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

doi:10.1016/S0014-5793(99)01305-8

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

45 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
巻	459
号	3
DOI	https://doi.org/10.1016/S0014-5793(99)01305-8
出版ステータス	Published - 1999 10月 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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10.1016/S0014-5793(99)01305-8

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引用スタイル

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

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.",

keywords = "Biodegradation, Pentachlorophenol, Ring-cleavage dioxygenase, Sphingomonas",

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

note = "Funding Information: We thank R.L. Crawford for the kind gift of S. chlorophenolica ATCC39723. Y.O. and K.M. are financially supported by research fellowships of the Japan Society for the Promotion of Science for Young Scientists. This work was supported in part by a Grant-in-Aid from the Ministry of Education, Science and Culture of Japan. This work was performed using the facilities of the Biotechnology Research Center, The University of Tokyo.",

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doi = "10.1016/S0014-5793(99)01305-8",

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AU - Ohtsubo, Yoshiyuki

AU - Miyauchi, Keisuke

AU - Kanda, Kenji

AU - Hatta, Takashi

AU - Kiyohara, Houzo

AU - Senda, Toshiya

AU - Nagata, Yuji

AU - Mitsui, Yukio

AU - Takagi, Masamichi

N1 - Funding Information: We thank R.L. Crawford for the kind gift of S. chlorophenolica ATCC39723. Y.O. and K.M. are financially supported by research fellowships of the Japan Society for the Promotion of Science for Young Scientists. This work was supported in part by a Grant-in-Aid from the Ministry of Education, Science and Culture of Japan. This work was performed using the facilities of the Biotechnology Research Center, The University of Tokyo.

PY - 1999/10/15

Y1 - 1999/10/15

N2 - 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.

AB - 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.

KW - Biodegradation

KW - Pentachlorophenol

KW - Ring-cleavage dioxygenase

KW - Sphingomonas

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