Article
Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme.
Biochemistry - 20 May 1997
Lo Bello M, Oakley A J, Battistoni A, Mazzetti A P, Nuccetelli M, Mazzarese G, Rossjohn J, Parker M W, Ricci G
Abstract excerpt
The possible role of the hydroxyl group of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1 has been investigated by means of site-directed mutagenesis, steady-state kinetic analysis, and crystallographic studies. Three representative cosubstrates have been used, i.e. etha...
Topics
- 4-Chloro-7-nitrobenzofurazan
- Crystallography, X-Ray
- Dinitrochlorobenzene
- Ethacrynic Acid
- Glutathione S-Transferase pi
- Glutathione Transferase
- Humans
- Inactivation, Metabolic
- Isoenzymes
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed