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Catabolic Degradation of 4-Chlorobiphenyl by Pseudomonas sp. DJ-12 via Consecutive Reaction of meta-Cleavage and Hydrolytic Dechlorination
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  • Catabolic Degradation of 4-Chlorobiphenyl by Pseudomonas sp. DJ-12 via Consecutive Reaction of meta-Cleavage and Hydrolytic Dechlorination
  • Catabolic Degradation of 4-Chlorobiphenyl by Pseudomonas sp. DJ-12 via Consecutive Reaction of meta-Cleavage and Hydrolytic Dechlorination
저자명
Chae. Jong-Chan,Kim. Eunheui,Park. Sang-Ho,Kim. Chi-Kyung
간행물명
Biotechnology and bioprocess engineering
권/호정보
2000년|5권 6호|pp.449-455 (7 pages)
발행정보
한국생물공학회
파일정보
정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

Pseudomonas sp. strain DJ-12 is a bacterial isolate capable of degrading 4-chlorobiphenyl (4CBP) as a carbon and energy source. The catabolic degradation of 4CBP by the strain DJ-12 was studied along with the genetic organization of the genes responsible for the crucial steps of the catabolic degradation. The catabolic pathway was characterized as being conducted by consecutive reactions of the meta-cleavage of 4CBP, hydrolytic dechlorination of 4-chlorobenzoate (4CBA), hydroxylation of 4-hydroxybenzoate, and meta-cleavage of protocatechuate. The pcbC gene responsible for the meta-cleavage of 4CBP only showed a 30 to 40% homology in its deduced amino acid sequence compared to those of the corresponding genes from other strains. The amino acid sequence of 4CBA-CoA dechlorinase showed an 86% homology with that of Pseudomonas sp. CBS3, yet only a 50% homology with that of Arthrobacter spp. However, the fcb genes for the hydrolytic dechlorination of 4CBA in Pseudomonas sp. DJ-12 showed an uniquely different organization from those of CBS3 and other reported strains. Accordingly, these results indicate that strain DJ-12 can degrade 4CBA completely via meta-cleavage and hydrolytic dechlorination using enzymes that are uniquely different in their amino acid sequences from those of other bacterial strains with the same degradation activities.