Chemical modification studies of yeast farnesyl protein transferase

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Title
Chemical modification studies of yeast farnesyl protein transferase
Author(s)
Seung Wan Sohn; Gyo Jun; Chul Hak Yang
Bibliographic Citation
BMB Reports, vol. 30, no. 4, pp. 280-284
Publication Year
1997
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.
Keyword
active sitechemical modificationfarnesyl protein transferase
ISSN
1225-8687
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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