The binding of the retro-analogue of glutathione disulfide to glutathione reductase.
The retro-analogue of glutathione disulfide was bound to the GSSG binding site of crystalline glutathione reductase. The binding mode revealed why the analogue is a very poor substrate in enzyme catalysis. The observed binding mode difference between natural substrate and retro-analogue is explained.
Janes
W
W
Institut für Organische Chemie und Biochemie, Universität Freiburg, Federal Republic of Germany.
Schulz
G E
GE
D001665:Binding Sites; D003460:Crystallization; D005978:Glutathione / Q000031:analogs & derivatives* / Q000378:metabolism; D019803:Glutathione Disulfide; D005980:Glutathione Reductase / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation
D005980:Glutathione Reductase; D005978:Glutathione; D019803:Glutathione Disulfide