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

研究成果: Article査読

58 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)395-398
ページ数4
ジャーナルFEBS Letters
459
3
DOI
出版ステータスPublished - 1999 10 15
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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