PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC39723, is a novel type of ring-cleavage dioxygenase

Yoshiyuki Ohtsubo, Keisuke Miyauchi, Kenji Kanda, Takashi Hatta, Houzo Kiyohara, Toshiya Senda, Yuji Nagata, Yukio Mitsui, Masamichi Takagi

Research output: Contribution to journalArticlepeer-review

56 Citations (Scopus)

Abstract

The pentachlorophenol (PCP) mineralizing bacterium Sphingomonas chlorophenolica ATCC39723 degrades PCP via 2,6-dichlorohydroquinone (2,6-DCHQ). The pathway converting PCP to 2,6-DCHQ has been established previously; however, the pathway beyond 2,6-DCHQ is not clear, although it has been suggested that a PcpA plays a role in 2,6-DCHQ conversion. In this study, PcpA expressed in Escherichia coli was purified to homogeneity and shown to have novel ring-cleavage dioxygenase activity in conjunction with hydroquinone derivatives, and converting 2,6-DCHQ to 2-chloromaleylacetate. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)395-398
Number of pages4
JournalFEBS Letters
Volume459
Issue number3
DOIs
Publication statusPublished - 1999 Oct 15

Keywords

  • Biodegradation
  • Pentachlorophenol
  • Ring-cleavage dioxygenase
  • Sphingomonas

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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