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PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC39723, is a novel type of ring‐cleavage dioxygenase
Author(s) -
Ohtsubo Yoshiyuki,
Miyauchi Keisuke,
Kanda Kenji,
Hatta Takashi,
Kiyohara Houzo,
Senda Toshiya,
Nagata Yuji,
Mitsui Yukio,
Takagi Masamichi
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01305-8
Subject(s) - pentachlorophenol , dioxygenase , sphingomonas , oxygenase , cleavage (geology) , chemistry , stereochemistry , hydroquinone , escherichia coli , biochemistry , enzyme , biology , organic chemistry , gene , paleontology , 16s ribosomal rna , fracture (geology)
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.