CLEAVAGE OF FARNESYLATED COOH-TERMINAL HEPTAPEPTIDE OF MOUSE N-RAS BY BRAIN MICROSOMAL-MEMBRANES - EVIDENCE FOR A CARBOXYPEPTIDASE, WHICH SPECIFICALLY REMOVES THE COOH-TERMINAL METHIONINE

被引：11

作者：

AKOPYAN, TN ^{[1
]}

COUEDEL, Y ^{[1
]}

BEAUMONT, A ^{[1
]}

FOURNIEZALUSKI, MC ^{[1
]}

ROQUES, BP ^{[1
]}

机构：

[1] UFR SCI PHARMACEUT & BIOL,DEPT CHIM ORGAN,CNRS,URA D1500,INSERM,UA498,U266,4 AVE OBSERV,F-75270 PARIS 06,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 187卷 / 03期

关键词：

D O I：

10.1016/0006-291X(92)90449-U

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Brain microsomal membranes are capable of sequentially removing Met, Leu and Val from a chemically synthesized COOH-terminal heptapeptide (propionyl-Gly-Ser-Pro-(farnesyl-Cys)-Val-Leu-Met) of mouse N-ras protein. The carboxypeptidase generating Met displays maximum activity at neutral pH and shows high affinity for the farnesylated substrate (Km=73 μM) as compared to its non farnesylated precursor (Km=600 μM). The results of inhibitor action suggest that the membrane carboxpeptidase is a novel, probably thiol-dependent, serine type peptidase. © 1992.

引用

页码：1336 / 1342

页数：7

共 23 条

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