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

FEBS Lett. 1999 Oct 15;459(3):395-8. doi: 10.1016/s0014-5793(99)01305-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Escherichia coli
  • Hydroquinones / metabolism
  • Maleates / metabolism
  • Molecular Sequence Data
  • Oxygenases
  • Pentachlorophenol / metabolism*
  • Sequence Homology, Amino Acid
  • Sphingomonas / enzymology*

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Hydroquinones
  • Maleates
  • 2,6-dichloro-4-hydroquinone
  • 2-chloromaleylacetate
  • Pentachlorophenol
  • PcpA protein, Sphingomonas
  • Oxygenases
  • hydroquinone