Production of mesaconate in Escherichia coli by engineered glutamate mutase pathway

Wang, Jingyu; Zhang, Kechun

doi:10.1016/j.ymben.2015.06.001

Cited by 30 publications

(27 citation statements)

References 44 publications

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“…Mesaconic, itaconic, methylsuccinic and other C 5 -dicarboxylic acids are regarded as important platform chemicals [ 64 , 65 , 66 ], and their bioproduction is currently being optimized [ 65 , 66 , 67 , 68 ]. The promiscuity of class I fumarases can therefore be important for the optimization of production of these compounds, but also for engineering of ( S )-citramalate producing strains.…”

Section: Discussionmentioning

confidence: 99%

Mesaconase/Fumarase FumD in Escherichia coli O157:H7 and Promiscuity of Escherichia coli Class I Fumarases FumA and FumB

Kronen

Berg

2015

PLoS ONE

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Mesaconase catalyzes the hydration of mesaconate (methylfumarate) to (S)-citramalate. The enzyme participates in the methylaspartate pathway of glutamate fermentation as well as in the metabolism of various C5-dicarboxylic acids such as mesaconate or L-threo-β-methylmalate. We have recently shown that Burkholderia xenovorans uses a promiscuous class I fumarase to catalyze this reaction in the course of mesaconate utilization. Here we show that classical Escherichia coli class I fumarases A and B (FumA and FumB) are capable of hydrating mesaconate with 4% (FumA) and 19% (FumB) of the catalytic efficiency k cat/K m, compared to the physiological substrate fumarate. Furthermore, the genomes of 14.8% of sequenced Enterobacteriaceae (26.5% of E. coli, 90.6% of E. coli O157:H7 strains) possess an additional class I fumarase homologue which we designated as fumarase D (FumD). All these organisms are (opportunistic) pathogens. fumD is clustered with the key genes for two enzymes of the methylaspartate pathway of glutamate fermentation, glutamate mutase and methylaspartate ammonia lyase, converting glutamate to mesaconate. Heterologously produced FumD was a promiscuous mesaconase/fumarase with a 2- to 3-fold preference for mesaconate over fumarate. Therefore, these bacteria have the genetic potential to convert glutamate to (S)-citramalate, but the further fate of citramalate is still unclear. Our bioinformatic analysis identified several other putative mesaconase genes and revealed that mesaconases probably evolved several times from various class I fumarases independently. Most, if not all iron-dependent fumarases, are capable to catalyze mesaconate hydration.

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Section: Discussionmentioning

confidence: 99%

Mesaconase/Fumarase FumD in Escherichia coli O157:H7 and Promiscuity of Escherichia coli Class I Fumarases FumA and FumB

Kronen

Berg

2015

PLoS ONE

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“…Mesaconate production relies on several natural pathways for glutamate catabolism and/or carbon fixation (Figure 1N), wherein a mutase converts glutamate to methyl aspartate, which through the action of a methyl aspartase is converted to mesaconate . Similarly to the HIBA-CoA mutase described above, the glutamate mutase is also a B12 dependent enzyme reliant on free radical chemistry and requires vitamin supplementation and continuous enzyme reactivation (Chih and Marsh, 2000;Wang and Zhang, 2015). Methyl Methacrylic acid production 0.0146g/L (E. coli) 0.0007 g/L-h 0.62% bioprocess yield Rates, yields, engineering resistance NA aspartase shares a reaction mechanism with aspartases converting aspartate to fumarate (de Villiers et al, 2012).…”

Section: Mesaconic Acidmentioning

confidence: 99%

A Review of the Biotechnological Production of Methacrylic Acid

Lebeau

Efromson

Lynch

2020

Front. Bioeng. Biotechnol.

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Industrial biotechnology can lead to new routes and potentially to more sustainable production of numerous chemicals. We review the potential of biobased routes from sugars to the large volume commodity, methacrylic acid, involving fermentation based bioprocesses. We cover the key progress over the past decade on direct and indirect fermentation based routes to methacrylic acid including both academic as well as patent literature. Finally, we take a critical look at the potential of biobased routes to methacrylic acid in comparison with both incumbent as well as newer greener petrochemical based processes.

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“…SeveralA TP-recyclinge nzyme systems are availablea nd af ew have already been successfully implemented in preparative biocatalysis. [26][27][28] However,c onsidering that the starting materials (fumarate and mesaconate) can be efficiently produced in high yields by large-scale fermentation using metabolicallye ngineered E. coli strains, [29,30] we envision to co-express the enzymes employed for the cascade in such a fermentation host to directly obtain vitaminB 5 and its amethyl-substitutedd erivatives from cheap carbon and nitrogen sources. Indeed, such ac ell-baseda pproach would eliminate the need for ATPr ecycling.…”

Section: Figuress18 Ands 25 In the Supporting Information)mentioning

confidence: 99%

Modular Enzymatic Cascade Synthesis of Vitamin B₅ and Its Derivatives

Abidin

Saravanan

Zhang

et al. 2018

Chemistry A European J

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Access to vitamin B [(R)-pantothenic acid] and both diastereoisomers of α-methyl-substituted vitamin B [(R)- and (S)-3-((R)-2,4-dihydroxy-3,3-dimethylbutanamido)-2-methylpropanoic acid] was achieved using a modular three-step biocatalytic cascade involving 3-methylaspartate ammonia lyase (MAL), aspartate-α-decarboxylase (ADC), β-methylaspartate-α-decarboxylase (CrpG) or glutamate decarboxylase (GAD), and pantothenate synthetase (PS) enzymes. Starting from simple non-chiral dicarboxylic acids (either fumaric acid or mesaconic acid), vitamin B and both diastereoisomers of α-methyl-substituted vitamin B , which are valuable precursors for promising antimicrobials against Plasmodium falciparum and multidrug-resistant Staphylococcus aureus, can be generated in good yields (up to 70 %) and excellent enantiopurity (>99 % ee). This newly developed cascade process may be tailored and used for the biocatalytic production of various vitamin B derivatives by modifying the pantoyl or β-alanine moiety.

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Production of mesaconate in Escherichia coli by engineered glutamate mutase pathway

Cited by 30 publications

References 44 publications

Mesaconase/Fumarase FumD in Escherichia coli O157:H7 and Promiscuity of Escherichia coli Class I Fumarases FumA and FumB

Mesaconase/Fumarase FumD in Escherichia coli O157:H7 and Promiscuity of Escherichia coli Class I Fumarases FumA and FumB

A Review of the Biotechnological Production of Methacrylic Acid

Modular Enzymatic Cascade Synthesis of Vitamin B₅ and Its Derivatives

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Production of mesaconate in Escherichia coli by engineered glutamate mutase pathway

Cited by 30 publications

References 44 publications

Mesaconase/Fumarase FumD in Escherichia coli O157:H7 and Promiscuity of Escherichia coli Class I Fumarases FumA and FumB

Mesaconase/Fumarase FumD in Escherichia coli O157:H7 and Promiscuity of Escherichia coli Class I Fumarases FumA and FumB

A Review of the Biotechnological Production of Methacrylic Acid

Modular Enzymatic Cascade Synthesis of Vitamin B5 and Its Derivatives

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Modular Enzymatic Cascade Synthesis of Vitamin B₅ and Its Derivatives