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PubMed1997

Classification of catechol 1,2-dioxygenase family: sequence analysis of a gene for the catechol 1,2-dioxygenase showing high specificity for methylcatechols from Gram+ aniline-assimilating Rhodococcus erythropolis AN-13.

Gram+ aniline-assimilating Rhodococcus erythropolis AN-13 (AN-13) produces catechol 1,2-dioxygenase (C12O) showing high enzymatic activities for 3- and 4-methylcatechols [Aoki et al. (1984) Agric. Biol. Chem. 48, 2087-2095]. A 3.0 kb Sau3AI fragment carrying a gene encoding C12O(catA) was cloned by selection of transformants showing C12O activity from a gene library of AN-13. Furthermore, we specified a 1.6 kb SalI fragment containing catA from the Sau3AI fragment by subcloning. Sequence analysis revealed that the 1.6 kb SalI fragment carried a 855 bp open reading frame (ORF) encoding the entire AN-13 catA, preceded by a potential ribosome binding site (RBS). From comparison of the deduced amino acid (aa) sequence of C12O from AN-13 with other C12O reported previously, it was found that the AN-13 enzyme shares 56.0% aa sequence identity with C12o from Arthrobacter sp. mA3 (mA3) [Eck and Belter (1991) Gene 123, 87-92] compared with less than 36.4% aa sequence identities with others. In conclusion, we classified all C12O including the AN-13 enzyme into three subfamilies on the basis of similarity of aa sequences, numbers of aa residues, and substrate specificity.

Amino Acid Sequence↗

PubMed1991

Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster, which encodes metabolism of chlorinated catechols: evidence for specialization of catechol 1,2-dioxygenases for chlorinated substrates.

Pseudomonas sp. strain P51 contains two gene clusters located on catabolic plasmid pP51 that encode the degradation of chlorinated benzenes. The nucleotide sequence of a 5,499-bp region containing the chlorocatechol-oxidative gene cluster tcbCDEF was determined. The sequence contained five large open reading frames, which were all colinear. The functionality of these open reading frames was studied with various Escherichia coli expression systems and by analysis of enzyme activities. The first gene, tcbC, encodes a 27.5-kDa protein with chlorocatechol 1,2-dioxygenase activity. The tcbC gene is followed by tcbD, which encodes cycloisomerase II (39.5 kDa); a large open reading frame (ORF3) with an unknown function; tcbE, which encodes hydrolase II (25.8 kDa); and tcbF, which encodes a putative trans-dienelactone isomerase (37.5 kDa). The tcbCDEF gene cluster showed strong DNA homology (between 57.6 and 72.1% identity) and an organization similar to that of other known plasmid-encoded operons for chlorocatechol metabolism, e.g., clcABD of Pseudomonas putida and tfdCDEF of Alcaligenes eutrophus JMP134. The identity between amino acid sequences of functionally related enzymes of the three operons varied between 50.6 and 75.7%, with the tcbCDEF and tfdCDEF pair being the least similar of the three. Measurements of the specific activities of chlorocatechol 1,2-dioxygenases encoded by tcbC, clcA, and tfdC suggested that a specialization among type II enzymes has taken place. TcbC preferentially converts 3,4-dichlorocatechol relative to other chlorinated catechols, whereas TfdC has a higher activity toward 3,5-dichlorocatechol. ClcA takes an intermediate position, with the highest activity level for 3-chlorocatechol and the second-highest level for 3,5-dichlorocatechol.

Amino Acid Sequence↗

PubMed1999

Paramagnetic Zinc(II) Complexes of a Bis(catechol): Dependence of Product Spin State on Tautomerization of the Bis(catechol) Ligand.

We report the preparation and characterization of zinc(II) hydrotris(3-cumenyl-5-methylpyrazolyl)borate (LZn) complexes, (LZn)(2)()1'-H and (LZn)(2)()1, of a bis(catechol) ligand. The formation of (LZn)(2)()1'-H, an S = (1)/(2) complex, rather than (LZn)(2)()1, an S = 1 complex, is observed due to tautomerization of a reaction intermediate. The biradical complex, (LZn)(2)()1, can be prepared from (LZn)(2)()1'-H by oxidation, a conversion that is accompanied by a blue-green to red-purple color change and an increase in spin from (1)/(2) to 1. The frozen solution EPR spectrum of the biradical complex (LZn)(2)()1 exhibits zero-field splitting and a Deltam(s)() = 2 transition characteristic of a triplet state. The temperature dependence of the EPR signal intensity is consistent with high-spin coupling of the unpaired electrons of the ligand.

Journal Article↗

PubMed1964