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J. Bacteriol., Jan 1995, 229-234, Vol 177, No. 1
Copyright © 1995, American Society for Microbiology

Purification and characterization of 6-chlorohydroxyquinol 1,2- dioxygenase from Streptomyces rochei 303: comparison with an analogous enzyme from Azotobacter sp. strain GP1

O Zaborina, M Latus, J Eberspacher, LA Golovleva and F Lingens
Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino.

The enzyme which cleaves the benzene ring of 6-chlorohydroxyquinol was purified to apparent homogeneity from an extract of 2,4,6- trichlorophenol-grown cells of Streptomyces rochei 303. Like the analogous enzyme from Azotobacter sp. strain GP1, it exhibited a highly restricted substrate specificity and was able to cleave only 6- chlorohydroxyquinol and hydroxyquinol and not catechol, chlorinated catechols, or pyrogallol. No extradiol-cleaving activity was observed. In contrast to 6-chlorohydroxyquinol 1,2-dioxygenase from Azotobacter sp. strain GP1, the S. rochei enzyme had a distinct preference for 6- chlorohydroxyquinol over hydroxyquinol (kcat/Km = 1.2 and 0.57 s- 1.microM-1, respectively). The enzyme from S. rochei appears to be a dimer of two identical 31-kDa subunits. It is a colored protein and was found to contain 1 mol of iron per mol of enzyme. The NH2-terminal amino acid sequences of 6-chlorohydroxyquinol 1,2-dioxygenase from S. rochei 303 and from Azotobacter sp. strain GP1 showed a high degree of similarity.

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