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Int. J. Mol. Sci. 2013, 14(6), 10809-10818;

Chicken Cytochrome P450 1A5 Is the Key Enzyme for Metabolizing T-2 Toxin to 3'OH-T-2

Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou 510642, Guangdong, China
Author to whom correspondence should be addressed.
Received: 10 April 2013 / Revised: 12 May 2013 / Accepted: 17 May 2013 / Published: 23 May 2013
(This article belongs to the Special Issue Xenobiotic Metabolism)
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The transmission of T-2 toxin and its metabolites into the edible tissues of poultry has potential effects on human health. We report that T-2 toxin significantly induces CYP1A4 and CYP1A5 expression in chicken embryonic hepatocyte cells. The enzyme activity assays of CYP1A4 and CYP1A5 heterologously expressed in HeLa cells indicate that only CYP1A5 metabolizes T-2 to 3'OH-T-2 by the 3'-hydroxylation of isovaleryl groups. In vitro enzyme assays of recombinant CYP1A5 expressed in DH5α further confirm that CYP1A5 can convert T-2 into TC-1 (3'OH-T-2). Therefore, CYP1A5 is critical for the metabolism of trichothecene mycotoxin in chickens. View Full-Text
Keywords: T-2 toxin; chicken CYP1A5; metabolism T-2 toxin; chicken CYP1A5; metabolism
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Shang, S.; Jiang, J.; Deng, Y. Chicken Cytochrome P450 1A5 Is the Key Enzyme for Metabolizing T-2 Toxin to 3'OH-T-2. Int. J. Mol. Sci. 2013, 14, 10809-10818.

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