Parker D D, Naider F, Becker J M
J Bacteriol. 1980 Aug;143(2):1066-9. doi: 10.1128/jb.143.2.1066-1069.1980.
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.
酿酒酵母139的完整细胞通过一种与酵母中特征明确的外肽酶氨基肽酶II相似的活性来水解氨基酸对硝基苯胺。相比之下,用于转运测定的模型肽三蛋氨酸并未被这种类似氨基肽酶II的活性水解,且针对该底物的肽酶活性定位于酵母的可溶部分。我们得出结论,这种三肽被完整的酿酒酵母摄取并在细胞内迅速水解。