PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC39723, is a novel type of ring-cleavage dioxygenase
PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC39723, is a novel type of ring-cleavage dioxygenase
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DOI：
10.1016/s0014-5793(99)01305-8
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发表时间：
1999-10-15
期刊：
影响因子：
3.5
通讯作者：
Takagi, M
中科院分区：
文献类型：
--
作者：
Ohtsubo, Y;Miyauchi, K;Takagi, M
五氯苯酚矿化细菌Sphingomonashlorophenolica ATCC 39723通过2，6-二氯氢醌（2，6-DCHQ）降解五氯苯酚。之前已经确定了将五氯苯酚转化为2，6-DCHQ的途径;然而，2，6-DCHQ以外的途径尚不清楚，尽管有人认为PcpA在2，6-DCHQ转化中起作用。在这项研究中，在大肠杆菌中表达的PcpA被纯化到同质，并显示出与氢醌衍生物结合具有新的环裂解双加氧酶活性，并将2，6-DCHQ转化为2-氯马来酰乙酸。(C)1999年欧洲生物化学学会联合会。
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. (C) 1999 Federation of European Biochemical Societies.