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Tocotrienols Inhibit Human Glutathione S‐Transferase P1‐1
Author(s) -
van Haaften Rachel I. M.,
Haenen Guido R. M. M.,
Evelo Chris T. A.,
Bast Aalt
Publication year - 2002
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540214315
Subject(s) - tocotrienol , chemistry , antioxidant , glutathione , enzyme , biochemistry , tocopherol , glutathione s transferase , stereochemistry , vitamin e
Tocopherols and tocotrienols are food ingredients that are believed to have a positive effect on health. The most studied property of both groups of compounds is their antioxidant action. Previously, we found that tocopherols and diverse tocopherol derivatives can inhibit the activity of human glutathione S‐transferase P1‐1 (GST P1‐1). In this study we found that GST P1‐1 is also inhibited, in a concentration‐dependent manner, by α‐ and γ‐tocotrienol. The concentration giving 50% inhibition of GST P1‐1 is 1.8 ±0.1 μM for α‐tocotrienol and 0.7 ±0.1 μM for γ‐tocotrienol. This inhibition of GST P1‐1 is noncompetitive with respect to both substrates CDNB and GSH. We also examined the 3D structure of GST P1‐1 for a possible tocopherol/tocotrienol binding site. The enzyme contains a very hydrophobic pit‐like structure where the phytyl tail of tocopherols and tocotrienols could fit in. Binding of tocopherol and tocotrienol to this hydrophobic region might lead to bending of the 3D structure. In this way tocopherols and tocotrienols can inhibit the activity of the enzyme; this inhibition can have far‐reaching implications for humans.