PMID: 2116982Jul 30, 1990Paper

Processing of yeast exoglucanase (beta-glucosidase) in a KEX2-dependent manner

FEBS Letters
R D BascoG Larriba

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.

References

Feb 24, 1989·Biochimica Et Biophysica Acta·M RamírezG Larriba
Jan 1, 1989·Archives of Microbiology·M RamírezG Larriba
Mar 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·R S FullerJ Thorner
Jul 1, 1989·Trends in Biochemical Sciences·H Neurath
Jul 1, 1989·Trends in Biochemical Sciences·J C Paulson
Sep 12, 1988·FEBS Letters·G LarribaR D Basco
Jan 1, 1984·Annual Review of Biochemistry·J DouglassE Herbert

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Citations

Jan 15, 1995·FEMS Microbiology Letters·G LarribaR D Basco
Sep 2, 1998·Proceedings of the National Academy of Sciences of the United States of America·A BevanR S Fuller
Jul 29, 2004·The Journal of Biological Chemistry·Raúl CondeGermán Larriba
Sep 1, 1995·Microbiological Reviews·V J CidM Sánchez

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