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  • Title: Prohormone processing by yeast proteases.
    Author: Bourbonnais Y, Germain D, Latchinian-Sadek L, Boileau G, Thomas DY.
    Journal: Enzyme; 1991; 45(5-6):244-56. PubMed ID: 1843279.
    Abstract:
    Investigations of the precursors of alpha-pheromone and killer toxin in the yeast Saccharomyces cerevisiae have defined the genes coding (KEX1 and KEX2) for the proteases which are responsible for their processing. In addition to processing at pairs of basic residues it is evident that yeast can also process at monobasic sites. We present data on the Kex1p and Kex2p enzymes, their cellular localization, and their post-translational modification. In addition initial characterisation of the monobasic specific protease and the isolation of mutants defective in this activity are presented. The use of the yeast system as a model for the processing of mammalian prohormones is discussed.
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