Article
Aromatic residues in the C-terminal region of glutathione transferase A1-1 influence rate-determining steps in the catalytic mechanism.
Biochimica et biophysica acta - 20 May 2002
Nilsson Lisa O, Edalat Maryam, Pettersson Pär L, Mannervik Bengt
Abstract excerpt
Human glutathione transferase A1-1 (GST A1-1) has a flexible C-terminal segment that forms a helix (alpha 9) closing the active site upon binding of glutathione and a small electrophilic substrate such as 1-chloro-2,4-dinitrobenzene (CDNB). In the absence of active-site ligands, the C-terminal segment is not fixed in one position and is not detectable in the crystal structure. A key residue in the alpha 9-helix...
Topics
- Amino Acid Sequence
- Catalysis
- Dinitrochlorobenzene
- Glutathione
- Glutathione Transferase
- Humans
- Isoenzymes
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutation