Specificity of Catechol ortho-Cleavage during para-Toluate Degradation by Rhodococcus opacus 1cp

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M. M. Suvorova¹, I. P. Solyanikova², and L. A. Golovleva^1,2*

¹Pushchino State University, 142290 Pushchino, Moscow Region, Russia

²Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: Golovleva@IBPM.Pushchino.ru

^* To whom correspondence should be addressed.

Received May 23, 2006; Revision received June 23, 2006

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Degradation of para-toluate by Rhodococcus opacus 1cp was investigated. Activities of the key enzymes of this process, catechol 1,2-dioxygenase and muconate cycloisomerase, are detected in this microorganism. Growth on p-toluate was accompanied by induction of two catechol 1,2-dioxygenases. The substrate specificity and physicochemical properties of one enzyme are identical to those of chlorocatechol 1,2-dioxygenase; induction of the latter enzyme was observed during R. opacus 1cp growth on 4-chlorophenol. The other enzyme isolated from the biomass grown on p-toluate exhibited lower rate of chlorinated substrate cleavage compared to the catechol substrate. However, this enzyme is not identical to the catechol 1,2-dioxygenase cloned in this strain within the benzoate catabolism operon. This supports the hypothesis on the existence of multiple forms of dioxygenases as adaptive reactions of microorganisms in response to environmental stress.

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KEY WORDS: para-toluate, degradation, catechol 1,2-dioxygenase, muconate cycloisomerase, Rhodococcus opacus 1cp

DOI: 10.1134/S0006297906120054

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