Localization of the thermosensitive X‐prolyl dipeptidyl aminopeptidase in the vacuolar membrane of Saccharomyces cerevisiae
Copyright policy )Localization of the thermosensitive X‐prolyl dipeptidyl aminopeptidase in the vacuolar membrane of Saccharomyces cerevisiae
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.
Hot Temperature, Dipeptidyl aminopeptidase, Membrane-bound proteinase, Intracellular Membranes, Saccharomyces cerevisiae, Proteinase, Aminopeptidases, Yeast, Organoids, Kinetics, Vacuoles, Vacuole, Tonoplast
Hot Temperature, Dipeptidyl aminopeptidase, Membrane-bound proteinase, Intracellular Membranes, Saccharomyces cerevisiae, Proteinase, Aminopeptidases, Yeast, Organoids, Kinetics, Vacuoles, Vacuole, Tonoplast
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