Structure-function analysis of porcine cytochrome P450 3A29 in the hydroxylation of T-2 toxin as revealed by docking and mutagenesis studies
T-2 toxin, one of the type A trichothecenes, presents a potential hazard to human and animal health. Our previous work demonstrated that porcine cytochrome P450 3A29 (CYP3A29) played an important role in the hydroxylation of T-2 toxin. To identify amino a
The catalytic activity of cytochrome P450 3A22 is critical for the metabolism of T-2 toxin in porcine reservoirs
Contamination of food by T-2 toxin, a trichothecene mycotoxin, poses a serious threat to human health. We report the identification of cytochrome P450 3A22 (CYP3A22) responsible for 3′-hydroxylation of T-2 and HT-2 in pigs. The present study shows that T-2 toxin significantly induces CYP3A22 expression in primary piglet hepatocytes. Moreover, recombinant pig CYP3A22 converted T-2 toxin into TC-1 (3′-OH-T-2 toxin) and HT-2 toxin into TC-3 (3′-OH-HT-2 toxin) in vitro. These results suggest that pig CYP3A22 primarily eliminates T-2 and HT-2 toxins by 3′-hydroxylation of isovaleryl groups. Therefore, CYP3A22 is critical for xenobiotic metabolism and endogenous biochemical biotransformation of trichothecene mycotoxin in porcine reservoirs.
Synthesis of HT-2 Toxin, Neosolaniol, T-2 Toxin, 3'-Hydroxy T-2 Toxin, and Sporotrichiol from Anguidine by Routes Involving Hydroxyl Inversion/Esterification
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Wani, Mansukh C.,Rector, Douglas H.,Cook, C. Edgar
p. 3468 - 3470
(2007/10/02)
3'-Hydroxy T-2 and 3'-hydroxy HT-2 toxins: New metabolites of T-2 toxin, a trichothecene mycotoxin, in animals
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Yoshizawa,Sakamoto,Ayano,Mirocha
p. 2613 - 2615
(2007/10/02)
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