Ho ParkSchool of Biotechnology, Yeungnam University, Gyeongsan, South Korea. hyunho@ynu.ac.kr.
Byung-Gee KimSchool of Chemical and Biological Engineering, Seoul National University, Seoul, South Korea. byungkim@snu.ac.kr.
Hyungdon YunDepartment of Bioscience and Biotechnology, Konkuk University, Seoul, South Korea. hyungdon@konkuk.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundOmega hydroxy fatty acids (ω-OHFAs) are multifunctional compounds that act as the basis for the production of various industrial products with broad commercial and pharmaceutical implications. However, the terminal oxygenation of saturated or unsaturated fatty acids for the synthesis of ω-OHFAs is intricate to accomplish through chemocatalysis, due to the selectivity and controlled reactivity in C-H oxygenation reactions. Cytochrome P450, the ubiquitous enzyme is capable of catalyzing the selective terminal omega hydroxylation naturally in biological kingdom.

resultsTo gain a deep insight on the biochemical role of fungal P450s towards the production of omega hydroxy fatty acids, two cytochrome P450 monooxygenases from Fusarium oxysporum (FoCYP), FoCYP539A7 and FoCYP655C2; were identified, cloned, and heterologously expressed in Saccharomyces cerevisiae. For the efficient production of ω-OHFAs, the S. cerevisiae was engineered to disrupt the acyl-CoA oxidase enzyme and the β-oxidation pathway inactivated (ΔPox1) S. cerevisiae mutant was generated. To elucidate the significance of the interaction of redox mechanism, FoCYPs were reconstituted with the heterologous and homologous reductase systems--S. cerevisiae CPR (ScCPR) and F. oxysporum CPR (FoCPR). To further improve the yield, the effect of pH was analyzed and the homologous FoCYP-FoCPR system efficiently hydroxylated caprylic acid, capric acid and lauric acid into their respective ω-hydroxy fatty acids with 56%, 79% and 67% conversion. Furthermore, based on computational simulations, we identified the key residues (Asn106 of FoCYP539A7 and Arg235 of FoCYP655C2) responsible for the recognition of fatty acids and demonstrated the structural insights of the active site of FoCYPs.

conclusionFungal CYP monooxygenases, FoCYP539A7 and FoCYP655C2 with its homologous redox partner, FoCPR constitutes a promising catalyst due to its high regio- and stereo-selectivity in the hydroxylation of fatty acids and in the substantial production of industrially valuable ω-hydroxy fatty acids.

Indexed as

Acyl-CoA OxidaseAmino Acid SequenceArginineAsparagineCatalytic DomainCytochrome P-450 Enzyme SystemFatty AcidsFungal ProteinsFusariumHydrogen-Ion ConcentrationHydroxylationIndustrial MicrobiologyIsoenzymesLauric AcidsMetabolic EngineeringMolecular Sequence Data12-hydroxydodecanoic acidAcyl-CoA OxidaseArginineAsparagineCytochrome P-450 Enzyme SystemFatty AcidsFungal ProteinsIsoenzymesLauric AcidsSaccharomyces cerevisiae Proteins

Identifiers

PMID25880760
PMCPMC4387584

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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.