Site-directed mutagenesis of tyrosine 108 residue in human glutathione S-transferase P1-1
- Authors
- Ahn, So-Yoon; Jeon, Sang-Hoon; Park, Hee-Joong; Kong, Kwang-Hoon
- Issue Date
- Aug-2003
- Publisher
- WILEY-V C H VERLAG GMBH
- Keywords
- tyrosinase 108 residue; enzymatic properties; glutathione S-transferase; inhibition characteristics; substrate specificity
- Citation
- BULLETIN OF THE KOREAN CHEMICAL SOCIETY, v.24, no.8, pp 1188 - 1192
- Pages
- 5
- Journal Title
- BULLETIN OF THE KOREAN CHEMICAL SOCIETY
- Volume
- 24
- Number
- 8
- Start Page
- 1188
- End Page
- 1192
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24947
- DOI
- 10.5012/bkcs.2003.24.8.1188
- ISSN
- 0253-2964
1229-5949
- Abstract
- In order to study the role of residue in the active site of glutathione S-transferase (GST), Tyr 108 residue in human GST P1-1 was replaced with alanine, phenylalanine and tryptophan by site-directed mutagenesis to obtain mutants Y108A, Y108F and Y108W. These three mutant enzymes were expressed in Escherichia coli and purified to electrophoretic homogeneity by affinity chromatography on immobilized GSH. The substitutions of Tyr108 significantly affected K-m(CDNB) and K-m(ETA), whereas scarcely affected K-m(GSH). The substitutions of Tyr108 also significantly affected I-50 of ETA, an electrophilic substrate-like compound. The effect of these substitutions on kinetic parameters and the response to inhibition suggests that tyrosine 108 in hGST PI-I contributes to the binding of the electrophilic substrate and a major determinant in the binding of CDNB is the aromatic ring of Tyr108, not its hydroxyl group.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - College of Natural Sciences > Department of Chemistry > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24947)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.