BMB Reports
- Volume 30 Issue 4
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- Pages.280-284
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- 1997
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- 1976-670X(eISSN)
Chemical Modification Studies of Yeast Farnesyl Protein Transferase
- Sohn, Seung-Wan (Department of Chemistry, Seoul National University) ;
- Jun, Gyo (Division of Protein Engineering, Korea Research Institute of Bioscience and Biotechnology) ;
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Yang, Chul-Hak
(Department of Chemistry, Seoul National University)
- Received : 1997.05.20
- Published : 1997.07.31
Abstract
Phenylglyoxal diethyl pyrocarbonate (DEPC), and 1-cyclohexyl-3-[2-morpholinoethyl]-carbodiimide metho-p-toluenesulfonate (CMC) are modifying reagents specific for arginine, histidine, and aspartate or glutamate, respectively. They were found to inactivate S. cerevisiae farnesyl protein transferase (FPTase). The peptide substrate protected the enzyme against inactivation by CMC and the other substrate farnesyl pyrophosphate showed protection against inactivation by phenylglyoxal. while neither of the two substrates protected the enzyme against DEPC inactivation. These results suggest the presence of aspartate/glutamate, arginine and histidine residues at the active site of this enzyme.