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

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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: http://dx.doi.org/10.2174/0929866023408940

Publication date: 2002-02-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.