Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Intracellular targeting and structural conservation of a prohormone-processing endoprotease.

Intracellular targeting and structural conservation of a prohormone-processing endoprotease. 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Science (New York, N.Y.) Pubmed

Intracellular targeting and structural conservation of a prohormone-processing endoprotease.

Science (New York, N.Y.) , Volume 246 (4929): -475 – Dec 4, 1989

Intracellular targeting and structural conservation of a prohormone-processing endoprotease.


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.

Loading next page...
 
/lp/pubmed/intracellular-targeting-and-structural-conservation-of-a-prohormone-Fc027iEEzG

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

ISSN
0036-8075
DOI
10.1126/science.2683070
pmid
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.

Journal

Science (New York, N.Y.)Pubmed

Published: Dec 4, 1989

There are no references for this article.