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The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution

Amino acids V12 (putative oxyanion hole), F112 (active site architecture), N108 (flavonoid binding) and C13 (GSH stabilization) were fully randomized by site saturation mutagenesis (NNK codons), and the created Pt GSTF8 variants were tested for conversion of flavan-3,3,4-triol ( 4 ) to cyanidin ( 8 ), and for their GSH-transferase activity towards CDNB ( 5 ) as a control of catalytic competence

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