Molecular characterisation of a Rhodococcus ohp op...[Antonie Van Leeuwenhoek. 1998 Jul-Oct]

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1: Antonie Van Leeuwenhoek. 1998 Jul-Oct;74(1-3):175-88. Links

Molecular characterisation of a Rhodococcus ohp operon.

Powell JA, Archer JA.

Department of Genetics, University of Cambridge, UK.

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.

PMID: 10068799 [PubMed - indexed for MEDLINE]

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