Purification of two isofunctional hydrolases (EC 3.7.1.8) in the degradative pathway for dibenzofuran inSphingomonas sp. strain RW1 |
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Authors: | Patricia V. Bünz Rocco Falchetto Alasdair M. Cook |
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Affiliation: | (1) Institute of Microbiology, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092 Zürich, Switzerland;(2) Institute of Biochemistry, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092 Zürich, Switzerland;(3) Institut für Allgemeine Botanik, Abteilung Mikrobiologie, Universität Hamburg, D-22609 Hamburg, Germany |
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Abstract: | Sphingomonas sp. strain RW1, when grown in salicylate-salts medium, synthesized the enzymes for the degradation of dibenzofuran. The reaction subsequent tometa cleavage of the first benzene ring was found to be catalyzed by two isofunctional hydrolases, H1 and H2, which were purified by chromatography on anion exchange, hydrophobic interaction and gel filtration media. Each enzyme was able to hydrolze 2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate and 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate to produce salicylate and benzoate, respectively. SDS/PAGE of each purified enzyme showed a single band ofMr31 000 (H1) or 29 000 (H2). The N-terminal amino acid sequences of the two proteins showed 50% homology.Abbreviations DHB 2,3-dihydroxybiphenyl - DSM German Culture Collection (Braunschweig) - FPLC protein liquid chromatograph(y) - HOHPDA 2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate - HOPDA 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate - THB 2,2,3-trihydroxybiphenyl |
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Keywords: | dibenzofuran metabolism of dibenzofuran pathway intermediates 2,2 /content/m582841g30054586/xxlarge8242.gif" alt=" prime" align=" BASELINE" BORDER=" 0" >,3-trihydroxybiphenyl meta cleavage enzymes hydrolysis of a C-C bond (EC 3.7.1.8) HOHPDA hydrolases (EC 3.7.1.8) |
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