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Information on EC 3.4.23.25 - saccharopepsin and Organism(s) Saccharomyces cerevisiae and UniProt Accession P07267
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3.4.23.25 saccharopepsinSpecify your search results
Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
proteinase ysca, pep4p, propra, saccharopepsin, yeast proteinase a, vacuolar aspartic proteinase, yeast proteinase, yeast aspartic proteinase a, proteinase a precursor, proteinase-a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
proteinase A precursor
inactive, maturation into active enzyme required proteinase B activity, 405 residues long precursor and 329 residues for the mature protein (77-405)
pseudo-proteinase A
active form of the enzyme resulting from autoactivation
Aspartate protease
-
-
-
-
Aspartic proteinase yscA
-
-
-
-
PEP4 gene product
PRA
Proteinase A
Proteinase yscA
-
-
-
-
Proteinase, yeast A
-
-
-
-
Saccharomyces aspartic proteinase
-
-
-
-
Saccharomyces cerevisiae aspartic proteinase A
-
-
-
-
Yeast endopeptidase A
-
-
-
-
Yeast proteinase A
PRA
-
-
-
-
Proteinase A
-
-
-
-
Proteinase A
-
-
Yeast proteinase A
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
-
CAS REGISTRY NUMBER
COMMENTARY
37228-80-1
-
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
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
-
?
(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
-
-
-
-
?
MOCAc-Ala-Pro-Ala-Lys-Phe-Phe-Arg-Leu-Lys(Dnp)-NH2 + H2O
?
-
-
-
-
?
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
-
-
?
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
-
-
?
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 B + H2O
propeptide of proteinase B + proteinase B
-
maturation and activation of proproteinase B
-
-
?
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
-
-
-
?
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
?
-
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
-
-
?
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
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
-
?
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 B + H2O
propeptide of proteinase B + proteinase B
-
maturation and activation of proproteinase B
-
-
?
Spt7p + H2O
?
-
the enzyme is required for cleavage of Spt7p subunit within SAGA in vitro into SLIK-related Spt7p
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IA3
peptide inhibitor synthesized by Saccharomyces cerevisae, a synthetic peptide containing residues 2-34 of IA3 exhibits comparable potency to natural IA3
-
IA3
-
endogenous 68-amino acid inhibitor. In absence of enzyme, IA3 is unstructured, addition of enzyme leads to large spectral transition of IA3
-
IA3
-
highly specific polypeptide inhibitor synthesized by Saccharomyces cerevisiae, a hydrogen bond network also residues K18 and D22 of the inhibitor directly to the catalytic Asp-32 and Tyr-75 residues of the enzyme, thus deadlocking the inhibitor in position, numerous mutants of IA3 created and tested for inhibition, all mutants are found to be inhibitory although to different extent, variations within residues 2-32 at positions other than 18 and 22 appears to have relatively minor effects
-
Specific proteinase inhibitor from yeast
-
completely selective for proteinase A from yeast
-
Specific proteinase inhibitor from yeast
-
Saccharomyces cerevisiae
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is activated by itself under acidic conditions
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00618
(7-methoxycoumarin-4-yl)acetyl-APAKFFRLK-(2,4-dinitrophenyl)-NH2
-
pH 4.5, 30°C
0.1
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
-
T222A mutant, pH 4.7
0.12
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
-
T287A/P288G mutant, pH 4.7
0.14
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
-
wild type enzyme, pH 4.7
0.25
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
-
A213I mutant, pH 4.7
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18.1
(7-methoxycoumarin-4-yl)acetyl-APAKFFRLK(2,4-dinitrophenyl)-NH2
-
pH 4.5, 30°C
21
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
-
T222A mutant, pH 4.7
21
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
-
T287A/P288G mutant, pH 4.7
44
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
-
wild type enzyme, pH 4.7
66
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
-
A213I mutant, pH 4.7
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000006
IA3 inhibitor
-
pH 4.7, 37°C, D22L inhibitor and synthetic peptide form 24 inhibitor
-
0.0000008
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 4 inhibitor and synthetic peptide form 9-NH2 inhibitor
-
0.000001
IA3 inhibitor
-
pH 4.7, 37°C, (Gly)9 inhibitor and synthetic peptide form 24 inhibitor
-
0.000002
IA3 inhibitor
-
pH 3.1, 37°C, K7mutant inhibitor and synthetic peptide form 2 inhibitor, pH 4.7, synthetic peptide form 9 inhibitor and synthetic peptide 10-NH2 inhibitor
-
0.000003
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 1 inhibitor and synthetic peptide form 3 inhibitor
-
0.0000035
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 21 inhibitor
-
0.000004
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 4 inhibitor
-
0.000005
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 9-NH2 inhibitor, pH 4.7, 37°C, synthetic peptide form 10 inhibitor
-
0.000006
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 5 inhibitor
-
0.000007
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 16 inhibitor
-
0.0000075
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 22 inhibitor
-
0.0000076
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 23 inhibitor
-
0.000008
IA3 inhibitor
-
pH 3.1, 37°C, chimera inhibitor, D22L inhibitor, synthetic peptide form 5 inhibitor, and synthetic peptide 10-NH2 inhibitor, pH 4.7, 37°C, synthetic peptide form 15 inhibitor
-
0.000015
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 6 inhibitor and synthetic peptide form 25 inhibitor
-
0.0000175
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 21 inhibitor
-
0.00002
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 22 inhibitor and synthetic peptide form 23 inhibitor
-
0.000025
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 10 inhibitor
-
0.000029
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 9 inhibitor
-
0.00004
IA3 inhibitor
-
pH 3.1, 37°C, (Gly)9 inhibitor, pH 4.7, 37°C, synthetic peptide form 25 inhibitor
-
0.000055
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 17 inhibitor
-
0.00006
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 16 inhibitor, pH 4.7, 37°C, synthetic peptide form 11-NH2 inhibitor
-
0.00007
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 15 inhibitor, pH 4.7, 37°C, synthetic peptide form 27 inhibitor
-
0.000085
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 6 inhibitor
-
0.00024
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 11-NH2 inhibitor
-
0.00033
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 18 inhibitor
-
0.0004
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 11 inhibitor, pH 3.1, synthetic peptide form 17 inhibitor
-
0.0005
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 7 inhibitor
-
0.0007
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 11 inhibitor
-
0.0008
IA3 inhibitor
-
pH 3.1, 37°C, MIX inhibitor, pH 4.7, 37°C, synthetic peptide form 19 inhibitor
-
0.001
IA3 inhibitor
-
pH 4.7, 37°C, synthetic peptide form 12 inhibitor
-
0.0021
IA3 inhibitor
-
pH 3.1, 37°C, synthetic peptide form 18 inhibitor
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
IA3
Saccharomyces cerevisiae
-
below 0.1 nM, exact detection impossible
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 5.5
-
succinyl-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
additional information
-
the pH-optimum for hydrolysis of protein substrates can be shifted to about 5 with 4-6 M urea
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6.5
-
4: about 50% of activity maximum, 6.5: about 30% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild type and proteinase B deficiency strain, in wild-type strains, proPrA is activated to mature PrA with a molecular weight of 42000 Da, whereas in PrB-deficient strains PrA maturation is delayed and a mature pseudo-form of PrA with a molecular weight of 43000 Da is detected
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
Pep4p is released from the vacuole into the cytosol in response to acetic acid treatment
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
-
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
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme is responsible for formation of the Spt-Ada-Gcn5 acetyltransferase (SAGA)-related SALSA/SAGA-like (SLIK) protein complex
physiological function
-
Pep4p has a role in mitochondrial degradation. Depletion and overexpression of Pep4p delays and enhances mitochondrial degradation, respectively
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
42000
45000
additional information
additional information
-
homology to: mammalian aspartyl proteases such as pepsin, renin and cathepsin
additional information
-
a precursor of MW 52000 is processed to the mature form of 42000 MW
additional information
-
proteinase A is synthesized as a 405-amino-acid precursor which is proteolytically converted to the 329-amino-acid mature enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
synthesized as inactive precursor of 405 residues with an apparent molecular weight of 52000 Da, mature nonglycosylated form of PrA has a molecular weight of 35800 Da, mature glycosylated form of PrA has a molecular weight of 41500 Da
monomer
additional information
monomer
-
1 * 54000, Saccharomyces cerevisiae, enzyme form A, SDS-PAGE
monomer
-
1 * 45000, Saccharomyces cerevisiae, enzyme form A', SDS-PAGE
additional information
in PrB-deficient strains PrA maturation is delayed and a mature pseudo-form of PrA with a molecular weight of 43000 Da is detected
additional information
-
in PrB-deficient strains PrA maturation is delayed and a mature pseudo-form of PrA with a molecular weight of 43000 Da is detected
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
contains 7.5% w/w mannose and 1% of glucosamine and galactosamine
glycoprotein
-
contains 8.5% neutral sugar and 1% glucosamine attached to asparagines in positions 67 and 267
glycoprotein
-
contains N-linked carbohydrate which is apparently not required for processing
glycoprotein
-
contains asparagine-linked carbohydrate at position 67
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of the native enzyme solved by molecular replacement in monoclinic and trygonal crystal forms, trigonal space group P3(2)21, cell dimensions a = b = 84.6 A, c = 108.7 A, monoclinic space group P2(1), cell dimensions a = 82.97 A, b = 49.08 A, c = 94.69 A
bound to inhibitor protein IA3, vapor diffusion, space group P6(2)22, unit cell dimensions a = b = 192.66 A, c = 52.09 A
-
crystallized with and without non-hydrolyzable transition-state analogue inhibitors
-
in complex with natural aspartic proteinase in hibitor IA3, space group P6(2)22, with unit-cell parameters a : b : 192.1 A, c : 59.80 A, native saccharopepsin crystals belongs to the orthorhombic space group I2(1)2(1)2(1) with unit-cell parameters a : 101.4 A, b 0 128.7 A, c : 155.4 A, in complex with CP81,282 and PD130,327 trigonal space group P3(2)21, with unit-cell parameters a 0 b : 87.4 A, c : 110.2 A
-
vapour diffusion, space group P3(2)21, in complex with inhibitor CP-81,198 unit cell dimensions a : b : 86.8 A, c : 110.2 A, in complex with inhibitor CP-108,420 unit cell dimensions a : b : 86.9 A, c : 110.2 A, in complex with inhibitor CP-72,647 unit cell dimensions a : b : 86.4 A, c : 109.9 A, in complex with inhibitor PD-129,541 unit cell dimensions a : b : 87.3 A, c : 110.7 A, in complex with inhibitor PD-133,450 unit cell dimensions a : b : 86.9 A, c : 110.2 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
the enzyme is stable at temperatures lower than 45°C and pH 5.5 and at 25°C and pH of 5.0-6.0
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Quite stable in concentrated solutions of urea, retains full activity after 1 h at 4°C in 6 M urea at pH 6.0, significant loss of activity at pH 5.0 and 7.0
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 0°C, 0.05 M potassium phosphate buffer, pH 6.7, stable for many months
-
-20°C, 50 mM imidazole buffer, pH 7.0, after 3 years, 40% of the original activity is retained
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overproduction-induced mislocation of the enzyme protein allows isolation of its structural gene
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
overexpression of the actin-severing protein cofilin reduces enzyme expression and excretion. Overexpression of Golgi apparatus-localized Ca2+ ATPase Pmr1 reduces enzyme excretion
-
the enzyme activity increases with increasing concentrations of 8-20% (w/v) D-glucose
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
important in a number of pathological processes, including gastric ulcers, Alzheimer's disease, hypertension, malaria, and AIDS
food industry
medicine
-
participates in a variety of physiological processes, and the onset of pathological conditions such as hypertension, gastric ulcers, and neoplastic diseases may be related to changes in the level of activity
food industry
-
important for the nitrogen release during alcoholic fermentation in wine production which is required for subsequent malolactic fermentation by Oenococcus oeni
food industry
-
the enzyme significantly affects the safety and quality of alcoholic drinks, especially the foam stability of beer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ammerer, G.; Hunter, C.P.; Rothman, J.H.; Saari, G.C.; Valls, L.A.; Stevens, T.H.
PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors
Mol. Cell. Biol.
6
2490-2499
1986
Saccharomyces cerevisiae
Meussendoerffer, F.; Tortora, P.; Holzer, H.
Purification and properties of proteinase A from yeast
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255
12087-12093
1980
Saccharomyces cerevisiae
Mechler, B.; Muller, M.; Muller, H.; Meussendoerffer, F.; Wolf, D.H.
In vivo biosynthesis of the vacuolar proteinases A and B in the yeast Saccharomyces cerevisiae
J. Biol. Chem.
257
11203-11206
1982
Saccharomyces cerevisiae
Rothman, J.H.; Hunter, C.P.; Valls, L.A.; Stevens, T.H.
Overproduction-induced mislocalization of a yeast vacuolar protein allows isolation of its structural gene
Proc. Natl. Acad. Sci. USA
83
3248-3252
1986
Saccharomyces cerevisiae
Mechler, B.; Wolf, D.H.
Analysis of proteinase A function in yeast
Eur. J. Biochem.
121
47-52
1981
Saccharomyces cerevisiae
Dreyer, T.; Valler, M.J.; Kay, J.; Charlton, P.; Dunn, B.M.
The selectivity of action of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae)
Biochem. J.
231
777-779
1985
Saccharomyces cerevisiae
Dreyer, T.; Svendsen, I.; Ottesen, M.
Partial primary structure and substance specificity of proteinase A from Saccharomyces cerevisiae
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13
1142-1143
1985
Saccharomyces cerevisiae
-
Jusic, M.; Hinze, H.; Holzer, H.
Inactivation of yeast enzymes by proteinase A and B and carboxypeptidase Y from yeast
Hoppe-Seyler's Z. Physiol. Chem.
357
735-740
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Saccharomyces cerevisiae
Huse, K.; Kopperschlger, G.; Hofmann, E.
Differences in the degradation of yeast phosphofructokinase by proteinases A and B from yeast
Biochem. J.
155
721-723
1976
Saccharomyces cerevisiae
Pedersen, J.; Biedermann, K.
Characterization of proteinase A glycoforms from recombinant Saccharomyces cerevisiae
Biotechnol. Appl. Biochem.
18
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Saccharomyces cerevisiae
Yokosawa, H.; Ito, H.; Murata, S.; Ishii, S.I.
Purification and fluorometric assay of proteinase A from yeast
Anal. Biochem.
134
210-215
1983
Saccharomyces cerevisiae
Badasso, M.; Wood, S.P.; Aguilar, C.; Cooper, J.B.; Blundell, T.L.
Crystallization and preliminary crystallographic characterization of aspartic proteinase-A from bakers yeast and its complexes with inhibitors
J. Mol. Biol.
232
701-703
1993
Saccharomyces cerevisiae
Faust, P.L.; Kornfeld, S.
Expression of the yeast aspartyl protease, proteinase A. Phosphorylation and binding to the mannose 6-phosphate receptor are altered by addition of cathepsin D sequences
J. Biol. Chem.
264
479-488
1989
Saccharomyces cerevisiae
Magni, G.; Natalini, P.; Santarelli, I.; Vita, A.
Bakers yeast protease A purification and enzymatic and molecular properties
Arch. Biochem. Biophys.
213
426-433
1982
Saccharomyces cerevisiae
Nowak, J.; Tsai, H.
Purification and properties of three endopeptidases from baker's yeast
Can. J. Microbiol.
35
295-303
1989
Saccharomyces cerevisiae
Dreyer, T.
Substrate specificity of proteinase yscA from saccharomyces cerevisiae
Carlsberg Res. Commun.
54
85-97
1989
Saccharomyces cerevisiae
Dreyer, T.; Halkier, B.; Svendsen, I.; Ottesen, M.
Primary structure of the aspartic proteinase A from Saccharomyces cerevisiae
Carlsberg Res. Commun.
51
27-41
1986
Saccharomyces cerevisiae
-
Badasso, M.O.; Read, J.A.; Dhanaraj, V.; Cooper, J.B.; Wood, S.P.; Blundell, T.L.; Dreyer, T.; Winther, J.
Purification, co-crystallization and preliminary X--ray analysis of the natural aspartic proteinase inhibitor IA3 complexed with saccharopepsin from Saccharomyces cerevisiae
Acta Crystallogr. Sect. D
56
915-917
2000
Saccharomyces cerevisiae
Gustchina, A.; Li, M.; Phylip, L.H.; Lees, W.E.; Kay, J.; Wlodawer, A.
An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
295
1020-1026
2002
Saccharomyces cerevisiae (P07267)
Cater, S.A.; Lees, W.E.; Hill, J.; Brzin, J.; Kay, J.; Phylip, L.H.
Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D
Biochim. Biophys. Acta
1596
76-82
2002
Saccharomyces cerevisiae
Kondo, H.; Shibano, Y.; Amachi, T.; Cronin, N.; Oda, K.; Dunn, B.M.
Substrate specificities and kinetic properties of proteinase A from the yeast Saccharomyces cerevisiae and the development of a novel substrate
J. Biochem.
124
141-147
1998
Saccharomyces cerevisiae
Phylip, L.H.; Lees, W.E.; Brownsey, B.G.; Bur, D.; Dunn, B.M.; Winther, J.R.; Gustchina, A.; Li, M.; Copeland, T.; Wlodawer, A.; Kay, J.
The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae
J. Biol. Chem.
276
2023-2030
2001
Saccharomyces cerevisiae
Cronin, N.B.; Badasso, M.O.; Tickle, J.; Dreyer, T.; Hoover, D.J.; Rosati, R.L.; Humblet, C.C.; Lunney, E.A.; Cooper, J.B.
X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity
J. Mol. Biol.
303
745-760
2000
Saccharomyces cerevisiae
Li, M.; Phylip, L.H.; Lees, W.E.; Winther, J.R.; Dunn, B.M.; Wlodawer, A.; Kay, J.; Gustchina, A.
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix
Nat. Struct. Biol.
7
113-117
2000
Saccharomyces cerevisiae
Green, T.B.; Ganesh, O.; Perry, K.; Smith, L.; Phylip, L.H.; Logan, T.M.; Hagen, S.J.; Dunn, B.M.; Edison, A.S.
IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution
Biochemistry
43
4071-4081
2004
Saccharomyces cerevisiae
Parr, C.L.; Keates, R.A.; Bryksa, B.C.; Ogawa, M.; Yada, R.Y.
The structure and function of Saccharomyces cerevisiae proteinase A
Yeast
24
467-480
2007
Saccharomyces cerevisiae (P07267), Saccharomyces cerevisiae
Kato, M.; Kuzuhara, Y.; Maeda, H.; Shiraga, S.; Ueda, M.
Analysis of a processing system for proteases using yeast cell surface engineering: conversion of precursor of proteinase A to active proteinase A
Appl. Microbiol. Biotechnol.
72
1229-1237
2006
Saccharomyces cerevisiae
Guilloux-Benatier, M.; Remize, F.; Gal, L.; Guzzo, J.; Alexandre, H.
Effects of yeast proteolytic activity on Oenococcus oeni and malolactic fermentation
FEMS Microbiol. Lett.
263
183-188
2006
Saccharomyces cerevisiae
Winterburn, T.J.; Wyatt, D.M.; Phylip, L.H.; Bur, D.; Harrison, R.J.; Berry, C.; Kay, J.
Key features determining the specificity of aspartic proteinase inhibition by the helix-forming IA3 polypeptide
J. Biol. Chem.
282
6508-6516
2007
Saccharomyces cerevisiae
Marques, M.; Mojzita, D.; Amorim, M.A.; Almeida, T.; Hohmann, S.; Moradas-Ferreira, P.; Costa, V.
The Pep4p vacuolar proteinase contributes to the turnover of oxidized proteins but PEP4 overexpression is not sufficient to increase chronological lifespan in Saccharomyces cerevisiae
Microbiology
152
3595-3605
2006
Saccharomyces cerevisiae
Narayanan, R.; Ganesh, O.K.; Edison, A.S.; Hagen, S.J.
Kinetics of folding and binding of an intrinsically disordered protein: the inhibitor of yeast aspartic proteinase YPrA
J. Am. Chem. Soc.
130
11477-11485
2008
Saccharomyces cerevisiae (P07267), Saccharomyces cerevisiae
Spedale, G.; Mischerikow, N.; Heck, A.; Marc Timmers, H.; Pim Pijnappel, W.
Identification of Pep4p as the protease responsible for formation of the SAGA-related SLIK protein complex
J. Biol. Chem.
285
22793-22799
2010
Saccharomyces cerevisiae
Pereira, C.; Chaves, S.; Alves, S.; Salin, B.; Camougrand, N.; Manon, S.; Sousa, M.; Corte-Real, M.
Mitochondrial degradation in acetic acid-induced yeast apoptosis: The role of Pep4 and the ADP/ATP carrier
Mol. Microbiol.
76
1398-1410
2010
Saccharomyces cerevisiae
Chen, Y.; Song, L.; Han, Y.; Liu, M.; Gong, R.; Luo, W.; Guo, X.; Xiao, D.
Decreased proteinase A excretion by strengthening its vacuolar sorting and weakening ist constitutive secretion in Saccharomyces cerevisiae
J. Ind. Microbiol. Biotechnol.
44
149-159
2017
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
Song, L.; Chen, Y.; Guo, Q.; Huang, S.; Guo, X.; Xiao, D.
Regulating the Golgi apparatus sorting of proteinase A to decrease its excretion in Saccharomyces cerevisiae
J. Ind. Microbiol. Biotechnol.
46
601-612
2019
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303-1A
Dong, L.; Li, F.; Piao, Y.; Sun, D.; Zhao, R.; Li, C.; Cong, L.; Zhao, C.
Characterization of proteinase A excretion from Saccharomyces cerevisiae in high sugar stress conditions
J. Korean Soc. Appl. Biol. Chem.
58
203-208
2015
Saccharomyces cerevisiae
-
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