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 acids involved in this metabolic process, T-2...

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Veröffentlicht in:	PloS one 2014-09, Vol.9 (9), p.e106769
Hauptverfasser:	Cheng, Guyue, Liu, Changcun, Wang, Xu, Ma, Hongmin, Pan, Yuanhu, Huang, Lingli, Hao, Haihong, Dai, Menghong, Yuan, Zonghui
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Analysis Animal health Animals Biochemistry Biology and Life Sciences Biotransformation Calorimetry Crystal structure Cytochrome Cytochrome P-450 Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - genetics Cytochrome P-450 Enzyme System - metabolism Cytochrome P450 Cytotoxicity Docking Enzymes Function analysis Homology Humans Hydroxylation Laboratories Ligands Livestock Metabolism Metabolites Molecular Docking Simulation Mutagenesis Nifedipine Oxidation Poultry Protein synthesis Quality Residues Risk assessment Site-directed mutagenesis Structure-Activity Relationship Structure-function relationships Studies Substrates Swine T-2 Toxin Titration Titration calorimetry Toxins Trichothecenes
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