The mechanism of anthracene degradation by tryptophan -2,3-dioxygenase (T23D) in Comamonas testosteroni
Copyright © 2024 Elsevier B.V. All rights reserved..
It is well known that anthracene is a persistent organic pollutant. Among the four natural polycyclic aromatic hydrocarbons (PAHs) degrading strains, Comamonas testosterone (CT1) was selected as the strain with the highest degradation efficiency. In the present study, prokaryotic transcriptome analysis of CT1 revealed an increase in a gene that encodes tryptophane-2,3-dioxygenase (T23D) in the anthracene and erythromycin groups compared to CK. Compared to the wild-type CT1 strain, anthracene degradation by the CtT23D knockout mutant (CT-M1) was significantly reduced. Compared to Escherichia coli (DH5α), CtT23D transformed DH5α (EC-M1) had a higher degradation efficiency for anthracene. The recombinant protein rT23D oxidized tryptophan at pH 7.0 and 37 °C with an enzyme activity of 2.42 ± 0.06 μmol min-1·mg-1 protein. In addition, gas chromatography-mass (GC-MS) analysis of anthracene degradation by EC-M1 and the purified rT23D revealed that 2-methyl-1-benzofuran-3-carbaldehyde is an anthracene metabolite, suggesting that it is a new pathway.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:393 |
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| Enthalten in: |
Chemico-biological interactions - 393(2024) vom: 25. Apr., Seite 110950 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Xu, Miao [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 08.04.2024 Date Revised 08.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.cbi.2024.110950 |
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| Förderinstitution / Projekttitel: |
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| 245 | 1 | 4 | |a The mechanism of anthracene degradation by tryptophan -2,3-dioxygenase (T23D) in Comamonas testosteroni |
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| 520 | |a It is well known that anthracene is a persistent organic pollutant. Among the four natural polycyclic aromatic hydrocarbons (PAHs) degrading strains, Comamonas testosterone (CT1) was selected as the strain with the highest degradation efficiency. In the present study, prokaryotic transcriptome analysis of CT1 revealed an increase in a gene that encodes tryptophane-2,3-dioxygenase (T23D) in the anthracene and erythromycin groups compared to CK. Compared to the wild-type CT1 strain, anthracene degradation by the CtT23D knockout mutant (CT-M1) was significantly reduced. Compared to Escherichia coli (DH5α), CtT23D transformed DH5α (EC-M1) had a higher degradation efficiency for anthracene. The recombinant protein rT23D oxidized tryptophan at pH 7.0 and 37 °C with an enzyme activity of 2.42 ± 0.06 μmol min-1·mg-1 protein. In addition, gas chromatography-mass (GC-MS) analysis of anthracene degradation by EC-M1 and the purified rT23D revealed that 2-methyl-1-benzofuran-3-carbaldehyde is an anthracene metabolite, suggesting that it is a new pathway | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a 2-Methyl-1-benzofuran-3-carbaldehyde | |
| 650 | 4 | |a Degradation pathway | |
| 650 | 4 | |a Genetic manipulation | |
| 650 | 4 | |a Prokaryotic transcriptome analysis | |
| 650 | 4 | |a Tryptophane-2,3-dioxygenase | |
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| 700 | 1 | |a Zhang, Jinyuan |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Dong |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Chuanzhi |e verfasserin |4 aut | |
| 700 | 1 | |a Wu, Ming |e verfasserin |4 aut | |
| 700 | 1 | |a Musazade, Elshan |e verfasserin |4 aut | |
| 700 | 1 | |a Maser, Edmund |e verfasserin |4 aut | |
| 700 | 1 | |a Xiong, Guangming |e verfasserin |4 aut | |
| 700 | 1 | |a Guo, Liquan |e verfasserin |4 aut | |
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