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
Reaction
Reaction on EC 3.4.23.25 - saccharopepsin
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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
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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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
Asp-32 and Tyr-75 residues involved in catalysis
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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
description of mechanism, two catalytically active aspartic acid residues, Asp32 and Asp215