Evidence for an Induced-Fit Mechanism Operating in Pi Class Glutathione Transferases,
- 23 June 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 37 (28) , 9912-9917
- https://doi.org/10.1021/bi980323w
Abstract
Three-dimensional structures of the apo form of human pi class glutathione transferase have been determined by X-ray crystallography. The structures suggest the enzyme recognizes its substrate, glutathione, by an induced-fit mechanism. Compared to complexed forms of the enzyme, the environment around the catalytic residue, Tyr 7, remains unchanged in the apoenzyme. This observation supports the view that Tyr 7 does not act as a general base in the reaction mechanism. The observed cooperativity of the dimeric enzyme may be due to the movements of a helix that forms one wall of the active site and, in particular, to movements of a tyrosine residue that is located in the subunit interface.Keywords
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