Evidence map›Paper›PMID 26639528›Full record

ArticleMicrobial biotechnology2016

Ustilago maydis produces itaconic acid via the unusual intermediate trans-aconitate.

Elena Geiser, Sandra K Przybilla, Alexandra Friedrich, Wolfgang Buckel, Nick Wierckx, Lars M Blank, Michael Bölker

Open access · goldAbstract read
In one paragraph

Article in Microbial biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

66 citing papers in PubMed, 137 citations in OpenAlex.

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  15. DoE-based medium optimization for improved biosurfactant production withFrontiers in bioengineering and biotechnology · 2024
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  18. Review
  19. Structural characterization of theComputational and structural biotechnology journal · 2023
    Article
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6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Elena GeiseriAMB - Institute of Applied Microbiology, ABBt - Aachen Biology and Biotechnology, RWTH Aachen University, Worringerweg 1, D-52074, Aachen, Germany.
Sandra K PrzybillaDepartment of Biology, Philipps-University Marburg, Karl-von-Frisch-Straße 8, D-35032, Marburg, Germany.
Alexandra FriedrichDepartment of Biology, Philipps-University Marburg, Karl-von-Frisch-Straße 8, D-35032, Marburg, Germany.
Wolfgang BuckelDepartment of Biology, Philipps-University Marburg, Karl-von-Frisch-Straße 8, D-35032, Marburg, Germany.
Nick WierckxiAMB - Institute of Applied Microbiology, ABBt - Aachen Biology and Biotechnology, RWTH Aachen University, Worringerweg 1, D-52074, Aachen, Germany.
Lars M BlankiAMB - Institute of Applied Microbiology, ABBt - Aachen Biology and Biotechnology, RWTH Aachen University, Worringerweg 1, D-52074, Aachen, Germany.
Michael BölkerDepartment of Biology, Philipps-University Marburg, Karl-von-Frisch-Straße 8, D-35032, Marburg, Germany.
Philipps University of Marburg · DERWTH Aachen University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Itaconic acid is an important biomass-derived chemical building block but has also recently been identified as a metabolite produced in mammals, which has antimicrobial activity. The biosynthetic pathway of itaconic acid has been elucidated in the ascomycetous fungus Aspergillus terreus and in human macrophages. In both organisms itaconic acid is generated by decarboxylation of the tricarboxylic acid (TCA) cycle intermediate cis-aconitate. Here, we show that the basidiomycetous fungus Ustilago maydis uses an alternative pathway and produces itaconic acid via trans-aconitate, the thermodynamically favoured isomer of cis-aconitate. We have identified a gene cluster that contains all genes involved in itaconic acid formation. Trans-aconitate is generated from cis-aconitate by a cytosolic aconitate-Δ-isomerase (Adi1) that belongs to the PrpF family of proteins involved in bacterial propionate degradation. Decarboxylation of trans-aconitate is catalyzed by a novel enzyme, trans-aconitate decarboxylase (Tad1). Tad1 displays significant sequence similarity with bacterial 3-carboxy-cis,cis-muconate lactonizing enzymes (CMLE). This suggests that U. maydis has evolved an alternative biosynthetic pathway for itaconate production using the toxic intermediate trans-aconitate. Overexpression of a pathway-specific transcription factor (Ria1) or a mitochondrial tricarboxylic acid transporter (Mtt1) resulted in a twofold increase in itaconate yield. Therefore, our findings offer new strategies for biotechnological production of this valuable biomass-derived chemical.

Indexed as

Aconitic AcidBiosynthetic PathwaysFungal ProteinsIsomerismSuccinatesUstilagoAconitic AcidFungal Proteinsitaconic acidSuccinates

Identifiers

PMID26639528
PMCPMC4720413
OpenAlexW2187961607

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.