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Processing of yeast exoglucanase (β‐glucosidase) in a KEX2‐dependent manner
Author(s) -
Basco Ricardo D.,
Giménez-Gallego Guillermo,
Larriba Germán
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80982-o
Subject(s) - saccharomyces cerevisiae , biochemistry , yeast , chemistry , endoplasmic reticulum , leupeptin , amino acid , enzyme , protease
We have detected proteolytic processing of a form of exoglucanase representative of the endoplasmic reticulum (form A). This processing did not take place when form A was obtained from protoplasts lysed in the presence of either EDTA or leupeptin, two wel‐characterized inhibitors of KEX2 endoprotease from Saccharomyces cerevisiae . Sequencing of the amino terminus of an A‐like form of enzyme secreted by a kex2 mutant indicated the presence of 4 amino acids, with a pair of basic residues (Lys‐Arg) at their carboxyl side, preceding the amino terminus of the wild‐type external exoglucanase.