PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC39723, is a novel type of ring-cleavage dioxygenase.
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.
Ohtsubo
Y
Y
Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, Japan.
Miyauchi
K
K
Kanda
K
K
Hatta
T
T
Kiyohara
H
H
Senda
T
T
Nagata
Y
Y
Mitsui
Y
Y
Takagi
M
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli; D006873:Hydroquinones / Q000378:metabolism; D008298:Maleates / Q000378:metabolism; D008969:Molecular Sequence Data; D010105:Oxygenases; D010416:Pentachlorophenol / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D020578:Sphingomonas / Q000201:enzymology*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D006873:Hydroquinones; D008298:Maleates; C104629:2,6-dichloro-4-hydroquinone; C079154:2-chloromaleylacetate; D010416:Pentachlorophenol; C499564:PcpA protein, Sphingomonas; D010105:Oxygenases; C031927:hydroquinone