Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 276, Issue 3, Pages 924-929Publisher
ACADEMIC PRESS INC
DOI: 10.1006/bbrc.2000.3553
Keywords
cathepsin B; propeptide; slow-binding inhibition
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A peptide corresponding to the full-length proregion (amino acids 16-114) of human cathepsin K was expressed and purified from Escherichia coli. This recombinant propeptide was investigated for its ability to inhibit the activity of three cysteine proteinases: cathepsins K, L, and B. Kinetic studies showed the propeptide to be a potent slow-binding inhibitor of its parent enzyme with a K-i = 2.61 nM at pH 6. This inhibition was pH-dependent, with a decrease in pH from 6 to 4 leading to a concomitant increase in K-i to 147 nM. The propeptide also inhibited cathepsin L with a K-i = 26.1 nM at pH 6, but showed little inhibition of cathepsin B at concentrations up to 400 nM. (C) 2000 Academic Press.
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