Recruitment of a chromosomally encoded maleylacetate reductase for degradation of 2,4-dichlorophenoxyacetic acid by plasmid pJP4

Kukor, Jerome J.; Olsen, Ronald H.; Siak, J.

doi:10.1128/jb.171.6.3385-3390.1989

Cited by 42 publications

(24 citation statements)

References 34 publications

(14 reference statements)

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“…strain B13 (25). However, it contrasts with the subunit molecular mass of the enzyme cloned by Kukor et al (27) (Fig. 1).…”

Section: Resultscontrasting

confidence: 46%

“…In the case of 4-nitrophenol catabolism, maleylacetate is the product of 4-hydroxymuconic semialdehyde oxidation (51), whereas from resorcinol and 2,4-dihydroxybenzoate it is generated by dioxygenation of the intermediate 1,2,4-trihydroxybenzene (7,54), a reaction which is more common in fungi. Tyrosine has also been proposed to be metabolized by some bacteria via maleylacetate (27). However, good biochemical evidence for this suggestion is lacking, and thus the hypothetical pathway for the time being might be assumed to resemble that in the yeast T. cutaneum (53).…”

Section: Resultsmentioning

confidence: 99%

“…Whether any of the above-mentioned compounds is the natural metabolic precursor of maleylacetate is doubtful, in several cases because of the xenobiotic properties of the compound and in the case of tyrosine because of the hypothetical character of the pathway. Resorcinol also is not likely to be the normal precursor, because various bacteria which had been shown to possess a maleylacetate reductase do not grow with resorcinol (27,44). It still remains to be elucidated whether the occurrence of maleylacetate reductase is typically associated with the capability to utilize 2,4-dihydroxybenzoate.…”

Section: Resultsmentioning

confidence: 99%

“…In contrast, the maleylacetate reductases (EC 1.3.1.32) of Alcaligenes euitrophius JMP134 and Pseudornonas sp. strain PKO1 seem to be chromosomally encoded (10,27,59). Since partially purified maleylacetate reductase preparations from A. eutrophu.s JMP134 and Pseudomonas sp.…”

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confidence: 99%

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Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4)

1993

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Maleylacetate reductase (EC 1.3.1.32) plays a major role in the degradation of chloroaromatic compounds by channeling maleylacetate and some of its substituted derivatives into the 3-oxoadipate pathway. Chloroaromatic compounds can bc degraded by bacteria by a variety of mechanisms (for recent reviews, see references 9, 15, 22, and 36). A predominant catabolic route for compounds carrying one to three chlorine substituents is the modified ortho cleavage pathway (Fig. 1). In this pathway chlorocatechols, generated by peripheral enzyme systems, are subject to intradiol cleavage, giving rise to the corresponding chlorocis,cis-muconates. The latter have long been known to be converted to (possibly still chlorosubstituted) maleylacetates by cycloisomerization, concomitant loss of one chlorine atom, and subsequent hydrolytic cleavage of the dienelactone (4-carboxymethylenebut-2-en-4-olide) intermediate (16,17,21,55). The unsubstituted maleylacetate can be funnelled into the ordinary 3-oxoadipate pathway simply by reduction of the carbon-carbon double bond (13). 2-Chloromaleylacetate enters the same route by two subsequent reductive reactions, the first of which is coupled to chloride elimination, giving rise to a maleylacetate intermediate (Fig.

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“…strain B13 (25). However, it contrasts with the subunit molecular mass of the enzyme cloned by Kukor et al (27) (Fig. 1).…”

Section: Resultscontrasting

confidence: 46%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4)

1993

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“…The maleylacetic acid is then catabolized by chromosomally encoded enzymes (21). Enzymes involved in this transformation are chlorocatechol 1,2-dioxygenase (catechol 1,2-dioxygenase II or pyrocatechase II; EC 1.13.11.1), encoded by clcA of pAC27 and tfdC of pJP4, chloromuconate cycloisomerase (EC 5.5.1.1), encoded by clcB of pAC27 and tfdD of pJP4, and dienelactone (4-carboxymethylenebut-2-en-4-olide) hydrolase (EC 3.1.1.45), encoded by clcD of pAC27 and tfdE of pJP4 ( Fig.…”

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Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4

et al. 1990

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Growth of Alcaligenes eutrophus JMP134 on 2,4-dichlorophenoxyacetate requires a 2,4-dichlorophenol hydroxylase encoded by gene tfdB. Catabolism of either 2,4-dichlorophenoxyacetate or 3-chlorobenzoate involves enzymes encoded by the chlorocatechol oxidative operon consisting of tfdCDEF, which converts 3-chloro-and 3,5-dichlorocatechol to maleylacetate and chloromaleylacetate, respectively. Transposon mutagenesis has localized tfdB and t.fdCDEF to EcoRI fragment B of plasmid pJP4 (R. H. Don, A. J. Wieghtman, H.-J. Knackmuss, and K. N. Timmis, J. Bacteriol. 161:85-90, 1985). We present the complete nucleotide sequence of tfdB and tfdCDEF contained within a 7,954-base-pair HindIII-SstI fragment from EcoRI fragment B. Sequence and expression analysis of tfdB in Escherichia coli suggested that 2,4-dichlorophenol hydroxylase consists of a single subunit of 65 kilodaltons. The amino acid sequences of proteins encoded by tfdD and tfdE were found to be 63 and 53% identical to those of functionally similar enzymes encoded by clcB and ckD, respectively, from plasmid pAC27 of Pseudomonas putida. P. putida(pAC27) can utilize 3-chlorocatechol but not dichlorinated catechols. A region of DNA adjacent to clcD in pAC27 was found to be 47% identical in amino acid sequence to tfdiF, a gene important in catabolizing dichlorocatechols. The region in pAC27 does not appear to encode a protein, suggesting that the absence of a functional trans-chlorodienelactone isomerase may prevent P. putida(pAC27) from utilizing 3,5-dichlorocatechol.Bacteria play a crucial role in the dissimilation of environmental pollutants. In general, the catabolism of aromatic compounds is channeled through catechol intermediates (33). Hence, the ability of an organism to form and catabolize catechols or their derivatives can play a major part in the utilization of an aromatic compound. Comparison of the degradative pathways of different aromatics may help in understanding the evolution of growth substrate specificity.Chlorinated aromatics, such as 2,4-dichlorophenoxyacetic acid (2,4D) and 3-chlorobenzoate (3CBA), are catabolized via a modified ortho pathway (11,12,20,28,34,35; for a review, see reference 33). Pseudomonas putida plasmid pAC27, a deletion derivative of pAC25, confers catabolism of 3CBA (5), whereas Alcaligenes eutrophus JMP134 plasmid pJP4 enables degradation of both 2,4D and 3CBA (10, 11). In both cases, 3CBA appears to be degraded to 3-chlorocatechol by enzymes encoded by chromosomal genes. 2,4D is catabolized by A. eutrophus JMP134 to 2,4-dichlorophenol (2,4DCP) by 2,4D monooxygenase. 2,4DCP is then hydroxylated by 2,4DCP hydroxylase to form 3,5-dichlorocatechol (11; Fig. 1).3-Chlorocatechol is oxidized to maleylacetic acid by enzymes encoded by the clcABD operon in pAC27 (13) and by the tfdCDEF operon of pJP4 (11). The maleylacetic acid is then catabolized by chromosomally encoded enzymes (21). Enzymes involved in this transformation are chlorocatechol 1,2-dioxygenase (catechol 1,2-dioxygenase II or pyrocatechase II; EC 1.13.11.1), encoded b...

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Biodegradation and plant protection from the herbicide 2,4-D by plant-microbial associations in cotton production systems

Feng

Kennedy

1997

Biotechnol. Bioeng.

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A significant “biosafening” protection of plants from the effect of 2,4‐D in plant‐microbial associations has been demonstrated in this study. The 2,4‐D‐degrading plasmid, pJP4 was transferred into Rhizobium sp. CB1024, which nodulates Dolichos lablab, and Azospirillum brasilense Sp7 carrying a nifA‐lacZ gene marker, which can colonize cotton roots. Both transconjugants degraded 2,4‐D in pure culture via cometabolism up to 50 μg mL−1. When the transconjugants were inoculated onto Dolichos lablab and cotton, respectively, such plants were resistant to this herbicide when the nutrient solution was treated with 2,4‐D up to 10 μg mL−1 for Dolichos lablab and 0.5 μg mL−1 for cotton. Plants inoculated with wild‐type strains were dead (Dolichos lablab) or dying (cotton). Because cotton is more sensitive to herbicides, only incomplete protection of plants was achieved with the transconjugant. Improving the effect of colonization of Azospirillum on cotton roots may be critical for a complete degradation and plant protection. The transconjugant of Rhizobium sp. CB1024 was still able to nodulate Dolichos lablab, N2‐fixing activity was only slightly affected. Other pesticide‐degrading capacities may also be inserted into those plant‐associated bacterial strains for the degradation of these chemicals by plant‐microbial associations. Whether such systems will be successful when applied in the field with competition from other bacteria is being examined. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 513–519, 1997.

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Recruitment of a chromosomally encoded maleylacetate reductase for degradation of 2,4-dichlorophenoxyacetic acid by plasmid pJP4

Cited by 42 publications

References 34 publications

Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4)

Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4)

Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4

Biodegradation and plant protection from the herbicide 2,4-D by plant-microbial associations in cotton production systems

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