BMB Reports
- Volume 29 Issue 1
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- Pages.32-37
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- 1996
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- 1976-670X(eISSN)
Spectral Studies of Conformational Change at the Active Site of Mutant O-acetylserine Sulfhydrylase-A (C43S)
- Park, Joon-Bum (Department of Chemistry, Hanyang University) ;
- Kim, Sung-Kun (Department of Chemistry, Hanyang University) ;
- Yoon, Moon-Young (Department of Chemistry, Hanyang University)
- Published : 1996.01.31
Abstract
The cysteine 43, potentially important in the activity of O-acetylserine sulfhydrylase (OASS) from Salmonella typhimurium, has been changed to serine. This mutant enzyme (C43S) has been studied in order to gain insight into the structural basis for the binding of inhibitor, substrate and product. UV-visible spectra of C43S exhibit the same spectral change in the presence of OAS as that observed with wild type enzyme, indicating C43S will form an