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 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.
D000626:Aminopeptidases / Q000378:metabolism*; D006358:Hot Temperature; D007425:Intracellular Membranes / Q000201:enzymology; D007700:Kinetics; D009940:Organoids / Q000201:enzymology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000648:ultrastructure; D014617:Vacuoles / Q000201:enzymology*
D000626:Aminopeptidases; C022750:X-Pro aminopeptidase