Microbial Degradation of Haloaromatics

Reineke, Walter; Knackmuss, Hans‐Joachim

doi:10.1146/annurev.mi.42.100188.001403

Cited by 356 publications

(133 citation statements)

References 0 publications

Supporting

Mentioning

132

Contrasting

Unclassified

Order By: Relevance

“…Enzymes involved in 4-methylmuconolactone degradation have thus far been characterized only from Rhodococcus rhodochrous N75 and Cupriavidus necator JMP134 and comprise a 4-methylmuconolactone 4-methylisomerase, forming 3-methylmuconolactone, as a key enzyme (7,13,43). Bacteria capable of degrading chloroaromatics via chlorocatechols usually contain enzymes of the chlorocatechol pathway (48,49), involving ortho cleavage by a chlorocatechol 1,2-dioxygenase with high activity against chlorocatechols (11), a chloromuconate cycloisomerase with high activity against chloromuconates (53), a dienelactone hydrolase active against both cis-and trans-dienelactone (4-carboxymethylenebut-2-en-4-olide) (53), and a maleylacetate reductase (23). In phylogenetic analyses, chlorocatechol and catechol 1,2-dioxygenases constitute different subfamilies of the family of intradiol dioxygenases.…”

mentioning

confidence: 99%

A Gene Cluster Involved in Degradation of Substituted Salicylates viaorthoCleavage inPseudomonassp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate

et al. 2007

View full text Add to dashboard Cite

Pseudomonas sp. strain MT1 has recently been reported to degrade 4-and 5-chlorosalicylate by a pathway assumed to consist of a patchwork of reactions comprising enzymes of the 3-oxoadipate pathway. Genes encoding the initial steps in the degradation of salicylate and substituted derivatives were now localized and sequenced. One of the gene clusters characterized (sal) showed a novel gene arrangement, with salA, encoding a salicylate 1-hydroxylase, being clustered with salCD genes, encoding muconate cycloisomerase and catechol 1,2-dioxygenase, respectively, and was expressed during growth on salicylate and chlorosalicylate. A second gene cluster (cat), exhibiting the typical catRBCA arrangement of genes of the catechol branch of the 3-oxoadipate pathway in Pseudomonas strains, was expressed during growth on salicylate. Despite their high sequence similarities with isoenzymes encoded by the cat gene cluster, the catechol 1,2-dioxygenase and muconate cycloisomerase encoded by the sal cluster showed unusual kinetic properties. Enzymes were adapted for turnover of 4-chlorocatechol and 3-chloromuconate; however, 4-methylcatechol and 3-methylmuconate were identified as the preferred substrates. Investigation of the substrate spectrum identified 4-and 5-methylsalicylate as growth substrates, which were effectively converted by enzymes of the sal cluster into 4-methylmuconolactone, followed by isomerization to 3-methylmuconolactone. The function of the sal gene cluster is therefore to channel both chlorosubstituted and methylsubstituted salicylates into a catechol ortho cleavage pathway, followed by dismantling of the formed substituted muconolactones through specific pathways.

show abstract

mentioning

confidence: 99%

A Gene Cluster Involved in Degradation of Substituted Salicylates viaorthoCleavage inPseudomonassp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate

et al. 2007

View full text Add to dashboard Cite

show abstract

“…Specialized strains of aerobic and anaerobic bacteria have been discovered to use selected halogenated hydrocarbons as sole carbon and energy sources (1,4,5).…”

mentioning

confidence: 99%

“…The aerobic catabolism of chloroaromatics usually occurs through two different pathways (5,6). Compounds containing one or two chlorine atoms are usually converted to chlorocatechols and then catabolized through the modified ortho-cleavage pathway (10,11).…”

mentioning

confidence: 99%

“…3,4-PCDs, specific for hydroxybenzoates, are typically composed of two homologous subunits in large oligomeric complexes (␣␤Fe 3ϩ ) [2][3][4][5][6][7][8][9][10][11][12] (22), 1,2-CTDs are dimers (␣Fe 3ϩ ) 2 with identical or very similar subunits and generally comprise enzymes with markedly different substrate * This work was supported by Grant ICA2-CT-2000-10006 from the European Commission Research and Technological Development Programme Copernicus, Contract HPRI-CT-1999-00017 from the European Community Access to Research Infrastructure Action of the Improving Human Potential Programme to the EMBL Hamburg Outstation, Cofin 2002 funding from the Italian Ministero Università e Ricerca Scientifica, and the Gruppo Nazionale di Ricerca per la Difesa dai Rischi Chimico-Industriali ed Ecologici, Consiglio Nazionale delle Ricerche.The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Crystal Structure of 4-Chlorocatechol 1,2-Dioxygenase from the Chlorophenol-utilizing Gram-positive Rhodococcus opacus 1CP

Ferraroni

Solyanikova

Kolomytseva

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

The crystal structure of the 4-chlorocatechol 1,2-dioxygenase from the Gram-positive bacterium Rhodococcus opacus (erythropolis) 1CP, a Fe(III) ion-containing enzyme involved in the aerobic biodegradation of chloroaromatic compounds, has been solved by multiple wavelength anomalous dispersion using the weak anomalous signal of the two catalytic irons (1 Fe/257 amino acids) and refined at a 2.5 Å resolution (R free 28.7%; R factor 21.4%). The analysis of the structure and its comparison with the structure of catechol 1,2-dioxygenase from Acinetobacter calcoaceticus ADP1 (Ac 1,2-CTD) highlight significant differences between these enzymes. The general topology of the present enzyme comprises two catalytic domains (one for each subunit) related by a noncrystallographic 2-fold axis and separated by a common ␣-helical zipper motif consisting of five N-terminal helices from each subunit; furthermore the C-terminal tail is shortened significantly with respect to the known Ac 1,2-CTD. The presence of two phospholipids binding in a hydrophobic tunnel along the dimer axis is shown here to be a common feature for this class of enzyme. The active site cavity presents several dissimilarities with respect to the known catechol-cleaving enzyme. The catalytic nonheme iron(III) ion is bound to the side chains of Tyr-134, Tyr-169, His-194, and His-196, and a cocrystallized benzoate ion, bound to the metal center, reveals details on a novel mode of binding of bidentate inhibitors and a distinctive hydrogen bond network with the surrounding ligands. Among the amino acid residues expected to interact with substrates, several are different from the corresponding analogs of Ac 1,2-CTD: Asp-52, Ala-53, Gly-76, Phe-78, and Cys-224; in addition, regions of largely conserved amino acid residues in the catalytic cleft show different shapes resulting from several substantial backbone and side chain shifts. The present structure is the first of intradiol dioxygenases that specifically catalyze the cleavage of chlorocatechols, key intermediates in the aerobic catabolism of toxic chloroaromatics.

show abstract

“…One factor that could be tested was that the genes are transferred and expressed in alternative hosts, but competition for the chlorobenzoate substrate by other aromatic ring-oxidizing enzymes occurs. Likely candidates for competing activities are the benzoate (toluate) 1,2-dioxygenases described previously (Reineke & Knackmuss 1988). In fluorescent Pseudomonads, these enzymes are able to oxidize 3thlorobenzoate to chlorocatechol metabolites that accumulate in the absence of 1,2-(1,6)-dioxygenas.…”

Section: Testing R I I Hypothesis To Explnin the Cbaab Host Rniigementioning

confidence: 99%

The phylogenetic distribution of a transposable dioxygenase from the Niagara River watershed

et al. 1995

View full text Add to dashboard Cite

Horizontal gene transfer in the Bacteria has been demonstrated to occur under natural conditions. The ecological impact of gene transfer events depends on the new genetic material being expressed in recipient organisms, and on natural selection processes operating on these recipients. The phylogenetic distribution of cbaAB genes for chlorobenzoate 3,4-(4,5)-dioxygenase, which are carried within Tn5271 on the IncPP plasmid pBRC60, was investigated using isolates from freshwater microcosms and from the Niagara River watershed. The latter included isolates from surface water, groundwater and bioremediation reactor samples. The cbaAB genes have become integrated, through interspecific transfer, primarily into species of the p Proteobacteria (W48 isolates). Only four isolates, identified as Pseudomonas j7uorescens (3/48) and Xanthomonas maltophilia (l/48), belonged to the r Proteobacteria, despite the observation that pBRC60 was capable of mobilizing these genes into a wide range of j3 and r Proteobacteria in the laboratory. The natural host range correlated with the distribution of the meta-ring-fission pathway for metabolism of protocatechuates formed when the cbaAB genes were expressed (45/48 isolates). We proposed the hypothesis that natural selection has favoured recipients that successfully integrate the activity of the transferred dioxygenase with the conserved meta ring-fission pathway. The hypothesis was tested by transfemng a pIasmid construct containing the cbaAB genes into type strains representative of the j3 and r Proteobacteria. The concept of applying mobile catabolic genes to probe the phylogenetic distribution of compatible degradative pathways is discussed.

show abstract

Microbial Degradation of Haloaromatics

Cited by 356 publications

References 0 publications

A Gene Cluster Involved in Degradation of Substituted Salicylates viaorthoCleavage inPseudomonassp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate

A Gene Cluster Involved in Degradation of Substituted Salicylates viaorthoCleavage inPseudomonassp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate

Crystal Structure of 4-Chlorocatechol 1,2-Dioxygenase from the Chlorophenol-utilizing Gram-positive Rhodococcus opacus 1CP

The phylogenetic distribution of a transposable dioxygenase from the Niagara River watershed

Contact Info

Product

Resources

About