1.14.13.50: pentachlorophenol monooxygenase
This is an abbreviated version!
For detailed information about pentachlorophenol monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.50
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1.14.13.50
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pcp-degrading
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flavobacterium
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sphingobium
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chlorophenolicum
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tetrachlorohydroquinone
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bioremediation
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tetrachlorobenzoquinone
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dehalogenation
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environmental protection
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arthrobacter
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degradation
- 1.14.13.50
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pcp-degrading
- flavobacterium
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sphingobium
- chlorophenolicum
- tetrachlorohydroquinone
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bioremediation
- tetrachlorobenzoquinone
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dehalogenation
- environmental protection
- arthrobacter
- degradation
Reaction
Synonyms
CpsB, dechlorinase, pentachlorophenol, GM610_18120, oxygenase, pentachlorophenol 4-mono-, PCB hydroxylase, PCP 4-monooxygenase, PCP hydroxylase, PCP-4-monooxygenase, PCP-monooxygenase, PCP4MO, PcpB, PcpD, pentachlorophenol 4-mono-oxygenase, pentachlorophenol 4-monooxygenase, pentachlorophenol dechlorinase, pentachlorophenol dehalogenase, pentachlorophenol hydroxylase, pentachlorophenol monooxygenase, pentachlorophenol-4-monooxygenase, Phe4MO, tetrachlorobenzoquinone reductase
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General Information
General Information on EC 1.14.13.50 - pentachlorophenol monooxygenase
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evolution
metabolism
physiological function
additional information
evolution
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the enzyme belongs to the Bacillus cereus group in the Phe4MO superfamily, sequence comparisons and phylogenetic analysis
evolution
Bacillus tropicus AOA-CPS1
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the enzyme belongs to the Bacillus cereus group in the Phe4MO superfamily, sequence comparisons and phylogenetic analysis
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hydroxylation of pentachlorophenol in the pentachlorophenol biodegradation pathway
metabolism
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the first step in the PCP degradation pathway is the rate-limiting step involving the hydroxylation of PCP to 1,4-tetrachlorobenzoquinone (Tet-CBQ). The reaction is catalysed by the enzyme PCP 4-monooxygenase (PcpB) in bacteria and cytochrome p450 monooxygenase in fungus. Phe4MO also plays a critical role in xenobiotic compound degradation and lipid metabolism
metabolism
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two pathways are proposed for pentachlorophenol (PCP) transformation in BtAOA. In the first pathway, 2,6-bis(1,1-dimethylethyl)phenol, 1-methoxy-5-trimetylsilyoxyhexane, trimethylsilyl 2-butoxyacetate and methyl 2-hydroxyl-3-methylbutanoate fragments are found. The metabolites detected for the proposed second pathway include 1,3-dimethyl-4,6-diisopropylbenzene, 2,4-dimethylbenzenecarboxaldehyde and 2,5-dimethylbenzaldehyde. Both 2,6-di-tert-butylbenzoquinone and 1,3-dimethyl-4,6-diisopropylbenzene cannot be metabolites from the same pathway, it could be that, one of the pathways is initiated by PcpB and the other by cytochrome P450 monooxygenase. Metabolic reconstruction of BtAOA xenobiotics biodegradation pathways, pathway regulation analysis, overview
metabolism
Bacillus tropicus AOA-CPS1
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the first step in the PCP degradation pathway is the rate-limiting step involving the hydroxylation of PCP to 1,4-tetrachlorobenzoquinone (Tet-CBQ). The reaction is catalysed by the enzyme PCP 4-monooxygenase (PcpB) in bacteria and cytochrome p450 monooxygenase in fungus. Phe4MO also plays a critical role in xenobiotic compound degradation and lipid metabolism
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metabolism
Bacillus tropicus AOA-CPS1
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two pathways are proposed for pentachlorophenol (PCP) transformation in BtAOA. In the first pathway, 2,6-bis(1,1-dimethylethyl)phenol, 1-methoxy-5-trimetylsilyoxyhexane, trimethylsilyl 2-butoxyacetate and methyl 2-hydroxyl-3-methylbutanoate fragments are found. The metabolites detected for the proposed second pathway include 1,3-dimethyl-4,6-diisopropylbenzene, 2,4-dimethylbenzenecarboxaldehyde and 2,5-dimethylbenzaldehyde. Both 2,6-di-tert-butylbenzoquinone and 1,3-dimethyl-4,6-diisopropylbenzene cannot be metabolites from the same pathway, it could be that, one of the pathways is initiated by PcpB and the other by cytochrome P450 monooxygenase. Metabolic reconstruction of BtAOA xenobiotics biodegradation pathways, pathway regulation analysis, overview
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efficient degradation of pentachlorophenol (PCP) and involvement of different genes and enzymes in the degradation pathway in Bacillus tropicus strain AOA-CPS1
physiological function
Bacillus tropicus AOA-CPS1
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efficient degradation of pentachlorophenol (PCP) and involvement of different genes and enzymes in the degradation pathway in Bacillus tropicus strain AOA-CPS1
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enzyme homology structure modeling using PDB IDs 4Q3W and 4JPY individually as templates, overview. The catalytic active site of the enzyme has a Fe3+ metal ion-binding centre in contact with residues His124, Glu125, His129 and Glu214
additional information
Bacillus tropicus AOA-CPS1
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enzyme homology structure modeling using PDB IDs 4Q3W and 4JPY individually as templates, overview. The catalytic active site of the enzyme has a Fe3+ metal ion-binding centre in contact with residues His124, Glu125, His129 and Glu214
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