3.4.23.25: saccharopepsin
This is an abbreviated version!
For detailed information about saccharopepsin, go to the full flat file.
Word Map on EC 3.4.23.25
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 =
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
3.4.23.25 saccharopepsinAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.23.25 - saccharopepsin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)acetyl-Ala-Pro-Ala-Ala-Lys-Phe-Phe-Arg-Leu-Lys(2,4-dinitrophenyl)-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-APAKFFRLK(2,4-dinitrophenyl)-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-APAKFFRLK-(2,4-dinitrophenyl)-NH2 + H2O
?
-
-
-
-
?
Acid-denatured hemoglobin + H2O
?
-
-
tyrosine-containing acid soluble peptides detected to measure enzyme activity
-
?
Ala-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Ala-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Arg-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Arg-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Asp-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Asp-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
hemoglobin + H2O
tyrosin-containing peptides + hemoglobin fragments
-
-
-
-
?
Leu-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Leu-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Ala-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Ala-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Arg-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Arg-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Asp-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Asp-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Leu-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Leu-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Pro-Arg-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Arg-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Pro-Asp-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Asp-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + L-nitrophenylalanine-Arg-Leu
-
-
-
-
?
Lys-Pro-Leu-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Leu-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Myoglobin + H2O
?
-
initially cleaved in 3 positions: Leu29-Ile30, Leu32-Phe33 and Leu137-Phe138 and subsequently also in positions Leu9-Val10, Leu11-His12, Leu69-Thr70, Leu89-Ala90, Phe106-Ile107 and Ile111-Ile112
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
Oxidized B-chain of insulin + H2O
?
-
at pH 3.0 or at pH 4.7 in the presence of 4 M urea, the enzyme preferentially cleaves peptide bonds of the X-Tyr and X-Phe types, the peptide bonds Leu15-Tyr16, Phe24-Phe25 and Phe25-Tyr26 are hydrolyzed simultaneously
-
-
?
proproteinase A + H2O
pseudo-proteinaseA + peptide
autoactivation of the enzyme yields a functional protein cleaved after Ser68, autoactivation can occur in rare situations when PrB is unable to activate PrA
Ser68 is the N-terminal amino acid
-
?
Ser-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Ser-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Spt7p + H2O
?
-
the enzyme is required for cleavage of Spt7p subunit within SAGA in vitro into SLIK-related Spt7p
-
-
?
Succinyl-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
Succinyl-Arg-Pro-Phe-His-Leu-Leu + Val-Tyr 4-methylcoumarin 7-amide
-
-
-
?
succinyl-LFAEVAYD-7-amido-4-methylcoumarin + H2O
succinyl-LFAEVAYD + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-RFFHLLVY-7-amido-4-methylcoumarin + H2O
succinyl-RFFHLL + Val-Tyr-7-amido-4-methylcoumarin
-
-
-
-
?
succinyl-RFFHLLVY-7-amido-4-methylcoumarin + H2O
succinyl-RFFHLLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (NO2)Phe-Arg-Leu
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (NO2)Phe-Arg-Leu
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (NO2)Phe-Arg-Leu
-
-
-
?
MOCAc-Ala-Pro-Ala-Lys-Phe-Phe-Arg-Leu-Lys(Dnp)-NH2 + H2O
?
-
-
-
-
?
MOCAc-Ala-Pro-Ala-Lys-Phe-Phe-Arg-Leu-Lys(Dnp)-NH2 + H2O
?
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
procarboxypeptidase Y + H2O
propeptide of carboxypeptidase Y + carboxypeptidase Y
-
maturation and activation of procarboxypeptidase Y
-
-
?
procarboxypeptidase Y + H2O
propeptide of carboxypeptidase Y + carboxypeptidase Y
-
maturation and activation of procarboxypeptidase Y
-
-
?
proproteinase A + H2O
propeptide of proteinase A + proteinase A
-
autocatalytic activation of proproteinase A
-
-
?
proproteinase A + H2O
propeptide of proteinase A + proteinase A
-
autocatalytic activation of proproteinase A
-
-
?
proproteinase B + H2O
propeptide of proteinase B + proteinase B
-
maturation and activation of proproteinase B
-
-
?
proproteinase B + H2O
propeptide of proteinase B + proteinase B
-
maturation and activation of proproteinase B
-
-
?
additional information
?
-
-
inactivates various yeast enzymes: cytoplasmic malate dehydrogenase
-
-
?
additional information
?
-
-
stepwise degradation of yeast phosphofructokinase with about 80% decrease of activity
-
-
?
additional information
?
-
-
glutamate dehydrogenase (NAD+-dependent)
-
-
?
additional information
?
-
-
more selective towards the peptide it cleaves than pepsin, shows the same preference for large hydrophobic residues on both sides of the cleaved bond as pepsin and lysosomal cathepsin D
-
-
?
additional information
?
-
-
catalyzes the cleavage of peptide bonds preferentially between two hydrophobic residues, but does not hydrolyze small pepsin substrates e.g. benzyloxycarbonyl-His-Phe-(4-nitro)Phe methyl ester
-
-
?
additional information
?
-
-
protein degradation under sporulation conditions is about 30% reduced in proteinase A mutant cells, the differentiation process of sporulation is also disturbed leading to a 40% reduced sporulation frequency in mutant cells
-
-
?
additional information
?
-
-
involved in intracellular proteolysis, especially under sporulation conditions
-
?
additional information
?
-
essential to the activities of other yeast vacuolar hydrolases, including proteinase B, aminopeptidase I, and carboxypeptidase Y
-
-
?
additional information
?
-
-
essential to the activities of other yeast vacuolar hydrolases, including proteinase B, aminopeptidase I, and carboxypeptidase Y
-
-
?
additional information
?
-
-
important for protein turnover after oxidative damage, supplies nitrogen under nutritional stress conditions
-
-
?
additional information
?
-
-
required for the activation of carboxypeptidase Y and proteinase B
-
-
?
additional information
?
-
preference for hydrophobic residues with Phe, Leu or Glu at the P1 position and Phe, Ile, Leu or Ala at P1
-
-
?
additional information
?
-
-
preference for hydrophobic residues with Phe, Leu or Glu at the P1 position and Phe, Ile, Leu or Ala at P1
-
-
?
