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Molecular analysis of a plasmid-encoded phenol hydroxylase from Pseudomonas CF600.
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).ORCID iD: 0000-0002-7349-1678
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1989 (English)In: Journal of general microbiology, ISSN 0022-1287, Vol. 135, no 5Article in journal (Refereed) Published
Abstract [en]

Pseudomonas strain CF600 is able to utilize 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.

Place, publisher, year, edition, pages
1989. Vol. 135, no 5
National Category
Natural Sciences
URN: urn:nbn:se:umu:diva-112354DOI: 10.1099/00221287-135-5-1083PubMedID: 2559941OAI: diva2:877214
Available from: 2015-12-06 Created: 2015-12-06 Last updated: 2015-12-06

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Shingler, V
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Department of Molecular Biology (Faculty of Science and Technology)
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