The mechanism of anthracene degradation by tryptophan -2,3-dioxygenase (T23D) in Comamonas testosterone.
2-Methyl-1-benzofuran-3-carbaldehyde
Degradation pathway
Genetic manipulation
Prokaryotic transcriptome analysis
Tryptophane-2,3-dioxygenase
Journal
Chemico-biological interactions
ISSN: 1872-7786
Titre abrégé: Chem Biol Interact
Pays: Ireland
ID NLM: 0227276
Informations de publication
Date de publication:
11 Mar 2024
11 Mar 2024
Historique:
received:
20
01
2024
revised:
02
03
2024
accepted:
09
03
2024
pubmed:
14
3
2024
medline:
14
3
2024
entrez:
13
3
2024
Statut:
aheadofprint
Résumé
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
Identifiants
pubmed: 38479715
pii: S0009-2797(24)00096-6
doi: 10.1016/j.cbi.2024.110950
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
110950Informations de copyright
Copyright © 2024 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.