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Enzyme


Title:Prohormone processing by yeast proteases
Author(s):Bourbonnais Y; Germain D; Latchinian-Sadek L; Boileau G; Thomas DY;
Address:"Eukaryotic Genetics Group, National Research Council of Canada, Montreal, Que"
Journal Title:Enzyme
Year:1991
Volume:45
Issue:5-Jun
Page Number:244 - 256
DOI: 10.1159/000468899
ISSN/ISBN:0013-9432 (Print) 0013-9432 (Linking)
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"
Keywords:"Amino Acid Sequence Carboxypeptidase B Carboxypeptidases/*genetics/metabolism Fungal Proteins/*metabolism Killer Factors, Yeast Mating Factor Molecular Sequence Data Mycotoxins/metabolism Peptides/metabolism *Proprotein Convertases Protein Precursors/*met;"
Notes:"MedlineBourbonnais, Y Germain, D Latchinian-Sadek, L Boileau, G Thomas, D Y eng Research Support, Non-U.S. Gov't Switzerland 1991/01/01 Enzyme. 1991; 45(5-6):244-56. doi: 10.1159/000468899"

 
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