Generation of a catR deficient mutant of P. putida KT2440 that produces cis, cis-muconate from benzoate at high rate and yield

Duuren, J.B.J.H. van; Wijte, Dorien; Leprince, Audrey; Karge, Bianka; Puchałka, Jacek; Wery, Jan; Santos, Vítor A. P. Martins dos; Eggink, Gerrit; Mars, Astrid E.

doi:10.1016/j.jbiotec.2011.08.030

Cited by 43 publications

(39 citation statements)

References 48 publications

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“…It also shows poor kinetic parameters when compared with CatA, something that is supported by other works reporting similar differences (Nakai et al ., ; van Duuren et al ., ). Furthermore, catA2 does not have a detectable role in controlling transcription of the ben and cat operons (http://onlinelibrary.wiley.com/doi/10.1111/1462-2920.12361/suppinfo) and does not affect either the transcriptome (van Duuren et al ., ) or the proteome (Yun et al ., ) of P. putida KT2440 growing on benzoate as sole carbon source. In contrast, CatA2 clearly helps to keep intracellular concentrations of catechol low, plausibly preventing its toxicity (Fig.…”

Section: Discussionmentioning

confidence: 97%

A second chromosomal copy of the catA gene endows Pseudomonas putida mt‐2 with an enzymatic safety valve for excess of catechol

Jiménez

Pérez‐Pantoja

Chavarría

et al. 2014

Environmental Microbiology

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Pseudomonas putida mt-2 harbours two different routes for catabolism of catechol, namely one meta pathway encoded by the xyl genes of the TOL plasmid pWW0 and one ortho pathway determined by the chromosomal ben and cat genes. P. putida mt-2 has a second chromosomal copy of the catA gene (named catA2) located downstream of the ben operon that encodes an additional catechol-1,2-dioxygenase. The metabolic and regulatory phenotypes of strains lacking one enzyme, the other and both of them in cells with and without the TOL plasmid were evaluated. The data consistently indicated that induction of the ortho pathway by benzoate plasmid-less strain P. putida KT2440 led to catechol surplus, the toxicity of which at high concentrations being counteracted by CatA2. Cells carrying pWW0 but lacking catA2 experienced both a rapid loss of the plasmid when grown on benzoate (a substrate of the lower pathway) and a slowdown of their growth rate when cultured with benzylalcohol (a substrate converted to benzoate by the upper pathway). These data reveal the role of CatA2 as a type of metabolic safety valve for excess catechol that alleviates the metabolic conflict generated by simultaneous expression of the meta and ortho pathways, thereby facilitating their co-existence.

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Section: Discussionmentioning

confidence: 97%

A second chromosomal copy of the catA gene endows Pseudomonas putida mt‐2 with an enzymatic safety valve for excess of catechol

Jiménez

Pérez‐Pantoja

Chavarría

et al. 2014

Environmental Microbiology

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“…Some bacteria can convert benzoic acid to catechol via benzoate 1,2-dioxygenase and 1,2-dihydroxybenzoate dehydrogenase, and further metabolize catechol via ccMA by the beta-ketoadipate pathway (Harwood and Parales, 1996;Polen et al, 2013). The production of ccMA from benzoic acid by microbial action has also been reported (van Duuren et al, 2011(van Duuren et al, , 2012Polen et al, 2013). Although this represents a bioconversion process, the benzoic acid source has typically been petroleum-based and it is preferable to use a renewable feedstock.…”

Section: Introductionmentioning

confidence: 99%

Enhancement of protocatechuate decarboxylase activity for the effective production of muconate from lignin-related aromatic compounds

Sonoki

Morooka

Sakamoto

et al. 2014

Journal of Biotechnology

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The decarboxylation reaction of protocatechuate has been described as a bottleneck and a rate-limiting step in cis,cis-muconate (ccMA) bioproduction from renewable feedstocks such as sugar. Because sugars are already in high demand in the development of many bio-based products, our work focuses on improving protocatechuate decarboxylase (Pdc) activity and ccMA production in particular, from lignin-related aromatic compounds. We previously had transformed an Escherichia coli strain using aroY, which had been used as a protocatechuate decarboxylase encoding gene from Klebsiella pneumoniae subsp. pneumoniae A170-40, and inserted other required genes from Pseudomonas putida KT2440, to allow the production of ccMA from vanillin. This recombinant strain produced ccMA from vanillin, however the Pdc reaction step remained a bottleneck during incubation. In the current study, we identify a way to increase protocatechuate decarboxylase activity in E. coli through enzyme production involving both aroY and kpdB; the latter which encodes for the B subunit of 4-hydroxybenzoate decarboxylase. This permits expression of Pdc activity at a level approximately 14-fold greater than the strain with aroY only. The expression level of AroY increased, apparently as a function of the co-expression of AroY and KpdB. Our results also imply that ccMA may inhibit vanillate demethylation, a reaction step that is rate limiting for efficient ccMA production from lignin-related aromatic compounds, so even though ccMA production may be enhanced, other challenges to overcome vanilate demethylation inhibition still remain.

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“…It is useful to note that the presence of chlorcatechol 1,2 dioxygenase was detected for the Pseudomonas sp. XP M2 and P. putida KT2440 but not catechol 2,3 dioxygenase [33,34].…”

Section: Methodsmentioning

confidence: 93%

Degradation of aromatic hydrocarbons by the Rhodococcus wratislaviensis KT112-7 isolated from waste products of a salt-mining plant

Егорова

Korsakova

Демаков

et al. 2013

Appl Biochem Microbiol

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Degradation of aromatic hydrocarbons by the Rhodococcus wratislaviensis KT112 7 isolated from technogenic mineral waste products of the BKRU1 "Uralkalii" plant was investigated (Berezniki, Perm krai). The R. wratislaviensis KT112 7 was shown to utilize increased concentrations of o phthalic (o PA) (8 g/L) and benzoic (BA) (3.4 g/L) acids. The strain grows with o PA, BA, and biphenyl at a NaCl content of up to 75, 90 and 100 g/L in the culture medium, respectively. Based on an analysis of the metabolic profile and nucleotide sequences of the bphA1, benA, and phtB genes, the strain KT112 7 was found to degrade o PA via the formation of 3,4 dihydroxyphthalic and 3,4 dihydroxybenzoic acids. Degradation of biphenyl proceeds via the formation of BA and then at low concentrations of NaCl (up to 50 g/L) via the formation of 4 hydroxy benzoic acid with its subsequent oxidation, while at high concentrations of NaCl (over 60 g/L)-via the direct oxidation of benzoic acid to resultant catechol. These data indicate that the Rhodococcus wratislaviensis KT112 7 is a promising strain in the development of new biotechnologies directed for utilization (transfor mation) of aromatic compounds, including the conditions of increased mineralization.

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Generation of a catR deficient mutant of P. putida KT2440 that produces cis, cis-muconate from benzoate at high rate and yield

Cited by 43 publications

References 48 publications

A second chromosomal copy of the catA gene endows Pseudomonas putida mt‐2 with an enzymatic safety valve for excess of catechol

A second chromosomal copy of the catA gene endows Pseudomonas putida mt‐2 with an enzymatic safety valve for excess of catechol

Enhancement of protocatechuate decarboxylase activity for the effective production of muconate from lignin-related aromatic compounds

Degradation of aromatic hydrocarbons by the Rhodococcus wratislaviensis KT112-7 isolated from waste products of a salt-mining plant

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