Novel 4-chlorophenoxyacetate dioxygenase-mediated phenoxyalkanoic acid herbicides initial catabolism in Cupriavidus sp. DL-D2

文献类型： 外文期刊

第一作者： Yang, Hao

作者： Yang, Hao;Liu, Shiyan;Chen, Sitong;Lu, Peng;Liu, Hongming;Yang, Hao;Liu, Shiyan;Chen, Sitong;Lu, Peng;Liu, Hongming;Huang, Junwei;Sun, Lina

作者机构：

关键词： 4-Chlorophenoxyacetic acid; Cupriavidus; cpd gene cluster; dioxygenase; Bacterial degradation

期刊名称：JOURNAL OF HAZARDOUS MATERIALS （ 影响因子：12.2； 五年影响因子：11.9 ）

ISSN： 0304-3894

年卷期： 2024 年 478 卷

页码：

收录情况： SCI

摘要： Microbial metabolism is an important driving force for the elimination of 4-chlorophenoxyacetic acid residues in the environment. The alpha-Ketoglutarate-dependent dioxygenase (TfdA) or 2,4-D oxygenase (CadAB) catalyzes the cleavage of the aryl ether bond of 4-chlorophenoxyacetic acid to 4-chlorophenol, which is one of the important pathways for the initial metabolism of 4-chlorophenoxyacetic acid by microorganisms. However, strain Cupriavidus sp. DL-D2 could utilize 4-chlorophenoxyacetic acid but not 4-chlorophenol for growth. This scarcely studied degradation pathway may involve novel enzymes that has not yet been characterized. Here, a gene cluster (designated cpd) responsible for the catabolism of 4-chlorophenoxyacetic acid in strain DL-D2 was cloned and identified, and the dioxygenase CpdA/CpdB responsible for the initial degradation of 4-chlorophenoxyacetic acid was successfully expressed, which could catalyze the conversion of 4-chlorphenoxyacetic acid to 4-chlorocatechol. Then, an aromatic cleavage enzyme CpdC further converts 4-chlorocatechol into 3-chloromuconate. The results of substrate degradation experiments showed that CpdA/CpdB could also degrade 3-chlorophenoxyacetic acid and phenoxyacetic acid, and homologous cpd gene clusters were widely discovered in microbial genomes. Our findings revealed a novel degradation mechanism of 4-chlorophenoxyacetic acid at the molecular level.

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