Molecular characterisation of a Rhodococcus ohp operon

Justin A C Powell, John Archer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The ohp operon of Rhodococcus strain V49 consists of five genes, ohpR, ohpA, ohpB, ohpC and ohpD which encode putative regulator and transport proteins and confirmed monooxygenase, hydroxymuconic semialdehyde hydrolase and catechol 2,3-dioxygenase enzymes, respectively. These enzymes catalyse the conversion of 3-(2-hydroxyphenyl) propionic acid to the corresponding linear product via a meta-cleavage pathway. Confirmation that the ohp gene cluster formed an operon was provided by gene disruption during which expression of Bacillus levansucrase was confirmed in Rhodococcus. Following biochemical assays of cell-free extracts from recombinant Escherichia coli expressing ohpB (monooxygenase), ohpC (hydroxymuconic-semialdehyde hydrolase) and ohpD (catechol 2,3-dioxygenase), the ortho-hydroxyphenylpropionic acid catabolic pathway in Rhodococcus strain V49 (ATCC 19070) has been predicted.

Original languageEnglish (US)
Pages (from-to)175-188
Number of pages14
JournalAntonie van Leeuwenhoek, International Journal of General and Molecular Microbiology
Volume74
Issue number1-3
DOIs
StatePublished - Dec 1 1998

Keywords

  • Catechol 2,3-dioxygenase
  • Gene disruption
  • Hydroxymuconicsemialdehyde hydrolase
  • Monooxygenase operon
  • Rhodococcus

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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