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

FEBS Letters

Hatta, Takashi³  Nagata, Yuji¹  Takagi, Masamichi¹  Ohtsubo, Yoshiyuki¹  Mitsui, Yukio²  Kanda, Kenji²  Kiyohara, Houzo³  Senda, Toshiya²  Miyauchi, Keisuke¹ 

[1] Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan;Department of BioEngineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan;Central Research Institute, Okayama University of Science, Seki 401-1, Okayama 703, Japan

关键词: Pentachlorophenol;    Ring-cleavage dioxygenase;    Biodegradation;    Sphingomonas;    HQ;    hydroquinone;    CHQ;    chlorohydroquinone;    2;    6-DCHQ;    2;    6-dichlorohydroquinone;    PCP;    pentachlorophenol;    TeCHQ;    tetrachlorohydroquinone;    TrCHQ;    trichlorohydroquinone;   

DOI  :  10.1016/S0014-5793(99)01305-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown