Mutational analysis of pcpA and its role in pentachlorophenol degradation by Sphingomonas (Flavobacterium) chlorophenolica ATCC 39723

Chanama, Suchart; Crawford, Ronald L.

doi:10.1128/aem.63.12.4833-4838.1997

Cited by 27 publications

(8 citation statements)

References 28 publications

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“…The mapping of several peptides onto the translated sequence of the pcpA gene leaves little doubt that the enzyme is encoded by this gene. This assignment is further supported by the recent report that a strain of S. chlorophenolica in which pcpA had been knocked out accumulates DCHQ when grown in the presence of PCP (41), suggesting that pcpA encodes the enzyme which converts DCHQ to the next compound in the pathway.…”

Section: Discussionsupporting

confidence: 60%

Evidence That pcpA Encodes 2,6-Dichlorohydroquinone Dioxygenase, the Ring Cleavage Enzyme Required for Pentachlorophenol Degradation in Sphingomonas chlorophenolica Strain ATCC 39723

Resing

Lawson

et al. 1999

Biochemistry

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An enzyme that catalyzes an Fe2+-dependent reaction of 2, 6-dichlorohydroquinone with O2 has been isolated from Sphingomonas chlorophenolica sp. strain ATCC 39723, a soil microorganism capable of complete mineralization of pentachlorophenol. The product of the reaction is too unstable to allow spectroscopic characterization, but is apparently negatively charged and retains the two chlorine atoms of the substrate. The enzyme was partially sequenced using electrospray LC-MS, and one peptide was used to search the NCBInr database. This peptide matched a part of PcpA, a protein of unknown function that is induced in S. chlorophenolica in response to pentachlorophenol. Several other peptides could also be mapped onto the sequence of PcpA, suggesting that the enzyme is encoded by pcpA. PcpA has low but significant sequence similarity to an unusual class of extradiol dioxygenases. On the basis of the sequence analysis, the Fe2+ and O2 dependence of the enzyme, and the characteristics of the product, the enzyme is proposed to be a 2,6-dichlorohydroquinone dioxygenase. The position of ring cleavage has not yet been identified.

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Section: Discussionsupporting

confidence: 60%

Evidence That pcpA Encodes 2,6-Dichlorohydroquinone Dioxygenase, the Ring Cleavage Enzyme Required for Pentachlorophenol Degradation in Sphingomonas chlorophenolica Strain ATCC 39723

Resing

Lawson

et al. 1999

Biochemistry

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“…PcpA has been suggested to play an essential role in PCP degradation, especially in the conversion of 2,6‐DCHQ [8] in ATCC39723. However, there has been no direct evidence that PcpA converts 2,6‐DCHQ.…”

Section: Discussionmentioning

confidence: 99%

“…PCP is converted to tetrachlorohydroquinone (TeCHQ) by PCP 4‐monooxygenase encoded by the pcpB gene [3,4], and subsequently TeCHQ is reductively dechlorinated to trichlorohydroquinone (TrCHQ) and subsequently to 2,6‐dichlorohydroquinone (2,6‐DCHQ) by reductive dehalogenase, which is encoded by the pcpC gene [5–7]. The pathway beyond 2,6‐DCHQ is unknown, although PcpA has been proposed to be involved in the conversion of 2,6‐DCHQ, based on the accumulation of 2,6‐DCHQ by a pcpA mutant [8].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 1999

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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.z 1999 Federation of European Biochemical Societies.

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“…24) However, our findings demonstrated that the TC-FDM possessed by the bacteria plays an important role in the dechlorination of halogenated aromatic compounds. In addition, genes derived from bacteria involved in PCP dechlorination have only been identified in Gram-negative bacteria 25,26) ; Gram-positive bacteria, including the strain PD653, have a different dechlorination mechanism. However, this study led to the first discovery of novel PCP dechlorination genes (hcbB1B2B3) in Gram-positive bacteria.…”

Section: Novel Catabolic Genes Involved In Catalyzing the Dechlorination Of Hcb And Pcpmentioning

confidence: 99%

Study on the biodegradation of persistent organic pollutants (POPs)

Takagi

2020

J. Pestic. Sci.

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The use of organochlorine pesticides, such as dichlorodiphenyltrichloroethane (DDT) and benzene hexachloride (BHC), have contributed substantially to the increase and stable supply of food production post-World War II. However, they have also become a major source of pollution on a global scale due to their persistence in the environment, high bioconcentration, toxicity, and their long-distance mobility. Although the use and production of these pesticides were banned over 45 years ago, they still present a risk to human health and ecosystems, and pose a threat to food safety. These pesticides were designated as persistent organic pollutants (POPs) by the Stockholm Convention in 2001, which urged the industry to reduce or eliminate them globally. The authors of this study have been involved in the research and development of bioaugmentation soil remediation technology to reduce the risk of environmental and crop contamination originating from POPs. In this paper, these studies are summarized, from basic studies (1, 2, 3) to an applied study (4), as follows: (1) use of the soil-charcoal perfusion method to explore POPdegrading bacteria, (2) bacteriological characteristics, metabolic pathways and dechlorination genes of the hexaclorobenzene (HCB)-mineralizing bacterial strain PD653, (3) characteristics and metabolic pathways of the dieldrin-degrading bacterial strain KSF27, and (4) application of these degrading bacteria for remediation of POPs-contaminated soil.

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Mutational analysis of pcpA and its role in pentachlorophenol degradation by Sphingomonas (Flavobacterium) chlorophenolica ATCC 39723

Cited by 27 publications

References 28 publications

Evidence That pcpA Encodes 2,6-Dichlorohydroquinone Dioxygenase, the Ring Cleavage Enzyme Required for Pentachlorophenol Degradation in Sphingomonas chlorophenolica Strain ATCC 39723

Evidence That pcpA Encodes 2,6-Dichlorohydroquinone Dioxygenase, the Ring Cleavage Enzyme Required for Pentachlorophenol Degradation in Sphingomonas chlorophenolica Strain ATCC 39723

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

Study on the biodegradation of persistent organic pollutants (POPs)

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