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Journal of Bacteriology, March 1999, p. 1444-1450, Vol. 181, No. 5
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

3-Hydroxylaminophenol Mutase from Ralstonia eutropha JMP134 Catalyzes a Bamberger Rearrangement

Andreas Schenzle,1,2,dagger Hiltrud Lenke,1 Jim C. Spain,3 and Hans-Joachim Knackmuss1,2,*

Fraunhofer Institut für Grenzflächen- und Bioverfahrenstechnik1 and Institut für Mikrobiologie der Universität Stuttgart,2 D-70569 Stuttgart, Germany, and Armstrong Laboratory, AFRL/MRLQ, Tyndall Air Force Base, Florida 32403-53193

Received 1 July 1998/Accepted 20 October 1998

3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134 is involved in the degradative pathway of 3-nitrophenol, in which it catalyzes the conversion of 3-hydroxylaminophenol to aminohydroquinone. To show that the reaction was really catalyzed by a single enzyme without the release of intermediates, the corresponding protein was purified to apparent homogeneity from an extract of cells grown on 3-nitrophenol as the nitrogen source and succinate as the carbon and energy source. 3-Hydroxylaminophenol mutase appears to be a relatively hydrophobic but soluble and colorless protein consisting of a single 62-kDa polypeptide. The pI was determined to be at pH 4.5. In a database search, the NH2-terminal amino acid sequence of the undigested protein and of two internal sequences of 3-hydroxylaminophenol mutase were found to be most similar to those of glutamine synthetases from different species. Hydroxylaminobenzene, 4-hydroxylaminotoluene, and 2-chloro-5-hydroxylaminophenol, but not 4-hydroxylaminobenzoate, can also serve as substrates for the enzyme. The enzyme requires no oxygen or added cofactors for its reaction, which suggests an enzymatic mechanism analogous to the acid-catalyzed Bamberger rearrangement.

* Corresponding author. Mailing address: Institut für Mikrobiologie der Universität Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany. Phone: (49) 711 685 5487. Fax: (49) 711 685 5725. E-mail: imbhjk{at}po.uni-stuttgart.de.

dagger Present address: Central Research & Development Department, DuPont Co., Wilmington, DE 19898.

Journal of Bacteriology, March 1999, p. 1444-1450, Vol. 181, No. 5
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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