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

Research output: Contribution to journal › Article › peer-review

60 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 language	English
Pages (from-to)	395-398
Number of pages	4
Journal	FEBS Letters
Volume	459
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(99)01305-8
Publication status	Published - 1999 Oct 15
Externally published	Yes

Keywords

Biodegradation
Pentachlorophenol
Ring-cleavage dioxygenase
Sphingomonas

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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@article{3b75bfea6e874529af14084da7723fe8,

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.",

year = "1999",

month = oct,

day = "15",

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

language = "English",

volume = "459",

pages = "395--398",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "3",

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TY - JOUR

T1 - PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC39723, is a novel type of ring-cleavage dioxygenase

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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U2 - 10.1016/S0014-5793(99)01305-8

DO - 10.1016/S0014-5793(99)01305-8

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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