Saccharopepsin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.23 Aspartic endopeptidases > 3.4.23.25 saccharopepsin
Saccharopepsin is a vacuolar aspartic endopeptidase of baker's yeast Saccharomyces cerevisiae, belonging to peptidase family A1. It hydrolyzes proteins with broad specificity for peptide bonds, cleaves the -Leu-Leu-/-Val-Tyr bond in a synthetic substrate, and does not act on esters of Tyr or Arg. In the yeast vacuole it contributes to bulk protein turnover and zymogen activation. It features a pepsin-like aspartic-protease fold active in the acidic vacuole.
Saccharopepsin is a vacuolar aspartic endopeptidase of baker's yeast Saccharomyces cerevisiae, belonging to peptidase family A1. It hydrolyzes proteins with broad specificity for peptide bonds, cleaves the -Leu-Leu-/-Val-Tyr bond in a synthetic substrate, and does not act on esters of Tyr or Arg. In the yeast vacuole it contributes to bulk protein turnover and zymogen activation. It features a pepsin-like aspartic-protease fold active in the acidic vacuole.
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