Inhibition of Human Napsin A

Title: Inhibition of Human Napsin A

Volume: 10 Issue: 1

Author(s): Rebecca F. Cronshaw, Vesna Schauer-Vukasinovic, David J. Powell, Thomas Giller, Daniel Bur and John Kay

Affiliation:

Keywords: human aspartic proteinase, selectivity of inhibition, active site mapping, importance of s1/s3, hapsin a, napsin a inhibitor

Abstract: The newly-discovered human aspartic proteinase, napsin A was not susceptible to protein inhibitors from potato, squash or yeast but was weakly inhibited by the 17 kDa polypeptide from Ascaris lumbricoides and potently by isovaleryl and lactoyl-pepstatins. A series of synthetic inhibitors was also investigated which contained in the P1-P1 positions the dipeptide analogue statine or its phenylalanine or cyclohexylalanine homologues and in which the residues occupying P4-P3 were varied systematically. On this basis, the active site of napsin A can be readily distinguished from other human aspartic proteinases.

Cite this article as:

Cronshaw F. Rebecca, Schauer-Vukasinovic Vesna, Powell J. David, Giller Thomas, Bur Daniel and Kay John, Inhibition of Human Napsin A, Protein & Peptide Letters 2003; 10 (1) . https://dx.doi.org/10.2174/0929866033408237