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  • Title: Intracellular targeting and structural conservation of a prohormone-processing endoprotease.
    Author: Fuller RS, Brake AJ, Thorner J.
    Journal: Science; 1989 Oct 27; 246(4929):482-6. PubMed ID: 2683070.
    Abstract:
    The prohormone-processing endoprotease (KEX2 gene product) of the yeast Saccharomyces cerevisiae is a membrane-bound, 135,000-dalton glycoprotein, which contains both asparagine-linked and serine- and threonine-linked oligosaccharide and resides in a secretory compartment. Analysis of mutant kex2 genes truncated at their 3' end indicates that carboxyl terminal domains of the enzyme are required for its proper localization within the cell. A human gene product, "furin," shares 50% identity with the catalytic domain of Kex2 protease and is, therefore, a candidate for a human prohormone-processing enzyme.
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