3.4.23.25: saccharopepsin
This is an abbreviated version!
For detailed information about saccharopepsin, go to the full flat file.
Reaction
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-/-Val-Tyr bond in a synthetic substrate. Does not act on esters of Tyr or Arg
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Synonyms
Acid protease, Aspartate protease, Aspartic proteinase, Aspartic proteinase yscA, EC 3.4.23.6, EC 3.4.23.8, EC 3.4.4.17, Pep4, PEP4 gene product, Pep4p, Pep4p vacuolar proteinase, pepsin-like aspartic proteinase, PRA, preproPrA, proPrA, Protease A, Proteinase A, proteinase A precursor, Proteinase yscA, Proteinase, yeast A, proteinase-A, pseudo-proteinase A, Saccharomyces aspartic proteinase, Saccharomyces cerevisiae aspartic proteinase A, saccharopepsin, vacuolar aspartic proteinase, yeast aspartic proteinase A, Yeast endopeptidase A, yeast proteinase, Yeast proteinase A
ECTree
Localization
Localization on EC 3.4.23.25 - saccharopepsin
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overexpression results in secretion
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Pep4p is released from the vacuole into the cytosol in response to acetic acid treatment
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lysosome-like vacuole
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lysozyme-like vacuole
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mature protein
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mature protein
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additional information
synthesized as an inactive precursor (zymogen), termed preproPrA, which transits to the endoplasmic reticulum where the protein is glycosylated and a hydrophobic signal peptide of the 22 amino acid is removed, the protein is then transported to the Golgi complex, where the carbohydrate side chains are modified by mannosyltransferases, the resulting 52 kDa proPrA is transported through the endosome to the vacuole, where a 54-amino acid propeptide is removed, yielding the mature 42 kDa proteinase
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additional information
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synthesized as an inactive precursor (zymogen), termed preproPrA, which transits to the endoplasmic reticulum where the protein is glycosylated and a hydrophobic signal peptide of the 22 amino acid is removed, the protein is then transported to the Golgi complex, where the carbohydrate side chains are modified by mannosyltransferases, the resulting 52 kDa proPrA is transported through the endosome to the vacuole, where a 54-amino acid propeptide is removed, yielding the mature 42 kDa proteinase
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brenda