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PMID: 6378661 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Localization of the thermosensitive X-prolyl dipeptidyl aminopeptidase in the vacuolar membrane of Saccharomyces cerevisiae.

FEBS letters ·Vol. 173 ·No. 1 ·1984-07-23 ·Pages 199-203

Bordallo C, Schwencke J, Suarez Rendueles M

Abstract

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 Km of 0.06 mM against L-alanyl-L-prolyl-p-nitroanilide while the heat-resistant enzyme shows an apparent Km of 0.4 mM against the same substrate.

MeSH Terms
Aminopeptidases/metabolism Hot Temperature Intracellular Membranes/enzymology Kinetics Organoids/enzymology Saccharomyces cerevisiae/enzymology,ultrastructure Vacuoles/enzymology
Chemicals
Aminopeptidases X-Pro aminopeptidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bordallo C
Schwencke J
Suarez Rendueles M
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1984-07-23
Pages
199-203
Language
English
Region
England
NLM ID
0155157
Subset
IM
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