ArticleApplied and environmental microbiology2010
Characterization of the isophthalate degradation genes of Comamonas sp. strain E6.
Article in Applied and environmental microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 108 citations in OpenAlex.
- Biological Degradation of Phthalates: From Bioremediation to Plastic Waste Valorization.ChemSusChem · 2026Review
- Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025Review
- It Is Dangerous to Go Alone: Strategies to Optimize PET Biocatalysis and Upcycling through Enzymatic Synergism.ACS omega · 2025Review
- Structure-guided engineering of an aromatic ring-hydroxylating dioxygenase for broad-spectrum phthalate degradation.Journal of bacteriology · 2025Article
- Precise Transcription Control Drives Optimized Catabolism of β-5-Type Lignin-Derived Dimers inJournal of agricultural and food chemistry · 2025Article
- Differential effect of monoterpenes and flavonoids on the transcription of aromatic ring-hydroxylating dioxygenase genes inMicrobial genomics · 2025Article
- Discovery of a distinct type of methylenetetrahydrofolate reductase family that couples with tetrahydrofolate-dependent demethylases.Communications biology · 2025Article
- Biodegradation of phthalic acid and terephthalic acid by Comamonas testosteroni strains.Folia microbiologica · 2024Article
- Mechanisms and high-value applications of phthalate isomers degradation pathways in bacteria.World journal of microbiology & biotechnology · 2024Review
- Unveiling the regulatory mechanisms of salicylate degradation gene clusterApplied and environmental microbiology · 2023Article
- The Catabolic System of Acetovanillone and Acetosyringone inApplied and environmental microbiology · 2022Article
- Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural Insights into Dihydroxylation of Terephthalate, a Product of Polyethylene Terephthalate Degradation.Journal of bacteriology · 2022Article
- Biodegradation of aromatic pollutants meets synthetic biology.Synthetic and systems biotechnology · 2021Article
- 2,3-Dihydroxybenzoate meta-Cleavage Pathway is Involved in o-Phthalate Utilization in Pseudomonas sp. strain PTH10.Scientific reports · 2019Article
- Bacterial Catabolism of β-Hydroxypropiovanillone and β-Hydroxypropiosyringone Produced in the Reductive Cleavage of Arylglycerol-β-Aryl Ether in Lignin.Applied and environmental microbiology · 2018Article
- The XylS/Pm regulator/promoter system and its use in fundamental studies of bacterial gene expression, recombinant protein production and metabolic engineering.Microbial biotechnology · 2017Review
- Membrane-associated glucose-methanol-choline oxidoreductase family enzymes PhcC and PhcD are essential for enantioselective catabolism of dehydrodiconiferyl alcohol.Applied and environmental microbiology · 2015Article
- γ-Resorcylate catabolic-pathway genes in the soil actinomycete Rhodococcus jostii RHA1.Applied and environmental microbiology · 2015Article
- Draft Genome Sequence of Comamonas sp. Strain E6 (NBRC 107749), a Degrader of Phthalate Isomers through the Protocatechuate 4,5-Cleavage Pathway.Genome announcements · 2015Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The isophthalate (IPA) degradation gene cluster (iphACBDR) responsible for the conversion of IPA into protocatechuate (PCA) was isolated from Comamonas sp. strain E6, which utilizes phthalate isomers as sole carbon and energy sources via the PCA 4,5-cleavage pathway. Based on amino acid sequence similarity, the iphA, iphC, iphB, iphD, and iphR genes were predicted to code for an oxygenase component of IPA dioxygenase (IPADO), a periplasmic IPA binding receptor, a 1,2-dihydroxy-3,5-cyclohexadiene-1,5-dicarboxylate (1,5-DCD) dehydrogenase, a reductase component of IPADO, and an IclR-type transcriptional regulator, respectively. The iphACBDR genes constitute a single transcriptional unit, and transcription of the iph catabolic operon was induced during growth of E6 on IPA. The iphA, iphD, and iphB genes were expressed in Escherichia coli. Crude IphA and IphD converted IPA in the presence of NADPH into a product which was transformed to PCA by IphB. These results suggested that IPADO is a two-component dioxygenase that consists of a terminal oxygenase component (IphA) and a reductase component (IphD) and that iphB encodes the 1,5-DCD dehydrogenase. Disruption of iphA and iphB resulted in complete loss of growth of E6 on IPA. Inactivation of iphD significantly affected growth on IPA, and the iphC mutant did not grow on IPA at neutral pH. These results indicated that the iphACBD genes are essential for the catabolism of IPA in E6. Disruption of iphR resulted in faster growth of E6 on IPA, suggesting that iphR encodes a repressor for the iph catabolic operon. Promoter analysis of the operon supported this notion.
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