Chemical Modification of Yeast Farnesyl Protein Transferase Expressed in E. coli

Bulletin of the Korean chemical society

Chul-Hak Yang¹  Hyun-Kyung Kim¹ 

关键词: Farnesyl protein transferase (FPT);    Chemical modification;    CMC;    Phenylglyoxal;    DEPC;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

Chemical modification of the S. cerevisiae farnesyl protein transferase (FPT) with CMC, phenylglyoxal and DEPC resulted in enzyme inactivation, depending upon the reagent concentration. The peptide substrate GSTPEP- I, a GST-fused undecapeptide mimicking the C-terminus of p21Ki-ras, protected the enzyme against inactivation by CMC which is specific to either aspartate or glutamate, while the other substrate farnesyl pyrophosphate (FPP) showed protection against phenylglyoxal which is the specific modifier of arginine residues, dependent on the substrate concentrations. Neither of the two substrates protected the enzyme against histidine inactivation by DEPC. It is suggested that there is at least one aspartate or glutamate residue at the peptide substrate binding site, and that at least one arginine residue is located at the binding site of FPP. There also seems to be at least one histidine residue which is critical for enzymic activity and is exposed toward the bulk solution, excluded from the substrate binding sites.

【 授权许可】

Unknown