Suitability of recombinant Escherichia coli and Pseudomonas putida strains for selective biotransformation of m-nitrotoluene by xylene monooxygenase

scientific article published on November 2005

Suitability of recombinant Escherichia coli and Pseudomonas putida strains for selective biotransformation of m-nitrotoluene by xylene monooxygenase is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/AEM.71.11.6624-6632.2005
P932PMC publication ID1287633
P698PubMed publication ID16269690
P5875ResearchGate publication ID7497781

P2093author name stringAndreas Schmid
Bernard Witholt
Daniel Meyer
P2860cites workBiodegradation of aromatic compounds by Escherichia coliQ28208239
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Chemoselective nitro group reduction and reductive dechlorination initiate degradation of 2-chloro-5-nitrophenol by Ralstonia eutropha JMP134.Q39481900
ntn genes determining the early steps in the divergent catabolism of 4-nitrotoluene and toluene in Pseudomonas sp. strain TW3.Q39565502
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A balanced DO-stat and its application to the control of acetic acid excretion by recombinant Escherichia coli.Q54707417
Choice of microbial host for the naphthalene dioxygenase bioconversionQ71398115
TOL plasmid-specified xylene oxygenase is a wide substrate range monooxygenase capable of olefin epoxidationQ72273546
Xylene monooxygenase catalyzes the multistep oxygenation of toluene and pseudocumene to corresponding alcohols, aldehydes, and acids in Escherichia coli JM101Q73615757
Pseudomonas putida--a versatile biocatalystQ78864939
Integrated two-liquid phase bioconversion and product-recovery processes for the oxidation of alkanes: process design and economic evaluationQ95305825
P433issue11
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
Pseudomonas putidaQ2738168
P304page(s)6624-6632
P577publication date2005-11-01
P1433published inApplied and Environmental MicrobiologyQ4781593
P1476titleSuitability of recombinant Escherichia coli and Pseudomonas putida strains for selective biotransformation of m-nitrotoluene by xylene monooxygenase
P478volume71

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cites work (P2860)
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