Modifying monooxygenases for biosynthesis

Research output: Contribution to specialist publicationArticle


Variants of three different monooxygenase enzymes were used to transform aromatics. Modification of the gene encoding 2,4-dinitrotoluene dioxygenase (DDO) of Burkholderia cepacia R34 at one amino acid position, increased the enzyme's activity with o-nitrophenol 47 fold, m-nitrophenol 34 fold, and o-methoxyphenol 174 fold. The modified enzyme also expanded its substrate range to include m-methoxyphenol, o-cresol, and m-cresol. Toluene-o-xylene monooxygenase from a different bacterium, Pseudomonas stutzeri OX1, oxidized toluene to 3- and 4-methylcatechol and benzene to phenol. Gene shuffling and amino acid modification generated mutants that synthesize novel dihydroxy and trihydroxy derivatives of benzene and toluene.

Original languageEnglish (US)
Number of pages1
Specialist publicationIndustrial Bioprocessing
StatePublished - Jul 2004

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • General Chemical Engineering
  • Organic Chemistry


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