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Dienelactone hydrolase from Rhodococcus erythropolis 1 CP: purification and properties

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Abstract

Dienelactone hydrolases (EC 3.1.1.45) have been shown to play an indispensable role in the degradation of chloroaromatic compounds via ortho-cleavage of chlorocatechols. We report on the purification of dienelactone hydrolase of the chlorophenol-utilizing strain Rhodococcus erythropolis 1CP to apparent homogeneity. Dienelactone hydrolase differed fron the corresponding enzymes of other chloroaromatic compound-catabolizing strains in being restricted to substrates with a cis-dienelactone structure. From the cis-dienelactone-hydrolyzing enzyme of a 4-fluorobenzoate-utilizing Burkholderia (Pseudomonas) cepacia strain, it differed considerably in properties such as pH optimum of activity, inhibition by p-chloromercuribenzoate, and amino acid composition. Thus, there is not necessarily a close relationship between substrate specificity and other properties of dienelactone hydrolases.

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Author notes

  1. Olga V. Maltseva

    Present address: Department of Microbiology, Michigan State University, 40 Giltner Hall, 48 824, East Lansing, MI, USA

Authors and Affiliations

  1. Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142292, Pushchino, Moscow Region, Russia

    Olga V. Maltseva, Inna P. Solyanikova & Ludmila A. Golovleva

  2. Institut für Mikrobiologie der Universität Stuttgart, Allmandring 31, D-70569, Stuttgart, Germany

    Michael Schlömann & Hans-Joachim Knackmuss

Authors
  1. Olga V. Maltseva
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  2. Inna P. Solyanikova
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  3. Ludmila A. Golovleva
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  4. Michael Schlömann
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  5. Hans-Joachim Knackmuss
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Correspondence to Olga V. Maltseva.

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Maltseva, O.V., Solyanikova, I.P., Golovleva, L.A. et al. Dienelactone hydrolase from Rhodococcus erythropolis 1 CP: purification and properties. Arch. Microbiol. 162, 368–374 (1994). https://doi.org/10.1007/BF00263786

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  • DOI: https://doi.org/10.1007/BF00263786

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