Publikation: Purification of two isofunctional hydrolases (EC 3.7.1.8) in the degradative pathway for dibenzofuran in Sphingomonas sp. strain RW1
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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 ofM r 31 000 (H1) or 29 000 (H2). The N-terminal amino acid sequences of the two proteins showed 50% homology.
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BÜNZ, Patricia V., Rocco FALCHETTO, Alasdair M. COOK, 1993. Purification of two isofunctional hydrolases (EC 3.7.1.8) in the degradative pathway for dibenzofuran in Sphingomonas sp. strain RW1. In: Biodegradation. 1993, 4(3), pp. 171-178. ISSN 0923-9820. eISSN 1572-9729. Available under: doi: 10.1007/BF00695119BibTex
@article{Bunz1993Purif-7102, year={1993}, doi={10.1007/BF00695119}, title={Purification of two isofunctional hydrolases (EC 3.7.1.8) in the degradative pathway for dibenzofuran in Sphingomonas sp. strain RW1}, number={3}, volume={4}, issn={0923-9820}, journal={Biodegradation}, pages={171--178}, author={Bünz, Patricia V. and Falchetto, Rocco and Cook, Alasdair M.} }
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