Chlorocatechols Substituted at Positions 4 and 5 Are Substrates of the Broad-Spectrum Chlorocatechol 1,2-Dioxygenase of
            <i>Pseudomonas chlororaphis</i>
            RW71

Potrawfke, Thomas; Armengaud, Jean; Wittich, Rolf-Michael

doi:10.1128/jb.183.3.997-1011.2001

Cited by 49 publications

(38 citation statements)

References 71 publications

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“…The exceptions to the Leu-48 and Ile-73 rule are TcbC; TetC (Val-73) of Pseudomonas chlororaphis RW71 (46), which is highly homologous to CbnA; and DccA I and DccA II of Sphingomonas herbicidovorans MH (Leu-73) (36). However, TetC, with Leu in position 48, exhibits threefold-higher catalytic activity for 3,5-DC than for 3,4-DC (46). The difference in the residues in the position 73 between the highly similar CCDs CbnA and TetC suggests that they could have slightly different substrate specificities.…”

Section: Discussionmentioning

confidence: 99%

“…When identity between the corresponding genes of the two clusters is compared at the amino acid sequence level, it is the lowest between CbnA and TcbC (95%) (40). Among the chlorocatechol ortho-cleavage gene clusters reported thus far, two chlorocatechol gene clusters (the tetRCDorfXEF gene cluster of chlorobenzene-degrading P. chlororaphis RW71 and the tfdRCDorfIEF gene cluster of 2,4-D-degrading Delftia acidovorans P4a) constitute a highly homologous subgroup together with the cbn and tcb clusters with identical lengths of the corresponding genes, and the two clusters are more homologous to the cbn cluster than to the tcb cluster (28,46). The N-terminal regions of CbnA, TetC, and TcbC differ only in five positions (46,48,52,70, and 73).…”

Section: Discussionmentioning

confidence: 99%

“…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.…”

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confidence: 99%

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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%

Section: Discussionmentioning

confidence: 99%

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

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“…Aromatic compounds containing more than two chlorine atoms are converted to hydroxyquinol or chlorohydroxyquinols and then cleaved by specific intradiol dioxygenases (Scheme 1) (12)(13)(14)(15)(16)(17)(18). A few interesting exceptions have been observed (7)(8)(9).…”

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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.…”

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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

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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.

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Development and Application of PCR Primers for the Detection of thetfd Genes inDelftia acidovorans P4a Involved in the Degradation of 2,4-D

et al. 2001

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Primers specific for the genes tfdD, tfdE and tfdF, derived from conserved amino acid sequence motifs of the corresponding homologous enzymes, and primers specific for the genes tfdA and tfdB as well as tfdC taken from the literature were applied in PCR reactions using the genomic DNA of Delftia acidovorans P4a as the template. PCR products were obtained with all primer pairs that were similar in size to those found with the genomic DNA of strains harbouring plasmid pJP4 as the carrier of tfd genes. The nucleotide sequences and the corresponding amino acid sequences of the PCR products obtained with Strain P4a were compared with the sequence databases. According to BLAST analyses, the partial sequences of tfdA and tfdB exhibited a 94-99% degree of identity with the homologous sequences of the 2,4-D-degrading strains Achromobacter xylosoxidans subsp. denitrificans EST4002 (pEST4011), Burkholderia sp. RASC, Variovorax paradoxus TV1 (pTV1) and Burkholderia cepacia 2a (pIJB1), whereas the partial sequences of the tfdC, tfdD, tfdE and tfdF genes revealed a 96-100% degree of identity with the homologous sequences of the chlorobenzene-utilizing strains Ralstonia eutropha NH9 (pENH91), Pseudomonas chlororaphis RW71 and Pseudomonas sp. P51 (pP51).

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Chlorocatechols Substituted at Positions 4 and 5 Are Substrates of the Broad-Spectrum Chlorocatechol 1,2-Dioxygenase of Pseudomonas chlororaphis RW71

Cited by 49 publications

References 71 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

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

Development and Application of PCR Primers for the Detection of thetfd Genes inDelftia acidovorans P4a Involved in the Degradation of 2,4-D

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