The binding of the retro-analogue of glutathione disulfide to glutathione reductase

W Janes; G E Schulz

doi:10.2210/pdb4gr1/pdb

The binding of the retro-analogue of glutathione disulfide to glutathione reductase

J Biol Chem. 1990 Jun 25;265(18):10443-5. doi: 10.2210/pdb4gr1/pdb.

Authors

W Janes¹, G E Schulz

Affiliation

¹ Institut für Organische Chemie und Biochemie, Universität Freiburg, Federal Republic of Germany.

PMID: 2355009
DOI: 10.2210/pdb4gr1/pdb

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Binding Sites
Crystallization
Glutathione / analogs & derivatives*
Glutathione / metabolism
Glutathione Disulfide
Glutathione Reductase / metabolism*
Humans
Models, Molecular
Protein Conformation

Substances

Glutathione Reductase
Glutathione
Glutathione Disulfide