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首页> 外文期刊>FEBS Letters >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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PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC39723, is a novel type of ring‐cleavage dioxygenase

机译:PcpA是一种新型的环裂解双加氧酶,它参与了鞘氨醇单胞菌ATCC39723中五氯酚的降解。

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>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.
机译:>五氯酚(PCP)矿化细菌 Sphingomonas chlorophenolica ATCC39723通过2,6-二氯氢醌(2,6-DCHQ)降解PCP。先前已经建立了将PCP转换为2,6-DCHQ的途径。然而,尽管有人提出PcpA在2,6-DCHQ转换中起作用,但尚不清楚2,6-DCHQ以外的途径。在这项研究中,在大肠杆菌中表达的PcpA被纯化至均质,并与氢醌衍生物结合后具有新颖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。

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