Genetic diversity of catechol 1,2-dioxygenase in the fecal microbial metagenome

Xu, Baojun; Xiong, Caiyun; Deng, Meng; Li, Junjun; Tang, Xianghua; Wu, Qian; Zhou, Junpei; Yang, Yunjuan; Ding, Junmei; Han, Nanyu; Huang, Zunxi

doi:10.1002/jobm.201700106

Cited by 7 publications

(2 citation statements)

References 51 publications

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“…and Geobacillus sp. (Giedraityte and Kalėdienė, 2009;Lin and Milase, 2015;Xu et al, 2017) but a lower proficiency than dioxygenases from Acinetobacter radioresistens LGM S13, Rhodococcus rhodochrous NCIMB 13259 and Rhodococcus opacus 1CP (Caglio et al, 2009;Subbotina et al, 2016).…”

Section: Kinetic Parameters Effects Of Ions and Substrate Specificity Of Psc12domentioning

confidence: 94%

Characterization of a Novel Functional Trimeric Catechol 1,2-Dioxygenase From a Pseudomonas stutzeri Isolated From the Gulf of Mexico

et al. 2020

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Catechol 1,2 dioxygenases (C12DOs) have been studied for its ability to cleavage the benzene ring of catechol, the main intermediate in the degradation of aromatic compounds derived from aerobic degradation of hydrocarbons. Here we report the genome sequence of the marine bacterium Pseudomonas stutzeri GOM2, isolated from the southwestern Gulf of Mexico, and the biochemical characterization of its C12DO (PsC12DO). The catA gene, encoding PsC12DO of 312 amino acid residues, was cloned and expressed in Escherichia coli. Many C12DOs have been described as dimeric enzymes including those present in Pseudomonas species. The purified PsC12DO enzyme was found as an active trimer, with a molecular mass of 107 kDa. Increasing NaCl concentration in the enzyme reaction gradually reduced activity; in high salt concentrations (0.7 M NaCl) quaternary structural analysis determined that the enzyme changes to a dimeric arrangement and causes a 51% decrease in specific activity on catechol substrate. In comparison with other C12DOs, our enzyme showed a broad range of action for PsC12DO in solutions with pH values ranging from neutral to alkaline (70%). The enzyme is still active after incubation at 50 • C for 30 min and in low temperatures to long term storage after 6 weeks at 4 • C (61%). EDTA or Ca 2+ inhibitors cause no drastic changes on residual activity; nevertheless, the activity of the enzyme was affected by metal ions Fe 3+ , Zn 2+ and was completely inhibited by Hg 2+ . Under optimal conditions the k cat and K m values were 16.13 s −1 and 13.2 µM, respectively. To our knowledge, this is the first report describing the characterization of a marine C12DOs from P. stutzeri isolated from the Gulf of Mexico that is active in a trimeric state. We consider that our enzyme has important features to be used in environments in presence of EDTA, metals and salinity conditions.

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Section: Kinetic Parameters Effects Of Ions and Substrate Specificity Of Psc12domentioning

confidence: 94%

Characterization of a Novel Functional Trimeric Catechol 1,2-Dioxygenase From a Pseudomonas stutzeri Isolated From the Gulf of Mexico

et al. 2020

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“…Catechol dioxygenase is the key enzyme to degrade catechol. Under the catalysis of catechol dioxygenase, polycyclic aromatic hydrocarbons are converted into long carbon chains and enter the tricarboxylic acid cycle, and then degrade into carbon dioxide and water [38]. According to the different ring opening positions, catechol dioxygenase can be divided into catechol 1, 2-dioxygenase (C 12 O) and catechol 2, 3-dioxygenase (C 23 O) [39].…”

Section: Changes In Enzyme Activitymentioning

confidence: 99%

Mechanism of Zn(II) enhanced biodegradation of m-dichlorobenzene

Shang

Yang

et al. 2021

Environmental Pollutants and Bioavailability

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M-dichlorobenzene can be degraded through biotrickling filter (BTF). However, its degradation needs to be enhanced, and the mechanism of enhancement is unclear. In this study, Zn(II) was taken as the biological growth promoter; the polysaccharides and proteins, zeta potential, Fourier transform infrared spectroscopy, x-ray photoelectron spectroscopy, and the enzyme activity of the strains were analyzed. The results indicated that Zn(II) at 5mg/L promoted the growth of the strain. When the inlet concentration was 505.74 mg/m 3 and the empty bed resistance time (EBRT) was 90 s, the removal efficiency of BTF2 was 86.15%. In BTF2, the enzyme activity, polysaccharide, and protein content increased, while the zeta potential decreased. The changes of zeta potential indicated that there existed an electrostatic interaction between extracellular polymeric substance (EPS) and Zn(II). The results of Fourier transform infrared spectroscopy and x-ray photoelectron spectroscopy confirmed that there was a bond between the EPS surface functional groups and Zn(II).

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A Novel Cold‐Adapted Catechol 1,2‐Dioxygenase From Antarctic Sea‐Ice Bacterium Halomonas sp. ANT108: Characterization and Immobilization

Wang,

Zhang,

Wang

et al. 2024

Journal of Basic Microbiology

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The enzyme catechol 1,2‐dioxygenase (CAT) plays a critical role in the biosynthesis pathway of cis, cis‐muconic acid (CCMA), which serves as an indispensable raw material for various industrial applications. In this research, we cloned a novel cold‐adapted CAT (HaCAT) from the Antarctic sea ice bacterium Halomonas sp. ANT108. Homology modeling analysis revealed that HaCAT possessed the characteristic Fe3+ binding site and catalytic active site of typical CATs, and it exhibited unique structural adaptations to cold environments. The optimal temperature and pH for recombinant HaCAT (rHaCAT) were found to be 25°C and 6.5, respectively. At 0°C, the enzyme retained a maximum activity of 43.6%, and in the presence of 1.0 M NaCl, its activity reached 173.9%, demonstrating significant salt tolerance. Additionally, the Vmax and Km of rHaCAT were 6.68 μmol/min/mg and 128.90 μM at 25°C, respectively. Furthermore, rHaCAT was successfully immobilized in the metal‐organic framework ZIF‐8 and retained almost 50% of its activity after five reuse cycles, demonstrating excellent reusability. Overall, these results provided a new resource and theoretical foundation for the industrial biocatalytic production and modification of CAT.

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Genetic diversity of catechol 1,2-dioxygenase in the fecal microbial metagenome

Cited by 7 publications

References 51 publications

Characterization of a Novel Functional Trimeric Catechol 1,2-Dioxygenase From a Pseudomonas stutzeri Isolated From the Gulf of Mexico

Characterization of a Novel Functional Trimeric Catechol 1,2-Dioxygenase From a Pseudomonas stutzeri Isolated From the Gulf of Mexico

Mechanism of Zn(II) enhanced biodegradation of m-dichlorobenzene

A Novel Cold‐Adapted Catechol 1,2‐Dioxygenase From Antarctic Sea‐Ice Bacterium Halomonas sp. ANT108: Characterization and Immobilization

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