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. 1997 Dec;63(12):4833–4838. doi: 10.1128/aem.63.12.4833-4838.1997

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

S Chanama 1, R L Crawford 1
PMCID: PMC168808  PMID: 9406403

Abstract

Sphingomonas (Flavobacterium) chlorophenolica ATCC 39723 degrades pentachlorophenol (PCP) through a catabolic pathway encoded by multiple genes. One gene required for PCP degradation is pcpA, which encodes information for a 30-kDa polypeptide, PcpA, found in the periplasm of the bacterium. The biological role of PcpA has remained unknown. We disrupted pcpA by replacing it with a defective copy through homologous recombination. The pcpA recombinant, mutant strains accumulated 2,6-dichlorohydroquinone (2,6-DiCH) as a metabolite of PCP. This work confirms that pcpA is essential for degradation of PCP by S. chlorophenolica ATCC 39723 and suggests that it encodes a protein involved in hydrolytic dehalogenation of 2,6-DiCH, an already established primary metabolite of the PCP catabolic pathway.

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Selected References

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