A high level of accumulation of 2-hydroxymuconic 6-semialdehyde from aniline by the transpositional mutant Y-2 of Pseudomonas species AW-2

Aoki, Kenji; Kodama, Noriko; Murakami, Shinichiro; Shinke, Ryu

doi:10.1016/s0944-5013(97)80003-1

Cited by 10 publications

(6 citation statements)

References 15 publications

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“…2-Aminophenol 1,6-dioxygenase was prepared, as described previously (Takenaka et al 1997). 2-Hydroxymuconic 6-semialdehyde, 2-oxopent-4-enoic acid, and 2-amino-2,4-pentadienoic acid were synthesized by the methods of Aoki et al (1997b), Collinsworth et al (1973, and Marcotte and Walsh (1978), respectively. 2-Aminomuconic acid was prepared by the method of He and Spain (1997).…”

Section: Chemicalsmentioning

confidence: 99%

Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3

Takenaka

Murakami

Kim

et al. 2000

Archives of Microbiology

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A 13.9-kb region, which contained the 2-aminophenol 1,6-dioxygenase genes (amnBA) reported before, was cloned from the 2-aminophenol-assimilating bacterium Pseudomonas sp. AP-3. The complete nucleotide sequence of this region was determined and six genes were found downstream of amnBA. The eight genes together were designated amnBACFEDHG. Each gene was similar to the corresponding gene operating in the meta-cleavage pathway, except for amnB, amnA, and amnD. The four 2-aminophenol-metabolizing enzymes, 2-aminomuconic 6-semialdehyde dehydrogenase, 2-aminomuconate deaminase, 4-oxalocrotonate decarboxylase, and 2-oxopent-4-enoate hydratase, were purified and characterized. NH2-terminal amino acid sequences of each purified enzyme agreed with those deduced from amnC, amnF, amnE, and amnD, respectively. These genes were therefore assigned as the genes encoding these respective proteins. The tight clustering of the amn genes, which were all transcribed in the same direction, raised the possibility that these genes formed a single operon. The organization of the amn genes was entirely different from that of the atd, dmp, and xyl genes reported in the meta-cleavage pathway, although these latter genes clustered similarly.

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Section: Chemicalsmentioning

confidence: 99%

Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3

Takenaka

Murakami

Kim

et al. 2000

Archives of Microbiology

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“…Species of Alcaligenes (Rhodes, 1970), Pseudomonas (Anson & Mackinnon, 1984;Aoki et al, 1997;Travkin et al, 2003), Acinetobacter (Kim et al, 1997), Rhodococcus (Aoki et al, 1983;Fuchs et al, 1991), Frateuria (Aoki et al, 1984), Moraxella (Zeyer et al, 1985), Nocardia (Bachofer et al, 1975) and Delftia (Kahng et al, 2000;Boon et al, 2001;Liu et al, 2002) are able to degrade aniline and/ or its derivatives. Moreover, plasmid-dependent aniline degradation has been reported in several bacterial strains (Anson & Mackinnon, 1984;Latorre et al, 1984;McClure & Venables, 1987;Fujii et al, 1997;Boon et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Chromosome-encoded gene cluster for the metabolic pathway that converts aniline to TCA-cycle intermediates in Delftia tsuruhatensis AD9

et al. 2005

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Delftia tsuruhatensis AD9 was isolated as an aniline-degrading bacterium from the soil surrounding a textile dyeing plant. The gene cluster involved in aniline degradation was cloned from the total DNA of strain AD9 into Escherichia coli JM109. After shotgun cloning, two recombinant E. coli strains showing aniline oxidation activity or catechol meta-cleavage activity were obtained by simple plate assays. These strains contained 9?3 kb and 15?4 kb DNA fragments, respectively. Sequence analysis of the total 24?7 kb region revealed that this region contains a gene cluster (consisting of at least 17 genes, named tadQTA1A2BRD1C1D2C2EFGIJKL) responsible for the complete metabolism of aniline to TCA-cycle intermediates. In the gene cluster, the first five genes (tadQTA1A2B) and the subsequent gene (tadR) were predicted to encode a multi-component aniline dioxygenase and a LysR-type regulator, respectively, while the others (tadD1C1D2C2EFGIJKL) were expected to encode meta-cleavage pathway enzymes for catechol degradation. In addition, it was found that the gene cluster is surrounded by two IS1071 sequences, indicating that it has a class I transposon-like structure. PFGE and Southern hybridization analyses confirmed that the tad gene cluster is encoded on the chromosome of strain AD9 in a single copy. These results suggest that, in strain AD9, aniline is degraded via catechol through a meta-cleavage pathway by the chromosome-encoded tad gene cluster. The tad gene cluster showed significant similarity in nucleotide sequence and genetic organization to the plasmid-encoded aniline degradation gene cluster of Pseudomonas putida UCC22.

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“…The transposon‐insertion mutant strain Y‐2 of the aniline‐assimilating Pseudomonas sp. AW‐2 was cultured as described in Aoki et al (1997). The dioxygenase gene ( ahdA ) was expressed in E. coli (pAHDA2) following previously reported methods (Murakami et al , 2004).…”

Section: Methodsmentioning

confidence: 99%

Gene cloning and characterization of a deaminase from the 4-amino-3-hydroxybenzoate-assimilatingBordetellasp. strain 10d

Takenaka

Satō

Koshiya

et al. 2009

FEMS Microbiology Letters

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The 4-amino-3-hydroxybenzoate-assimilating Bordetella sp. strain 10d produces a deaminase that catalyzes the deamination of 2-amino-5-carboxymuconic 6-semialdehyde. A gene encoding the deaminase, ahdB, was cloned and expressed in Escherichia coli; ahdB is located downstream from the previously reported genes encoding 4-amino-3-hydroxybenzoate 2,3-dioxygenase (ahdA) and a LysR-type regulator. The deduced amino acid sequence of ahdB shows 30-33% identity to those of previously reported 2-aminomuconate deaminases. We identified a region (RAGDFLXVSG) conserved in AhdB and three other deaminases. The recombinant enzyme AhdB was purified to homogeneity. After a coupled enzyme assay with purified AhdA, AhdB, and the substrate 4-amino-3-hydroxybenzoate, the final product, formed by the action of AhdA, AhdB, and by nonenzymatic decarboxylation, was identified by HPLC, MS, and (1)H-nuclear magnetic resonance analyses as 2-hydroxymuconic 6-semialdehyde.

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A high level of accumulation of 2-hydroxymuconic 6-semialdehyde from aniline by the transpositional mutant Y-2 of Pseudomonas species AW-2

Cited by 10 publications

References 15 publications

Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3

Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3

Chromosome-encoded gene cluster for the metabolic pathway that converts aniline to TCA-cycle intermediates in Delftia tsuruhatensis AD9

Gene cloning and characterization of a deaminase from the 4-amino-3-hydroxybenzoate-assimilatingBordetellasp. strain 10d

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