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Localization of the thermosensitive X‐prolyl dipeptidyl aminopeptidase in the vacuolar membrane of Saccharomyces cerevisiae
Author(s) -
Bordallo Carmen,
Schwencke Jaime,
Rendueles Maripaz Suarez
Publication year - 1984
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(84)81046-7
Subject(s) - protoplast , lysis , saccharomyces cerevisiae , enzyme , aminopeptidase , vacuole , membrane , biochemistry , chemistry , dipeptidyl peptidase , yeast , amino acid , leucine , cytoplasm
Most of the X‐prolyl dipeptidyl aminopeptidase activity of Saccharomyces cerevisiae was found to be associated with purified vacuolar membranes (specific activity approx. 75‐times higher than in the protoplast lysate). The tonoplast‐bound enzyme is thermosensitive. Another heat‐resistant enzyme was found in the protoplast lysate. The tonoplast‐bound thermosensitive enzyme shows an apparent K m of 0.06 mM against L‐alanyl‐L‐prolyl‐ p ‐nitroanilide while the heat‐resistant enzyme shows an apparent K m of 0.4 mM against the same substrate.