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Science 16 January 1987:
Vol. 235. no. 4786, pp. 348 - 350
DOI: 10.1126/science.3541206
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Articles

Science, Vol 235, Issue 4786, 348-350
Copyright © 1987 by American Association for the Advancement of Science

articles

Yeast KEX2 protease has the properties of a human proalbumin converting enzyme

IC Bathurst, SO Brennan, RW Carrell, LS Cousens, AJ Brake, and PJ Barr

Several classes of proteolytic enzymes have been proposed to have a role in the processing of precursor forms of proproteins at paired basic amino acid residues. In higher eukaryotes, a single endopeptidase has yet to fulfill the necessary criteria as the physiologically relevant convertase. The observation of proalbumin circulating in a child with a bleeding disorder caused by an unusual alpha 1-antitrypsin mutation led to speculation that the presence of this alpha 1-antitrypsin mutant was inhibitory to the convertase. This provided an additional means of characterizing the processing enzyme. In this study the yeast KEX2 enzyme, a calcium-dependent thiol protease, was found to have all the properties expected for this processing enzyme. KEX2 correctly recognized and cleaved the prosequence in proalbumin. In addition, KEX2 was specifically inhibited by the mutant alpha 1-antitrypsin but not by other serine protease inhibitors.


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