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Processing of yeast exoglucanase (beta-glucosidase) in a KEX2-dependent manner
R D Basco1, G Giménez-Gallego, G Larriba
1Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, Badajoz, Spain.
FEBS Letters
|July 30, 1990
Abstract:
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.