Chicken CYP1A5 is able to hydroxylate aflatoxin B1 to aflatoxin M1

文献类型： 外文期刊

第一作者： Yuan, Yiyang

作者： Yuan, Yiyang;Li, Mei;Qiu, Xinghui

作者机构：

关键词： Aflatoxin B 1; Aflatoxin M 1; Gallus gallus; Hydroxylation

期刊名称：TOXICON （ 影响因子：2.8； 五年影响因子：2.8 ）

ISSN： 0041-0101

年卷期： 2024 年 239 卷

页码：

收录情况： SCI

摘要： Aflatoxin B1 (AFB1), a naturally-occurring mycotoxin, can cause severe toxicological and carcinogenic effects in livestock and humans. Given that the chicken is one of the most important food-producing animals, knowledge regarding AFB1 metabolism and enzymes responsible for AFB1 transformation in the chicken has important implications for chicken production and food safety. Previously, we have successfully expressed chicken CYP1A5 and CYP3A37 monooxygenases in E. coli, and reconstituted them into a functional CYP system consisting of CYP1A5 or CYP3A37, CPR and cytochrome b5. In this study, we aimed to investigate the roles of CYP1A5 and CYP3A37 in the bioconversion of AFB1 to AFM1. Our results showed that chicken CYP1A5 was able to hydroxylate AFB1 to AFM1. The formation of AFM1 followed the typical Michaelis-Menten kinetics. The kinetics parameters of Vmax and Km were determined as 0.83 +/- 0.039 nmol/min/nmol P450 and 26.9 +/- 4.52 mu M respectively. Docking simulations further revealed that AFB1 adopts a "side -on" conformation in chicken CYP1A5, facilitating the hydroxylation of the C9a atom and the production of AFM1. On the other hand, AFB1 assumes a "face -on" conformation in chicken CYP3A37, leading to the displacement of the C9a atom from the heme iron and explaining the lack of AFM1 hydroxylation activity. The results demonstrate that chicken CYP1A5 possesses efficient hydroxylase activity towards AFB1 to form AFM1.

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