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(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
?
-
-
-
-
?
A-L-S-A-F-(4NO2)F-R-L + H2O
?
very effective substrate
-
-
?
A-P-A-K-F-(4NO2)F-R-L + H2O
?
very effective substrate
-
-
?
Acid-denatured hemoglobin + H2O
?
-
-
tyrosine-containing acid soluble peptides detected to measure enzyme activity
-
?
Ala-Leu-Ser-Ala-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Ala-Pro-Ala-Lys-Phe-(NO2)-Phe-Arg-Leu + H2O
?
-
-
-
?
Ala-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Ala-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Ala-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Arg-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Arg-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Arg-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Asp-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Asp-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Asp-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
Cathepsin + H2O
?
-
-
-
-
?
Dimethylcasein + H2O
?
-
-
-
-
?
Gly-Ala-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
haemoglobin + H2O
?
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
hemoglobin + H2O
tyrosin-containing peptides + hemoglobin fragments
-
-
-
-
?
K-L-A-K-F-(4NO2)F-R-L + H2O
?
-
-
-
?
K-P-A-A-F-(4NO2)F-R-L + H2O
?
-
-
-
?
K-P-A-K-F-(4NO2)F-R-L + H2O
?
-
-
-
?
K-P-S-K-F-(4NO2)F-R-L + H2O
?
-
-
-
?
Leu-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Leu-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Leu-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
lipid transfer protein 1 + H2O
?
Lys-Ala-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Ala-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Ala-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Arg-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Arg-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Arg-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Asp-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Asp-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Asp-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Leu-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Leu-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Leu-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Ala -Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Arg-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Leu-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Ala-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Ala + H2O
?
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Arg + H2O
?
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Asp + H2O
?
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Ser + H2O
?
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Asp-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Leu-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Ser-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Ser-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Arg-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Arg-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Pro-Arg-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Asp-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Asp-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Pro-Asp-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (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-Pro-Leu-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Ser-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
Lys-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
Lys-Ser-Ala-Asp-Phe + 4-(NO2)Phe-Arg-Leu
-
-
-
-
?
Lys-Ser-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
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
-
-
?
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
-
-
?
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
?
-
-
-
-
?
procarboxypeptidase Y + H2O
propeptide of carboxypeptidase Y + carboxypeptidase Y
proproteinase A + H2O
propeptide of proteinase A + proteinase A
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
-
?
proproteinase B + H2O
propeptide of proteinase B + proteinase B
Ser-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
-
-
-
?
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
-
-
?
Suc-APAKFFRL-4-methylcoumarin 7-amide + H2O
?
-
-
-
?
Suc-RPFHLLVY-4-methylcoumarin 7-amide + H2O
?
-
-
-
?
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-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
-
-
-
-
?
SucLFALEVAYD-4-methylcoumarin 7-amide + H2O
?
-
-
-
?
additional information
?
-
lipid transfer protein 1 + H2O
?
-
-
-
-
?
lipid transfer protein 1 + H2O
?
-
-
-
-
?
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
?
-
-
tryptophan synthase
-
-
?
additional information
?
-
-
phosphoribosyl transferase
-
-
?
additional information
?
-
-
inactivates uridine nucleosidase
-
-
?
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
?
-
-
negligible milk clotting activity
-
-
?
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
-
-
?
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0.000398
CP-108,420
-
pH 4.7, 37°C
0.003742
CP-72,647
-
pH 4.7, 37°C
0.0009418
CP-81,198
-
pH 4.7, 37°C
0.0000071
CP-81,282
-
pH 4.7, 37°C
0.0000006 - 0.0021
IA3 inhibitor
-
0.000004
PD-129,541
-
pH 4.7, 37°C
0.0000137
PD-133,450
-
pH 4.7, 37°C
0.0000002
potato aspartic proteinase inhibitor
-
pH 4.7, 37°C
-
0.0000011
protein IA3
-
pH 4.7, 37°C
-
0.000003
protein IA3 mutant 2-34
-
pH 4.7, 37°C
-
0.0000009
protein IA3 mutant M31-M32
-
pH 4.7, 37°C
-
0.00003
tomato aspartic proteinase inhibitor
-
pH 4.7, 37°C
-
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
-
0.0000009
IA3 inhibitor
-
pH 3.1, 37°C, K31M/K32mutant inhibitor
-
0.000001
IA3 inhibitor
-
pH 4.7, 37°C, (Gly)9 inhibitor and synthetic peptide form 24 inhibitor
-
0.0000011
IA3 inhibitor
-
pH 3.1, 37°C, wild-type inhibitor
-
0.0000013
IA3 inhibitor
-
pH 3.1, 37°C, K24mutant 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
-
0.00005
IA3 inhibitor
-
pH 4.7, 37°C, MIX 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
-
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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
brenda
Meussendoerffer, F.; Tortora, P.; Holzer, H.
Purification and properties of proteinase A from yeast
J. Biol. Chem.
255
12087-12093
1980
Saccharomyces cerevisiae
brenda
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
brenda
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
brenda
Mechler, B.; Wolf, D.H.
Analysis of proteinase A function in yeast
Eur. J. Biochem.
121
47-52
1981
Saccharomyces cerevisiae
brenda
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
brenda
Dreyer, T.; Svendsen, I.; Ottesen, M.
Partial primary structure and substance specificity of proteinase A from Saccharomyces cerevisiae
Biochem. Soc. Trans.
13
1142-1143
1985
Saccharomyces cerevisiae
-
brenda
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
1976
Saccharomyces cerevisiae
brenda
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
brenda
Pedersen, J.; Biedermann, K.
Characterization of proteinase A glycoforms from recombinant Saccharomyces cerevisiae
Biotechnol. Appl. Biochem.
18
377-388
1993
Saccharomyces cerevisiae
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Nowak, J.; Tsai, H.
Purification and properties of three endopeptidases from baker's yeast
Can. J. Microbiol.
35
295-303
1989
Saccharomyces cerevisiae
brenda
Dreyer, T.
Substrate specificity of proteinase yscA from saccharomyces cerevisiae
Carlsberg Res. Commun.
54
85-97
1989
Saccharomyces cerevisiae
brenda
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
-
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Tello-Solis, S.R.
Effect of the pH in the conformation and activity of the acid protease from Aspergillus saitoi
Protein Pept. Lett.
8
101-108
2001
Aspergillus phoenicis
-
brenda
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
brenda
Bae, J.H.; Sohn, J.H.; Rhee, S.K.; Choi, E.S.
Cloning and characterization of the Hansenula polymorpha PEP4 gene encoding proteinase A
Yeast
22
13-19
2005
Ogataea angusta (O14413)
brenda
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
brenda
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
brenda
Bolumar, T.; Sanz, Y.; Aristoy, M.C.; Toldra, F.
Purification and characterisation of proteases A and D from Debaryomyces hansenii
Int. J. Food Microbiol.
124
135-141
2008
Debaryomyces hansenii, Debaryomyces hansenii CECT12487
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
Song, L.; Chen, Y.; Du, Y.; Wang, X.; Guo, X.; Dong, J.; Xiao, D.
Saccharomyces cerevisiae proteinase A excretion and wine making
World J. Microbiol. Biotechnol.
33
210
2017
Saccharomyces cerevisiae
brenda