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The Questor Centre, David Keir Building, The Queen's University of Belfast, Belfast BT9 5AG, UK and School of Biology and Biochemistry, Medical Biology Centre, The Queen's University of Belfast, Belfast BT9 7BL, UK
Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Science, Pushchino, Moscow region, Russia
ABSTRACT
Four extradiol dioxygenase genes which encode enzymes active against catechol and substituted catechols were cloned from two different Rhodococcus strains, and their nucleotide sequences were determined. A catechol 2,3-dioxygenase gene (edoC) was shown to be identical to the previously described ipbC gene from the isopropylbenzene operon of Rhodococcus erythropolis. Amino acid sequences deduced from the three other genes (edoA, edoB and edoD) were shown to have various degrees of homology to different extradiol dioxygenases. The EdoA and EdoB dioxygenases were classified as belonging to the third family of type I oxygenases and represented two new subfamilies, whereas the EdoD dioxygenase was a type II enzyme. Analysis of six Rhodococcus strains revealed a wide distribution of the above dioxygenase genes. Rhodococcus sp. I1 was shown to harbour all four of the analysed dioxygenase genes. Nucleotide sequences homologous to the edoB gene were present in all of the strains, including R. erythropolis NCIMB 13065, which did not utilize any of the aromatic compounds analysed. The latter finding points to the existence of a silent pathway(s) for degradation of aromatic compounds in this Rhodococcus strain.
*Author for correspondence: Leonid A. Kulakov (Questor Centre). Tel: +44 1232 335577. Fax: +44 1232 661462. e-mail: l.kulakov@queens-belfast.ac.uk
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