Article
pH-dependent processing of yeast procarboxypeptidase Y by proteinase A in vivo and in vitro.
European journal of biochemistry - 15 Feb 1994
Sørensen S O, van den Hazel H B, Kielland-Brandt M C, Winther J R
Abstract excerpt
Carboxypeptidase Y is a vacuolar enzyme from Saccharomyces cerevisiae. It enters the vacuole as a zymogen, procarboxypeptidase Y, which is immediately processed in a reaction involving two endoproteases, proteinase A and proteinase B. We have investigated the in vitro activation of purified proca...
Topics
- Amino Acid Sequence
- Aspartic Acid Endopeptidases
- Binding Sites
- Carboxypeptidases
- Cathepsin A
- Enzyme Activation
- Enzyme Precursors
- Genes, Fungal
- Hydrogen-Ion Concentration
- Molecular Sequence Data
- Mutation
- Protein Processing, Post-Translational
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Serine Endopeptidases
- Vacuoles