• Journal of Microbiology and Biotechnology
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• 제8권1호
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• pp.96-100
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• 1998

Pseudomonas sp. S-47 degraded 4-chlorobenzoate (4CBA) to 4-chlorocatechol (4CC) that was subsequently ring-cleaved to form 5-chloro-2-hydroxymuconic semialdehyde. These intermediate compounds were identified by GC-mass spectrometry and UV-visible spectrophotometry. 5-chloro-2-hydroxymuconic acid converted from 5-chloro-2- hydroxymuconic semialdehyde (5C-2HMS) was dechlorinated to produce 2-hydroxypenta-2,4-dienoic acid (2HP-2,4DA) by the strain. These results indicate that Pseudomonas sp. S-47 degrades 4CBA to 2HP-2,4DA via a novel pathway including the meta-cleavage of 4CC and dechlorination of 5C-2HMS.

• Journal of Microbiology
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• 제35권4호
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• pp.290-294
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• 1997

4-Chlorobiphenyl-degrading Pseudomonas sp. DJ-12 was able to degrade 4-chlorobenzoate(4CBA), 4-iodobenzoate, and 4-bromobenzoate completely under aerobic conditions. During. the degradation of 4CBA by Pseudomonas sp. DJ-12, chloride ions were released by dechlorination and 4-hydroxybenzoate was produced as an intermediate metabolite. The NotI-KNA fragments of pKC157 containing dechlorination genes hybridized with the gene encoding 4CBA:CoA dehalogenase of Pseudomonas sp. CBS3 which is responsible for the hydrolytic dechlorination of 4CBA. These results imply that Pseudomonas sp. DJ-12 degrades 4CBA to 40hydroxybenzoate via dechlorination as the initial step of its degradativ pathway. The genes responsible for dechlorination of 4CBA were found to be blcated on the chromosomal DNA of Pseudomonas sp. DJ-12.

• Journal of Microbiology
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• 제35권4호
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• pp.295-299
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• 1997

Pseudomonas sp. S-47 is capable of transforming 4-chlorobenzoate to 4-chlorocatechol which is subsequently oxidized bty meta-cleavage dioxygenase to prodyce 5-chloro-2-hydroxymuconic semialdehyde. Catechol 2,3-dioxygenase (C23O) produced by Pseudomonas sp. S-47 was purified and characterized in this study. The C23O enzyme was maximally produced in the late logarithmic growth phase, and the temperature and pH for maximunm enzyme activity were $30{\sim}35^{\circ}C$ and 7.0, respectively. The enzyme was purified and concentrated 5 fold from the crude cell extracts through Q Sepharose chromatography and Sephadex G-100 gel filtration after acetone precipitation. The enzyme was identified as consisting of 35 kDa subunits when analyzed by SDS-PAGE. The C23O produced by Pseudomonas sp. S-47 was similar to Xy1E of Pseudomonas putida with respect to substrate specificity for several catecholic compounds.

• 한국동물학회:학술대회논문집
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• 한국동물학회 1997년도 한국생물과학협회 학술발표대회
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• pp.244.2-244
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• 1997

No Abstract, See Full Text

• 미생물학회지
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• 제24권3호
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• pp.317-322
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• 1986

It was observed that the strains of Klebsiella pneumoniae isolated from rhizosphere of rice, capable of utilizing chlorivated hervicides, such as 2, 4-dichlorophenoxyacetate, 2-methyl-4-chlorophenoxyacetate and 3-chlorobenzoate, as sole source of carbon and energy and confirmed that their degrading ability of the herbicides was due to plasmid genes. Characteristics of selected strains such as nitrogenase activity, resistances to antibiotics and heavy metal ion were measured.

• 미생물학회지
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• 제38권4호
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• pp.275-275
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• 2002

Pseudomonas sp. S-47 is capable of catabolizing 4-chlorobenzoate (4CBA) as carbon and energy sources under aerobic conditions via the mesa-cleavage pathway. 4CBA-dioxygenase and 4CBA-dihydrodiol dehydrogenase (4CBA-DD) catalyzed the degradation af 4CBA to produce 4-chlorocatechol in the pathway. In this study, the xylL gene encoding 4CBA-DD was cloned from the chromosomal DNA of Pseudomonas sp. S-47 and its nucleotide sequence was analyzed. The xylL gene was found to be composed of 777 nucleotide pairs and to encode a polypeptide of 28 kDa with 258 amino acid residues. The deduced amino acid sequence of the dehydrogenase (XylL) from strain S-47 exhibited 98% and 60% homologies with these of the corresponding enzymes, Pseudomonas putida mt-2 (XyIL) and Acinetobacter calcoaceticus (BenD), respectively. However, the amino arid sequences show 30% or less homology with those of Pseudomonas putida (BnzE), Pseudomonas putida Fl (TodD), Pseudomonas pseudoalcaligenes KF707 (BphB), and Pseudomonas sp. C18 (NahB). Therefore, the 4CBA-dihydrodiol dehdrogenase of strain S-47 belongs to the group I dehydrogenase involved in the degradation of mono-aryls with a carboxyl group.

• Biotechnology and Bioprocess Engineering:BBE
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• 제5권6호
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• pp.449-455
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• 2000

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.

• Journal of Microbiology and Biotechnology
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• 제14권3호
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• pp.483-489
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• 2004

Pseudomonas sp. S-47 is a bacterium capable of degrading benzoate as well as 4-chlorobenzoate (4CBA). Benzoate and 4CBA are known to be degraded via a meta-cleavage pathway characterized by a series of enzymes encoded by xyl genes. The meta-cleavage pathway operon in Pseudomonas sp. S-47 encodes a set of enzymes which transform benzoate and 4CBA into TCA cycle intermediates via the meta-cleavage of (4-chloro )catechol to produce pyruvate and acetyl-CoA. In the current study, the meta-pathway gene cluster was cloned from the chromosomal DNA of S-47 strain to obtain pCS1, which included the degradation activities for 4CBA and catechol. The genetic organization of the operon was then examined by cloning the meta-pathway genes into a pBluescript SKII(+) vector. As such, the meta-pathway operon from Pseudomonas sp. S-47 was found to contain 13 genes in the order of xylXYZLTEGFlQKIH. The two regulatory genes, xylS and xylR, that control the expression of the meta-pathway operon, were located adjacently downstream of the meta-pathway operon. The xyl genes from strain S-47 exhibited a high nucleoside sequence homology to those from Pseudomonas putida mt-2, except for the xylJQK genes, which were more homologous to the corresponding three genes from P. stutzeri AN10. One open reading frame was found between the xylH and xylS genes, which may playa role of a transposase. Accordingly, the current results suggest that the xyl gene cluster in Pseudomonas sp. S-47 responsible for the complete degradation of benzoate was recombined with the corresponding genes from P. putida mt-2 and P. stutzeri AN10.

• Journal of Microbiology
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• 제38권4호
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• pp.275-280
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• 2000

Pseudomonas sp. S-47 is capable of catabolizing 4-chlorobenzoate (4CBA) as rarbon and energy sources under aerobic conditions via the mesa-cleavage pathway. 4CBA-dioxygenase and 4CBA-dihydrodiol dehydrogenase (4CBA-DD) catalyzed the degradation af 4CBA to produce 4-chlorocatechol in the pathway. In this study, the xylL gene encoding 4CBA-DD was cloned from the chromosomal DNA of Pseudomonas sp. S-47 and its nucleotide sequence was analyzed. The xylL gene was found to be composed of 777 nucleotide pairs and to encode a polypeptide of 28 kDa with 258 amino acid residues. The deduced amino acid sequence of the dehydrogenase (XylL) from strain S-47 exhibited 98% and 60% homologies with these of the corresponding enzymes, Pseudomonas putida mt-2 (XyIL) and Acinetobacter calcoaceticus (BenD), respectively. However, the amino arid sequences show 30% or less homology with those of Pseudomonas putida (BnzE), Pseudomonas putida Fl (TodD), Pseudomonas pseudoalcaligenes KF707 (BphB), and Pseudomonas sp. C18 (NahB). Therefore, the 4CBA-dihydrodiol dehdrogenase of strain S-47 belongs to the group I dehydrogenase involved in the degradation of mono-aryls with a carboxyl group.

• Journal of Microbiology and Biotechnology
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• 제13권5호
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• pp.700-705
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• 2003

Pseudomonas sp. S-47 is capable of degrading benzoate and 4-chlorobenzoate as well as catechol and 4-chlorocatechol via the meta-cleavage pathway. The three enzymes of 2-oxopenta-4-enoate hydratase (OEH), acetaldehyde dehydrogenase (acylating) (ADA), and 2-oxo-4-hydroxypentonate aldolase (HOA) encoded by xylJQK genes are responsible for the three steps after the meta-cleavage of catechol. The nucleotide sequence of the xylJQK genes located in the chromosomal DNA was cloned and analyzed. GC content of xylJ, xylQ, and xylK was 65% and consisted of 786, 924, and 1,041 nucleotides, respectively. The deduced amino acid sequences of xylJ, xylQ, and xylK genes from Pseudomonas sp. S-47 showed 93%, 99%, and 99% identity, compared with those of nahT, nahH, and nahI in Pseudomonas stutzeri An10. However, there were only about 53% to 85% identity with xylJQK of Pseudomonas putida mt-2, dmpEFG of P. putida CF600, aphEFG of Comamonas testosteroni TA441, and ipbEGF of P. putida RE204. On the other hand, the xylLTEGF genes located upstream of xylJQK in the strain S-47 showed high homology with those of TOL plasmid from Pseudomonas putida mt-2. These findings suggested that the xylLTEGFIJQK of Pseudomonas sp. S-47 responsible for complete degradation of benzoate and then catechol via the meta-pathway were phylogenetically recombinated from the genes of Pseudomonas putida mt-2 and Pseudomonas stutzeri An10.