Heterologous expression of Mus musculus immunoresponsive gene 1 (irg1) in Escherichia coli results in itaconate production

K.S. Vuoristo; A.E. Mars; S. Loon; E. Orsi; G. Eggink; J.P.M. Sanders; R.A. Weusthuis

doi:10.3389/fmicb.2015.00849

Heterologous expression of Mus musculus immunoresponsive gene 1 (irg1) in Escherichia coli results in itaconate production

K.S. Vuoristo, A.E. Mars, S. Loon, E. Orsi, G. Eggink, J.P.M. Sanders, R.A. Weusthuis

Research output: Contribution to journal › Article › Academic › peer-review

8 Citations (Scopus)

Abstract

Itaconic acid, a C5-dicarboxylic acid, is a potential biobased building block for the polymer industry. It is obtained from the citric acid cycle by decarboxylation of cis-aconitic acid. This reaction is catalyzed by CadA in the native itaconic acid producer Aspergillus terreus. Recently, another enzyme encoded by the mammalian immunoresponsive gene 1 (irg1), was found to decarboxylate cis-aconitate to itaconate in vitro. We show that heterologous expression of irg1 enabled itaconate production in Escherichia coli with production titres up to 560 mg/L.

Original language	English
Article number	849
Journal	Frontiers in Microbiology
Volume	6
DOIs	https://doi.org/10.3389/fmicb.2015.00849
Publication status	Published - 2015

Keywords

codon usage frequencies
aspergillus-terreus
acid production
protein expression
niger
host

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title = "Heterologous expression of Mus musculus immunoresponsive gene 1 (irg1) in Escherichia coli results in itaconate production",

abstract = "Itaconic acid, a C5-dicarboxylic acid, is a potential biobased building block for the polymer industry. It is obtained from the citric acid cycle by decarboxylation of cis-aconitic acid. This reaction is catalyzed by CadA in the native itaconic acid producer Aspergillus terreus. Recently, another enzyme encoded by the mammalian immunoresponsive gene 1 (irg1), was found to decarboxylate cis-aconitate to itaconate in vitro. We show that heterologous expression of irg1 enabled itaconate production in Escherichia coli with production titres up to 560 mg/L.",

keywords = "codon usage frequencies, aspergillus-terreus, acid production, protein expression, niger, host",

author = "K.S. Vuoristo and A.E. Mars and S. Loon and E. Orsi and G. Eggink and J.P.M. Sanders and R.A. Weusthuis",

year = "2015",

doi = "10.3389/fmicb.2015.00849",

language = "English",

volume = "6",

journal = "Frontiers in Microbiology",

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publisher = "Frontiers",

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TY - JOUR

T1 - Heterologous expression of Mus musculus immunoresponsive gene 1 (irg1) in Escherichia coli results in itaconate production

AU - Vuoristo, K.S.

AU - Mars, A.E.

AU - Loon, S.

AU - Orsi, E.

AU - Eggink, G.

AU - Sanders, J.P.M.

AU - Weusthuis, R.A.

PY - 2015

Y1 - 2015

N2 - Itaconic acid, a C5-dicarboxylic acid, is a potential biobased building block for the polymer industry. It is obtained from the citric acid cycle by decarboxylation of cis-aconitic acid. This reaction is catalyzed by CadA in the native itaconic acid producer Aspergillus terreus. Recently, another enzyme encoded by the mammalian immunoresponsive gene 1 (irg1), was found to decarboxylate cis-aconitate to itaconate in vitro. We show that heterologous expression of irg1 enabled itaconate production in Escherichia coli with production titres up to 560 mg/L.

AB - Itaconic acid, a C5-dicarboxylic acid, is a potential biobased building block for the polymer industry. It is obtained from the citric acid cycle by decarboxylation of cis-aconitic acid. This reaction is catalyzed by CadA in the native itaconic acid producer Aspergillus terreus. Recently, another enzyme encoded by the mammalian immunoresponsive gene 1 (irg1), was found to decarboxylate cis-aconitate to itaconate in vitro. We show that heterologous expression of irg1 enabled itaconate production in Escherichia coli with production titres up to 560 mg/L.

KW - codon usage frequencies

KW - aspergillus-terreus

KW - acid production

KW - protein expression

KW - niger

KW - host

U2 - 10.3389/fmicb.2015.00849

DO - 10.3389/fmicb.2015.00849

M3 - Article

VL - 6

JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

SN - 1664-302X

M1 - 849

ER -