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
Molecular Weight
Molecular Weight on EC 3.4.23.25 - saccharopepsin
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40760
-
laser desorption mass spectroscopy, a second form with MW 38132 isolated from the culture medium is an underglycosylated form lacking the carbohydrate moiety at Asn269
41400
-
sedimentation-diffusion equilibrium ultracentrifugation
41700
-
1 * 41700, Saccharomyces cerevisiae, SDS-PAGE
49000
-
enzyme form A, gel filtration
54000
-
1 * 54000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE
42000
-
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42000
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enzyme form A', gel filtration
42000
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1 * 42000, Saccharomyces cerevisiae, SDS-PAGE
42000
-
1 * 42000, SDS-PAGE, native mass by gel filtration
45000
-
gel filtration
45000
-
1 * 45000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE
additional information
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primary structure
additional information
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homology to: mammalian aspartyl proteases such as pepsin, renin and cathepsin
additional information
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partial primary structure
additional information
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a precursor of MW 52000 is processed to the mature form of 42000 MW
additional information
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proteinase A is synthesized as a 405-amino-acid precursor which is proteolytically converted to the 329-amino-acid mature enzyme