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Figure 1.

Sequence alignment of catechol 1,2-dioxygenase from Halomonas organivorans and related catechol 1,2-dioxygenases from halophilic bacteria.

Residues in boxes show the lipid-binding sites. Residues with asterisk show the active sites. Residues in discontinuous boxes indicate the Fe-ligands. Helices are labeled with arrows and strands with black sticks.

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Figure 1 Expand

Figure 2.

Comparative analysis of cat and ben genes from H. organivorans and other strains.

The direction of transcription is indicated by the arrowheads. catA, catechol 1,2-dioxygenase; catB, cis,cis-muconate cycloisomerase; catC, muconolactone delta-isomerase; catR, lysR-type transcriptional regulator; benA, benzoate 1,2-dioxygenase large subunit; benB, benzoate 1,2-dioxygenase small subunit; benC, benzoate 1,2-dioxygenase reductase subunit; benD, 1,6-dihydroxy cyclohexe-2,4-diene-1-carboxylate dehydrogenase; benE, MFS family benzoate membrane transporter; benK, benzoate transporter protein.

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Figure 2 Expand

Figure 3.

16S rRNA and catA gene-based phylogenic trees.

(A) Phylogenetic tree based on the analysis of nucleotide sequences of c. 1,500 bp of 16S rRNA gene from Halomonas organivorans and other degrading bacteria; (B) Phylogenetic tree based on the comparison of c. 840 bp of catA gene from Halomonas organivorans and other catA genes from related degrading bacteria. The trees are constructed using the software DNAstar Lasergene and the ClustalW method was used for the alignment. Branch lengths are proportional to the interfered phylogenetic distances.

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Figure 3 Expand

Figure 4.

Results of RT-PCR.

The PCR-products were amplified from cDNA template to prove the induction of the cat and ben genes in presence of glucose (G), benzoate (B) and phenol (P). catB/catC (881 bp); catC/catA (866 bp); benA/benB (197 bp).

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Figure 4 Expand

Table 1.

Activity of catechol 1,2-dioxygenase in extracts of the clone E. coli H7 cells grown in various substrates.

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Table 1 Expand