Cloning and characterization of a chromosome-encoded catechol 2,3-dioxygenase gene from Pseudomonas aeruginosa ZD 4-3

Chen, Y X; Liu, He; Zhu, Lizhong; Jin, Yongfeng

doi:10.1007/s11021-005-0010-2

Cited by 6 publications

(3 citation statements)

References 11 publications

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“…As a crucial enzyme involved in the degradation of aromatic hydrocarbons, catechol 2, 3-dioxygenase (C23O, key enzyme of meta -cleavage pathway) has been identified as one of the most widespread ring cleavage enzymes 22 and many C23Os have been reported from non-halophilic bacteria ( Pseudomonas , Sphingomonas , Acinetobacter , Bacillus , Ralstonia , Burkholderia and Nocardia ) 23 . As a member of extradiol dioxygenases, C23Os from non-halophiles had a well characterized phylogeny based on their amino acid sequences and could be divided into several subfamilies and families 24 25 .…”

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confidence: 99%

Isolation and characterization of two novel halotolerant Catechol 2, 3-dioxygenases from a halophilic bacterial consortium

Guo

Fang

Wang

et al. 2015

Sci Rep

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Study of enzymes in halophiles will help to understand the mechanism of aromatic hydrocarbons degradation in saline environment. In this study, two novel catechol 2,3-dioxygenases (C23O1 and C23O2) were cloned and overexpressed from a halophilic bacterial consortium enriched from an oil-contaminated saline soil. Phylogenetic analysis indicated that the novel C23Os and their relatives formed a new branch in subfamily I.2.A of extradiol dioxygenases and the sequence differences were further analyzed by amino acid sequence alignment. Two enzymes with the halotolerant feature were active over a range of 0–30% salinity and they performed more stable at high salinity than in the absence of salt. Surface electrostatic potential and amino acids composition calculation suggested high acidic residues content, accounting for their tolerance to high salinity. Moreover, two enzymes were further characterized. The enzymes activity both increased in the presence of Fe3+, Fe2+, Cu2+ and Al3+ and showed no significant inhibition by other tested metal ions. The optimal temperatures for the C23Os were 40 °C and 60 °C and their best substrates were catechol and 4-methylcatechol respectively. As the firstly isolated and characterized catechol dioxygenases from halophiles, the two halotolerant C23Os presented novel characteristics suggesting their potential application in aromatic hydrocarbons biodegradation.

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confidence: 99%

Isolation and characterization of two novel halotolerant Catechol 2, 3-dioxygenases from a halophilic bacterial consortium

Guo

Fang

Wang

et al. 2015

Sci Rep

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“…Phenylpropionate dioxygenase and related ringhydroxylating dioxygenases could be used to metabolize monocyclic or polycyclic aromatic compounds released by phytoplankton in the surface ocean and provide energy and carbon sources for SAR202 cells [16,18,19]. The ring-cleavage extradiol dioxygenase protein could be further annotated as catechol 2,3-dioxygenase, which was one of the most important enzymes in the degradation pathway of aromatic compounds, and could catalyze catechol to 2-hydroxymuconate-6-semialdehyde [45,46]. The transcripts of those genes were only detected in SAR202 subcluster III, suggesting that subcluster III was one of the important consumers for refractory organic carbon in the deep sea as reported in previous studies [17,18].…”

Section: Carbon Sources For Each Sar202 Subclustermentioning

confidence: 99%

In Situ Genomics and Transcriptomics of SAR202 Subclusters Revealed Subtle Distinct Activities in Deep-Sea Water

Wei

et al. 2022

Microorganisms

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Deep-sea water columns are enriched with SAR202 that may conduct detrital matter degradation. There are several subclusters in SAR202, but their subtle differences in geochemical cycles are largely unknown, particularly for their in situ activities in the marine deep zone. Deep-sea DNA/RNA samples obtained from 12 continuous time periods over two days by in situ nucleic acid collection apparatus were used to re-evaluate the ecological functions of each SAR202 subcluster at a depth of ~1000 m in the South China Sea (SCS). Phylogenomics of 32 new SAR202 genomes from the SCS and western Pacific revealed their distribution in five subclusters. Metatranscriptomics analysis showed that the subclusters II and III were the dominant SAR202 groups with higher transcriptional activities in the SCS deep-sea zone than other subclusters. The analyses of functional gene expression further indicated that SAR202 subclusters II and III might be involved in different metabolic pathways in the deep-sea environment. The SAR202 subcluster III might take part in the degradation of deep-sea aromatic compounds. Time-course metagenomics and metatranscriptomics data did not show metabolic correlation of subclusters II and III over two days, suggesting diversified ecological functions of SAR202 subclusters under different organic inputs from the overlying water column. Collectively, our results indicate that the SAR202 subclusters play different roles in organic degradation and have probably undergone subtle and gradual adaptive evolution in the dynamic environment of the deep ocean.

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“…Catechol 2,3‐dioxygenase (C23O, EC 1.13.11.2), which catalyzes the dioxygenation of catechol to form 2‐hydroxymuconate semialdehyde, is one of the most important enzymes in many bacterial pathways for the degradation of aromatic compounds . Due to its potential application in environmental protection, C23O has been purified from a variety of organisms including Alcaligenes , Bacillus , Planococcus , Pseudomonas , Stenotrophomonas , Variovorax , and Sphingomonas .…”

Section: Introductionmentioning

confidence: 99%

Catechol 2,3‐dioxygenase from a new phenolic compound degrader Thauera sp. K11: purification and biochemical characterization

Liu

Wang

et al. 2018

J Basic Microbiol

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Catechol 2,3-dioxygenase (C23O) from a new phenolic compound degrader Thauera sp. K11 was purified and characterized. The native form of the enzyme was determined as a homotetramer with a molecular weight of 140 kDa, and its isoelectric point was close to 6.4. One iron per enzyme subunit was detected using atom absorption spectroscopy, and the effective size of C23O in its dilute solution (0.2 g L , pH 8.0) was 14.5 nm. The optimal pH and temperature were 8.4 and 45 °C, respectively. The addition of Mg , Cu , Fe , and Mn could improve the enzyme activity, while Ag was found to be a strong inhibitor. C23O was stable in alkali conditions (pH 7.6-11.0) and thermostable below 50 °C. The final purified C23O had a sheet content of 53%, consistent with the theoretical value. This showed that the purified catechol 2,3-dioxygenase folded with a reasonable secondary structure.

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Cloning and characterization of a chromosome-encoded catechol 2,3-dioxygenase gene from Pseudomonas aeruginosa ZD 4-3

Cited by 6 publications

References 11 publications

Isolation and characterization of two novel halotolerant Catechol 2, 3-dioxygenases from a halophilic bacterial consortium

Isolation and characterization of two novel halotolerant Catechol 2, 3-dioxygenases from a halophilic bacterial consortium

In Situ Genomics and Transcriptomics of SAR202 Subclusters Revealed Subtle Distinct Activities in Deep-Sea Water

Catechol 2,3‐dioxygenase from a new phenolic compound degrader Thauera sp. K11: purification and biochemical characterization

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