Separation of peptide transport and hydrolysis in trimethionine uptake by Saccharomyces cerevisiae.
Intact cells of Saccharomyces cerevisiae 139 hydrolyzed amino acid-p-nitroanilide by an activity similar to that of aminopeptidase II, as well-characterized external peptidase in yeast. In contrast, trimethionine, a model peptide used in transport assays, was not hydrolyzed by this aminopeptidase II-like activity, and the peptidase activity toward this substrate was localized in the soluble fraction of the yeast. We conclude that this tripeptide is taken up by S. cerevisiae intact and rapidly hydrolyzed inside the cell.
D000596:Amino Acids / Q000378:metabolism; D000626:Aminopeptidases / Q000378:metabolism; D001692:Biological Transport; D005110:Extracellular Space / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007931:Leucyl Aminopeptidase / Q000378:metabolism; D009842:Oligopeptides / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins
D000596:Amino Acids; D009842:Oligopeptides; D029701:Saccharomyces cerevisiae Proteins; C022877:trimethionine; D000626:Aminopeptidases; C021108:yscII protein, S cerevisiae; D007931:Leucyl Aminopeptidase