Purification and properties of a plasmid‐encoded 2,4‐dichlorophenol hydroxylase

Liu, Ting; Chapman, P. J.

doi:10.1016/0014-5793(84)80797-8

Cited by 66 publications

(59 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…T his is consistent wi th the observation that CPH , constitutively expressed by JMP 134-1 , exhibits no activity against phenol (liu and Chapman 1984;Pieper el al. 1988).…”

Section: L: Nzyme Activities Of Jmp 134-1 During Growth On Pa 24-supporting

confidence: 90%

Regulation of catabolic pathways of phenoxyacetic acids and phenols in Alcaligenes eutrophus JMP 134

1989

View full text Add to dashboard Cite

Institllt fUr Mikrobio logie, Univcrsitii t Stuttgart, 0-7000 StUllgart, Federal Republ ic of Ge rmany Abstract. Alicaligenes eulrophus JMP 134 is able to grow on 2,4~dich loro-, 4-chloro-2-methyl· and 2-methylphcnoltY acetic acid . The unsubstilUted phenoxyacetic acid, however, is no growth substrate due to very poor induction of the 2,4-D monooxygenase. Spontaneous mutants of Alcaligene.f eutrophus JMP 134 capable of growth with phenoltyacctic acid were selected on agar pla tes. One of these mutants, designa ted Alcaligenes eJJlrophus JMP 134-1, shows consti· tutive production of six enzymes of the 2,4-D pathway, which were known to be localized in at least tluee different transcriptional units. A common regulatory gene is postu~ lated to be mutated. 2,4~Oichloro-, 4·chloro-2-methyl-and 2-methylphenoxyacctic acid were the inducers of the en~ zymes of the "chloroaromatic pathway" in Alcaligenes eutrophus JMP 134. Phenol and 2-methylphenol. metabolites of the degradation of phenoxyacct ic acid and 2-methyl· phenoxyacetie acid, were shown to be inducers of the mcta-cleavage pathway. whereas 2,4-dichlorophenol and 4-chloro-2-methylphenol were no\. Thus efficient regulation prevents chloroaromatics from being misrouted into the unproductive meta-cleavage pathway. Because 2,4-dichloroand 4-chloro~2 -methylphenol did no t show any induction potential, they were growth substrates only for the mutant strainJMP 134-1.

show abstract

“…T his is consistent wi th the observation that CPH , constitutively expressed by JMP 134-1 , exhibits no activity against phenol (liu and Chapman 1984;Pieper el al. 1988).…”

Section: L: Nzyme Activities Of Jmp 134-1 During Growth On Pa 24-supporting

confidence: 90%

Regulation of catabolic pathways of phenoxyacetic acids and phenols in Alcaligenes eutrophus JMP 134

1989

View full text Add to dashboard Cite

show abstract

“…1). This has been shown for the chlorophenol hydroxylase by Liu and Chapman (1984). A second phenol hydroxylating activity, found in 2,4-0-and MCPA-grown cells (fable 2) showed high activity against phenol and is therefore assumed to be a ring-hydroxylating activity.…”

Section: Dis(:ussionmentioning

confidence: 61%

“…2,4-D grown cells from the early stationary growth phase exhibited high activity against 2,4-dichlara-and 4-chloro-2-mcthylphenol but not against phenol and 2-and 4-methylphenoL This indicates induction of the pJP4-encodcd chlorophenol hydroxylase which had been purified by Liu and Chapman (1984). During exponential growth, additional activities against phenol, 2-and 4-methylphenol were induced, in 2,4-0-and MCPAgrown cells in a ratio of 4: 1 : 1, in 2MPA-grown cells in a ratio of approximately 1 : 1: 1.…”

Section: Dis(:ussionmentioning

confidence: 96%

“…A similar situation of induction of two ca techol 1,2-dioxygenases after growth of baetcrial strains on chloroaromatics has been described by Oorn and Knaekmuss (1978a) and Reineke and Knaekmuss (1980), but also the induction of only one catechol 1,2-dioxygenase with broad substrate specifity bas been reported (Reineke and Knackmuss 1984). Due to the fact that chlorophenol hydroxylase of strain JMP 134, as shown by Liu and Chapman (1984), was highly specific against chlorophenols and exhibited no activity against unsubstituted phenol, we investigated if further enzymes, highly specific for chlorosubstituted substrates, were synthesized by strain JMP 134. Purificatio.n of catechol 1,2-dioxygenasc active against chlorocatechols has already been carried out with bacterial species isolated on monochloroaromatics such as 3-chlorobenzoate (Reineke and Knackmuss 1980) and chlorobenzene (Reineke and K nackmuss 1984).…”

Section: Dis(:ussionmentioning

confidence: 99%

“…1985;Streber et al 1987) and evidence has beeu given for a pathway which includes 2,4-dicWorophcnol and 3,5-dichlorocatechol as intennediates (Don et al 1985). Further, Liu and Chapman (1984) described the purification of a pJJ>4-cncoded chlorophenol hydroxylasc, which formed 3,5-dichlorocatcchol from 2,4-dichlorophenol. Don and Pemberton (1981) reported that after transfer of pJP4 to different recipient strains, these strains aquired the ability to degrade 2,4-D.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Metabolism of 2,4-dichlorophenoxyacetic acid, 4-chloro-2-methylphenoxyacetic acid and 2-methylphenoxyacetic acid by Alcaligenes eutrophus JMP 134

et al. 1988

View full text Add to dashboard Cite

Abstract. Of eleven substituted phenoxyacetic acids tested, only three (2,4-dichloro-, 4-chloro-2-methyl-and 2-methylphenoxyacetic acid) served as growth substrates for Alcaligenes eutroplws JMP 134. Whereas only one enzyme seems to be responsible for the initial cleavage of the ether bond, there was evidence for the presence of three different phenol hydroxylascs in this strain. 3,5-Dichlorocatechol and 5-ch loro-3-methylca techol, metabolites of the degradation of 2,4-diehlorophenoxyacetic acid and 4-cWoro-2-methylphenoxyacetic acid, respectively, were exclusively metabolized via the ortho-cleavage pathway. 2-Methylphenoxy. acetic acid-grown cells showed sim ultaneous induction of meta-and ortho-cleavage enzymes. Two catechol 1,2-dioxygcnases responsible for o rlho-cleavage of the intcr~ mediate catechols were partially purified and characterized. One of these enzymes converted 3,5-dichlorocatechol considerably faster than catechol or 3-chlorocatechoL A new enzyme for the cycloisomerisation ofmuconates was found , which exhibited high activity against the ring-cleavage products of 3,5-dichlorocatcchol and 4-chlorocatechol, but low activities against 2-chloromuconate and muconate.

show abstract

Molecular basis of biodegradation of chloroaromatic compounds

Sangodkar

Aldrich

Haugland

et al. 1989

Acta Biotechnologica

View full text Add to dashboard Cite

Chlorinated aromatic hydrocarbons are widely used in industry and agriculture, and comprise the bulk of environmental pollutants. Although simple aromatic compounds are biodegradable by a variety of degradative pathways, their halogenated counterparts are more resistant to bacterial attack and often necessitate evolution of novel pathways. An understanding of such evolutionary processes is essential for developing genetically improved strains capable of mineralizing highly chlorinated compounds. This article provides an overview of the genetic aspects of dissimilation of chloroaromatic compounds and discusses the potential of gene manipulation to promote enhanced evolution of the degradative pathways.

show abstract

Purification and properties of a plasmid‐encoded 2,4‐dichlorophenol hydroxylase

Abstract: 2,4‐Dichlorophenol hydroxylase 2,4‐Dichlorophenoxyacetate plasmid 2,4‐Dichlorophenoxyacetate degradation Alcaligenes eutrophus Pseudomonas putida

Cited by 66 publications

References 16 publications

Regulation of catabolic pathways of phenoxyacetic acids and phenols in Alcaligenes eutrophus JMP 134

Regulation of catabolic pathways of phenoxyacetic acids and phenols in Alcaligenes eutrophus JMP 134

Metabolism of 2,4-dichlorophenoxyacetic acid, 4-chloro-2-methylphenoxyacetic acid and 2-methylphenoxyacetic acid by Alcaligenes eutrophus JMP 134

Molecular basis of biodegradation of chloroaromatic compounds

Contact Info

Product

Resources

About