Distinct Cleavage Specificity of Human Cathepsin E at Neutral pH with Special Preference for Arg-Arg Bonds

Authors: Athauda S.B.P.; Takahashi K.

Source: Protein and Peptide Letters, Volume 9, Number 1, February 2002 , pp. 15-22(8)

Publisher: Bentham Science Publishers

Key:

- Free Content

- New Content

- Subscribed Content

- Free Trial Content

Abstract:

In order to clarify the potential role of cathepsin E at neutral pH, the cleavage specificity of human cathepsin E was examined at pH 7.4 toward reduced-carboxymethylated(RCm-)ribonuclease A and various bioactive and related peptides. The specificity of the enzyme at pH 7.4 was found to be considerably different from that at acidic pH preferential cleavages were observed with Arg-X and Glu-X bonds, which are not the major cleavage sites at acidic pH. Moreover, the Arg-Arg bond was found to be the most preferential site of cleavage. This unique specificity observed at pH 7.4 suggests the possibility that cathepsin E might be involved in processing and/or degradation of certain proteins and / or peptides at or near neutral pH in vivo.

Keywords: Cathepsin E; RCm-ribonuclease; Tyr-X bonds; Lys-Lys bonds; Glu-X bonds

Language: English

Document Type: Review article

DOI: 10.2174/0929866023408940

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$55.10 plus tax Refund Policy