Triphenyltin degradation and proteomic response by an engineered Escherichia coli expressing cytochrome P450 enzyme.
Ecotoxicol Environ Saf
; 137: 29-34, 2017 Mar.
Article
em En
| MEDLINE
| ID: mdl-27907843
ABSTRACT
Although triphenyltin (TPT) degradation pathway has been determined, information about the enzyme and protein networks involved was severely limited. To this end, a cytochrome P450 hydroxylase (CYP450) gene from Bacillus thuringiensis was cloned and expressed in Escherichia coli BL21 (DE3), namely E. coli pET32a-CYP450, whose dosage at 1gL-1 could degrade 54.6% TPT at 1mgL-1 within 6 d through attacking the carbon-tin bonds of TPT by CYP450. Sequence analysis verified that the CYP450 gene had a 1214bp open reading frame, encoding a protein with 404 amino acids. Proteomic analysis determined that 60 proteins were significantly differentially regulated expression in E. coli pET32a-CYP450 after TPT degradation. The up-regulated proteins enriched in a network related to transport, cell division, biosynthesis of amino acids and secondary metabolites, and microbial metabolism in diverse environments. The current findings demonstrated for the first time that P450 received electrons transferring from NADH could effectively cleave carbon-metal bonds.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Compostos Orgânicos de Estanho
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Proteoma
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Sistema Enzimático do Citocromo P-450
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Poluentes Ambientais
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Escherichia coli
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article