The Broad Substrate Chlorobenzene Dioxygenase and cis-Chlorobenzene Dihydrodiol Dehydrogenase of Pseudomonas sp. Strain P51 Are Linked Evolutionarily to the Enzymes for Benzene and Toluene Degradation

Werlen, Christoph; Kohler, Hans‐Peter E.; Meer, Jan Roelof van der

doi:10.1074/jbc.271.8.4009

Cited by 121 publications

(85 citation statements)

References 48 publications

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“…The above comparison and the enzymatic data of this study cast light upon the uniqueness of TcbC in terms of its specificity toward 3,4-DC and the amino acids occupying positions 48, 52, and 73, strongly suggesting the adaptation of TcbC for conversion of 3,4-DC produced by the upstream enzymes TcbA and TcbB in strain P51 (61,66).…”

Section: Discussionmentioning

confidence: 99%

Amino Acids in Positions 48, 52, and 73 Differentiate the Substrate Specificities of the Highly Homologous Chlorocatechol 1,2-Dioxygenases CbnA and TcbC

et al. 2005

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Chlorocatechols are the central metabolites in the bacterial degradation processes of many chlorinated aromatic compounds (reviewed in references 50 and 60). The degradation processes via chlorocatechols have been studied intensively with simple chlorinated aromatics such as chlorobenzoates (7, 10, 18, 23, 25, 26), chlorobenzenes (21, 47, 51, 53, 54, 56, 57, 62), and 2,4-dichlorophenoxyacetic acid (2,4-D) (4,9,14). In the degradation of chlorocatechols, the chlorocatechol orthocleavage pathway (modified ortho-cleavage pathway) plays a central role, converting chlorocatechols into 3-oxoadipate (reviewed in references 24, 42, and 50), although several examples of degradation of chlorocatechols via the meta-cleavage pathway have been documented (1, 34).The genes encoding enzymes of the chlorocatechol orthocleavage pathway have been found as a cluster and mostly on large plasmids, which are often transmissible (3,6,7,8,32,39,62,67; for a review, see reference 38). Some of the chlorocatechol gene clusters have been found to be carried on transposons (30,40,45,63) or a phage-like element (49,55). Recent reports on the entire sequencing of two 2,4-D degradative plasmids, pJP4 and pEST4011, illustrated their genetic features of basic plasmid functions such as replication, maintenance, and transfer, shared with other broad-host-range IncP1 plasmids (59, 63). These findings have revealed some of the reasons underlying the wide distribution of the gene clusters of the chlorocatechol ortho-cleavage pathway.In the first step of the chlorocatechol ortho-cleavage pathway, chlorocatechol 1,2-dioxygenase (CCD) cleaves the aromatic ring, converting chlorocatechols into chloro-cis,cis-muconates, and thus has been a subject of intensive study from an enzymatic viewpoint. The CCDs of several strains have been characterized, and some of them have been purified (2,5,10,27,31,33,35,43,44,46,61). The early enzymatic studies of the CCD from the 3-chlorobenzoate (3-CB)-degradative Pseudomonas sp. strain B13 revealed that the CCD is adapted for the conversion of chlorocatechols such as 3-chlorocatechol, unlike catechol 1,2-dioxygenase, which cannot process chlorocatechols efficiently (10, 11). Several studies have revealed a tendency such that CCDs responsible for the conversion of 3,5-dichlorocatechol (3,5-DC) produced as an intermediate of 2,4-D degradation are adapted for the preferential conversion of 3,5-DC (2, 43). CCDs engaged in degradative pathways for other compounds could show different substrate specificities towards congeners of chlorocatechols: one example is TcbC from the 1,2,4-trichlorobenzene-degrading Pseudomonas sp. strain P51, which favors 3,4-dichlorocatechol (3,4-DC) (61). Recently, the crystal structure of the 4-chlorocatechol 1,2-dioxygenase from Rhodococcus opacus strain 1CP has been solved (15, 17), and another CCD from the strain 1CP has been

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Section: Discussionmentioning

confidence: 99%

Amino Acids in Positions 48, 52, and 73 Differentiate the Substrate Specificities of the Highly Homologous Chlorocatechol 1,2-Dioxygenases CbnA and TcbC

et al. 2005

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“…On the other hand, it was found that there was a 5Ј terminus of a putative ORF in the downstream region of carC. The nucleotide sequence of this putative ORF showed 58.0, 57.1, and 57.1% homologies with ferredoxin components of chlorobenzene dioxygenase (56), biphenyl dioxygenase (35), and toluene dioxygenase (59), respectively. In this study, we observed that E. coli harboring pUCA1 forms indigo on 2ϫ YT plates.…”

Section: Discussionmentioning

confidence: 99%

Cloning of genes involved in carbazole degradation of Pseudomonas sp. strain CA10: nucleotide sequences of genes and characterization of meta-cleavage enzymes and hydrolase

et al. 1997

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The DNA fragment encoding meta-cleavage enzymes and the meta-cleavage compound hydrolase, involved in carbazole degradation, was cloned from the carbazole-utilizing bacterium Pseudomonas sp. strain CA10. DNA sequence analysis of this 2.6-kb SmaI-SphI fragment revealed that there were three open reading frames (ORF1, ORF2, and ORF3, in this gene order). ORF1 and ORF2 were indispensable for meta-cleavage activity for 2-aminobiphenyl-2,3-diol and its easily available analog, 2,3-dihydroxybiphenyl, and were designated carBa and carBb, respectively. The alignment of CarBb with other meta-cleavage enzymes indicated that CarBb may have a non-heme iron cofactor coordinating site. On the basis of the phylogenetic tree, CarBb was classified as a member of the protocatechuate 4,5-dioxygenase family. This unique extradiol dioxygenase, CarB, had significantly higher affinity and about 20-times-higher meta-cleavage activity for 2,3-dihydroxybiphenyl than for catechol derivatives. The putative polypeptide encoded by ORF3 was homologous with meta-cleavage compound hydrolases in other bacteria, and ORF3 was designated carC. The hydrolase activity of CarC for 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, the meta-cleavage compound of 2,3-dihydroxybiphenyl, was 40 times higher than that for 2-hydroxy-6-oxohepta-2,4-dienoic acid, the meta-cleavage compound of 3-methylcatechol. Alignment analysis and the phylogenetic tree indicate that CarC has greatest homologies with hydrolases involved in the monoaromatic compound degradation pathway. These results suggest the possibility that CarC is a novel type of hydrolase.

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“…The nucleotide sequence of ORF6 showed 58.0, 57.1, and 57.1% homologies with the ferredoxin components of chlorobenzene dioxygenase (41), biphenyl dioxygenase (27), and toluene dioxygenase (43), respectively. The consensus sequence of Rieske-type iron-sulfur proteins for the binding of a [2Fe-2S] cluster (32) was also found in ORF6.…”

Section: Resultsmentioning

confidence: 99%

Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10

et al. 1997

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Nucleotide sequence analysis of the flanking regions of the carBC genes of Pseudomonas sp. strain CA10 revealed that there were two open reading frames (ORFs) ORF4 and ORF5, in the upstream region of carBC. Similarly, three ORFs, ORF6 to ORF8, were found in the downstream region of carBC. The deduced amino acid sequences of ORF6 and ORF8 showed homologies with ferredoxin and ferredoxin reductase components of bacterial multicomponent dioxygenase systems, respectively. ORF4 and ORF5 had the same sequence and were tandemly linked. Their deduced amino acid sequences showed about 30% homology with large (␣) subunits of other terminal oxygenase components. Functional analysis using resting cells harboring the deleted plasmids revealed that the products of ORF4 and -5, ORF6, and ORF8 were terminal dioxygenase, ferredoxin, and ferredoxin reductase, respectively, of carbazole 1,9a-dioxygenase (CARDO), which attacks the angular position adjacent to the nitrogen atom of carbazole, and that the product of ORF7 is not indispensable for CARDO activity. Based on the results, ORF4, ORF5, ORF6, and ORF8 were designated carAa, carAa, carAc, and carAd, respectively. The products of carAa, carAd, and ORF7 were shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be polypeptides with molecular masses of 43, 36, and 11 kDa, respectively. However, the product of carAc was not detected in Escherichia coli. CARDO has the ability to oxidize a wide variety of polyaromatic compounds, including dibenzo-p-dioxin, dibenzofuran, biphenyl, and polycyclic aromatic hydrocarbons such as naphthalene and phenanthrene. Since 2,2,3-trihydroxydiphenyl ether and 2,2,3-trihydroxybiphenyl were identified as metabolites of dibenzo-p-dioxin and dibenzofuran, respectively, it was considered that CARDO attacked at the angular position adjacent to the oxygen atom of dibenzo-p-dioxin and dibenzofuran as in the case with carbazole.Microbial degradation of xenobiotics such as polycyclic aromatic hydrocarbons, heterocyclic polyaromatics, and halogenated aromatics and aliphatics is quite useful to detoxify and mineralize these pollutants and thus is an important goal of research related to bioremediation. Among these pollutants, polychlorinated dibenzo-p-dioxin (DD), dibenzofuran (DBF), and carbazole (CAR) are well known to possess strong mutagenic and toxic activities (2) and also to be recalcitrant molecules (7). A critical point in the degradative pathways of these compounds is the initial oxidation of the chemically stable aromatic ring. In the aerobic degradation of many aromatic compounds, the multicomponent aromatic ring dioxygenases are very important enzyme complexes, consisting of two or three protein components (17, 28). Multicomponent dioxygenases catalyze a redox reaction in which molecular oxygen atoms are incorporated into the aromatic ring at the expense of the oxidation of NAD(P)H (17, 28). The recalcitrance of these xenobiotic compounds is considered to be due to requirement of rare and unique aromatic ring oxygenases for degrada...

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The Broad Substrate Chlorobenzene Dioxygenase and cis-Chlorobenzene Dihydrodiol Dehydrogenase of Pseudomonas sp. Strain P51 Are Linked Evolutionarily to the Enzymes for Benzene and Toluene Degradation

Cited by 121 publications

References 48 publications

Amino Acids in Positions 48, 52, and 73 Differentiate the Substrate Specificities of the Highly Homologous Chlorocatechol 1,2-Dioxygenases CbnA and TcbC

Amino Acids in Positions 48, 52, and 73 Differentiate the Substrate Specificities of the Highly Homologous Chlorocatechol 1,2-Dioxygenases CbnA and TcbC

Cloning of genes involved in carbazole degradation of Pseudomonas sp. strain CA10: nucleotide sequences of genes and characterization of meta-cleavage enzymes and hydrolase

Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10

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