Article
Rational reconstruction of the active site of a class mu glutathione S-transferase.
The Journal of biological chemistry - 23 Dec 1994
Shan S, Armstrong R N
Abstract excerpt
Isoenzymes 3-3 and 4-4 of the mu class glutathione S-transferases share 77% sequence identity but have distinctly different catalytic properties. Analysis of the crystal structure of isoenzyme 3-3 in complex with the diastereomeric products of the addition of GSH to phenanthrene 9,10-oxide (Ji, X., Johnson, W. W., Sesay, M. A., Dickert, L., Prasad, S. M., Ammon, H. L., Armstrong, R. N., and Gilliland, G. L....
Topics
- Animals
- Binding Sites
- Butanones
- Epoxy Compounds
- Glutathione Transferase
- Isoenzymes
- Kinetics
- Mutation
- Phenanthrenes
- Rats
- Substrate Specificity