ArticleScientific reports2019
2,3-Dihydroxybenzoate meta-Cleavage Pathway is Involved in o-Phthalate Utilization in Pseudomonas sp. strain PTH10.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 15 citations in OpenAlex.
- Ancestral hydrocarbon metabolism enables PET degradation by a natural bacterial consortium.mSystems · 2026Article
- A novel phthalic acid degradation pathway in Klebsiella variicola SY1 and engineering the strain for degradation of multiple phthalate esters.World journal of microbiology & biotechnology · 2026Article
- Article
- Biological Degradation of Phthalates: From Bioremediation to Plastic Waste Valorization.ChemSusChem · 2026Review
- Environmental Impact of Xenobiotic Aromatic Compounds and Their Biodegradation Potential inInternational journal of molecular sciences · 2024Review
- Engineering bacterial biocatalysts for the degradation of phthalic acid esters.Microbial biotechnology · 2024Review
- Mechanisms and high-value applications of phthalate isomers degradation pathways in bacteria.World journal of microbiology & biotechnology · 2024Review
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Pseudomonas sp. strain PTH10 can utilize o-phthalate which is a key intermediate in the bacterial degradation of some polycyclic aromatic hydrocarbons. In this strain, o-phthalate is degraded to 2,3-dihydroxybenzoate and further metabolized via the 2,3-dihydroxybenzoate meta-cleavage pathway. Here, the opa genes which are involved in the o-phthalate catabolism were identified. Based on the enzymatic activity of the opa gene products, opaAaAbAcAd, opaB, opaC, and opaD were found to code for o-phthalate 2,3-dioxygenase, dihydrodiol dehydrogenase, 2,3-dihydroxybenzoate 3,4-dioxygenase, and 3-carboxy-2-hydroxymuconate-6-semialdehyde decarboxylase, respectively. Collectively, these enzymes are thought to catalyze the conversion of o-phthalate to 2-hydroxymuconate-6-semialdehyde. Deletion mutants of the above opa genes indicated that their products were required for the utilization of o-phthalate. Transcriptional analysis showed that the opa genes were organized in the same transcriptional unit. Quantitative analysis of opaAa, opaB, opaC, opaD, opaE, and opaN revealed that, except for opaB and opaC, all other genes were transcriptionally induced during growth on o-phthalate. The constitutive expression of opaB and opaC, and the transcriptional induction of opaD located downstream of opaB, suggest several possible internal promoters are existence in the opa cluster. Together, these results strongly suggest that the opa genes are involved in a novel o-phthalate catabolic pathway in strain PTH10.
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