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Specificity of catechol ortho-cleavage during para-toluate degradation by Rhodococcus opacus 1cp

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Abstract

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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Abbreviations

(C)Cat:

(chloro)catechol

(C)C-1,2-DO:

(chloro)catechol 1,2-dioxygenase

4-CP:

4-chlorophenol

MCI:

muconate cycloisomerase

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Authors and Affiliations

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

    M. M. Suvorova & L. A. Golovleva

  2. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia

    I. P. Solyanikova & L. A. Golovleva

Authors
  1. M. M. Suvorova
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  2. I. P. Solyanikova
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  3. L. A. Golovleva
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Corresponding author

Correspondence to L. A. Golovleva.

Additional information

Original Russian Text © M. M. Suvorova, I. P. Solyanikova, L. A. Golovleva, 2006, published in Biokhimiya, 2006, Vol. 71, No. 12, pp. 1618–1626.

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Suvorova, M.M., Solyanikova, I.P. & Golovleva, L.A. Specificity of catechol ortho-cleavage during para-toluate degradation by Rhodococcus opacus 1cp. Biochemistry (Moscow) 71, 1316–1323 (2006). https://doi.org/10.1134/S0006297906120054

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  • DOI: https://doi.org/10.1134/S0006297906120054

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