Molecular analysis of a plasmid-encoded phenol hydroxylase from Pseudomonas CF600

V. Shingler, C. H. Franklin, M. Tsuda, D. Holroyd, M. Bagdasarian

    Research output: Contribution to journalArticlepeer-review

    88 Citations (Scopus)


    Pseudomonas strain CF600 is able to ultilize phenol and 3,4-dimethylphenol as sole carbon and energy source. We demonstrate that growth on these substrates is by virtue of plasmid-encoded phenol hydroxylase and a meta-cleavage pathway. Screening of a genomic bank, with DNA from the previously cloned catechol 2,3-dioxygenase gene of the TOL plasmid pWW0, was used in the identification of a clone which could complement a phenol-hydroxylase-deficient transposon insertion mutant. Deletion mapping and polypeptide production analysis identified a 1.2 kb region of DNA encoding a 39.5 kDa polypeptide which mediated this complementation. Enzyme activities and growth properties of Pseudomonas strains harbouring this fragment on a broad-host-range expression vector indicate that phenol hydroxylase is a multicomponent enzyme containing the 39.5 kDa polypeptide as one component.

    Original languageEnglish
    Pages (from-to)1083-1092
    Number of pages10
    JournalJournal of General Microbiology
    Issue number5
    Publication statusPublished - 1989

    ASJC Scopus subject areas

    • Microbiology

    Fingerprint Dive into the research topics of 'Molecular analysis of a plasmid-encoded phenol hydroxylase from Pseudomonas CF600'. Together they form a unique fingerprint.

    Cite this