Substrate specificity of the isoprenylated protein endoprotease

Ma, Yu Ting ; Chaudhuri, Arabinda ; Rando, Robert R. (1992) Substrate specificity of the isoprenylated protein endoprotease Biochemistry, 31 (47). pp. 11772-11777. ISSN 0006-2960

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Official URL: http://pubs.acs.org/doi/abs/10.1021/bi00162a014

Related URL: http://dx.doi.org/10.1021/bi00162a014

Abstract

Proteins containing a CAAX motif at their carboxyl termini are subject to isoprenylation at the cysteine residue, Proteolytic trimming of isoprenylated proteins is essential in the activation of these proteins, A microsomal endopeptidase activity bas been identified which cleaves all-trans farnesylated cysteine containing tetrapeptides between the modified residue and the adjacent amino acid to liberate the modified cysteine residue and an intact tripeptide. Structure/activity studies are reported here on this endopeptidase activity which are consistent with the premise that this protease is identical to the one normally involved in the cellular isoprenylation pathway. The protease only processes peptides which possess an isoprenyl moiety. Within the isoprenyl series, the enzyme hydrolyzes all-trans-farnesyl-, all-trans--geranylgeranyl-, and geranyl-containing peptides, The protease also recognizes the AAX sequence, because the protease behaves either stereospecifically or stereoselectively with respect to the individual amino acids of the tripeptide. The enzyme only measurably hydrolyzes isoprenylated peptides possessing L-amino acids at C and A. On the other hand, there is a small but measurable hydrolysis of isoprenylated peptides containing a D-amino acid at X.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:82527
Deposited On:11 Feb 2012 12:21
Last Modified:11 Feb 2012 12:21

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