Information on EC 3.4.23.25 - Saccharopepsin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.23.25
-
RECOMMENDED NAME
GeneOntology No.
Saccharopepsin
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
aspartic proteinase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37228-80-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain CECT12487
-
-
Manually annotated by BRENDA team
strain CECT12487
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
?
show the reaction diagram
-
-
-
?
A-L-S-A-F-(4NO2)F-R-L + H2O
?
show the reaction diagram
very effective substrate
-
-
?
A-P-A-K-F-(4NO2)F-R-L + H2O
?
show the reaction diagram
very effective substrate
-
-
?
Acid-denatured hemoglobin + H2O
?
show the reaction diagram
-
-
tyrosine-containing acid soluble peptides detected to measure enzyme activity
-
?
Ala-Leu-Ser-Ala-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Ala-Pro-Ala-Lys-Phe-(NO2)-Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Ala-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Arg-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Asp-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
?
show the reaction diagram
-
-
-
-
-
Cathepsin + H2O
?
show the reaction diagram
-
-
-
-
-
Dimethylcasein + H2O
?
show the reaction diagram
-
-
-
-
-
Gly-Ala-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
haemoglobin + H2O
?
show the reaction diagram
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
-
hemoglobin + H2O
tyrosin-containing peptides + hemoglobin fragments
show the reaction diagram
-
-
-
-
?
K-L-A-K-F-(4NO2)F-R-L + H2O
?
show the reaction diagram
-
-
-
?
K-P-A-A-F-(4NO2)F-R-L + H2O
?
show the reaction diagram
-
-
-
?
K-P-A-K-F-(4NO2)F-R-L + H2O
?
show the reaction diagram
-
-
-
?
K-P-S-K-F-(4NO2)F-R-L + H2O
?
show the reaction diagram
-
-
-
?
Leu-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Ala-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Arg-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Asp-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Leu-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Ala -Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Arg-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Leu-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Ala-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Ala + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Arg + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Asp + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Ser + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Asp-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Leu-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Ser-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ala-Ser-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Arg-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Asp-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(NO2)Phe-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + (NO2)Phe-Arg-Leu
show the reaction diagram
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu + H2O
Lys-Pro-Ile-Glu-Phe + L-nitrophenylalanine-Arg-Leu
show the reaction diagram
-
-
-
-
?
Lys-Pro-Leu-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Pro-Ser-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Lys-Ser-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Myoglobin + H2O
?
show the reaction diagram
-
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
show the reaction diagram
Oxidized B-chain of insulin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
-
procarboxypeptidase Y + H2O
propeptide of carboxypeptidase Y + carboxypeptidase Y
show the reaction diagram
-
maturation and activation of procarboxypeptidase Y
-
-
?
proproteinase A + H2O
propeptide of proteinase A + proteinase A
show the reaction diagram
-
autocatalytic activation of proproteinase A
-
-
?
proproteinase A + H2O
pseudo-proteinaseA + peptide
show the reaction diagram
autoactivation of the enzyme yields a functional protein cleaved after Ser68
Ser68 is the N-terminal amino acid
-
?
proproteinase B + H2O
propeptide of proteinase B + proteinase B
show the reaction diagram
-
maturation and activation of proproteinase B
-
-
?
Ser-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
?
Spt7p + H2O
?
show the reaction diagram
-
the enzyme is required for cleavage of Spt7p subunit within SAGA in vitro into SLIK-related Spt7p
-
-
?
Suc-APAKFFRL-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
?
Suc-RPFHLLVY-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
SucLFALEVAYD-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
procarboxypeptidase Y + H2O
propeptide of carboxypeptidase Y + carboxypeptidase Y
show the reaction diagram
-
maturation and activation of procarboxypeptidase Y
-
-
?
proproteinase A + H2O
propeptide of proteinase A + proteinase A
show the reaction diagram
-
autocatalytic activation of proproteinase A
-
-
?
proproteinase A + H2O
pseudo-proteinaseA + peptide
show the reaction diagram
P07267
autoactivation of the enzyme yields a functional protein cleaved after Ser68
Ser68 is the N-terminal amino acid
-
?
proproteinase B + H2O
propeptide of proteinase B + proteinase B
show the reaction diagram
-
maturation and activation of proproteinase B
-
-
?
Spt7p + H2O
?
show the reaction diagram
-
the enzyme is required for cleavage of Spt7p subunit within SAGA in vitro into SLIK-related Spt7p
-
-
?
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
1,2-epoxy-3-(p-nitrophenoxy) propane
-
2-mercaptoethanol
-
-
Diazoacetyl-D,L-norleucine methyl ester
-
Diazoacetyl-DL-norleucine methyl ester
HgCl2
-
complete inhibition at 0.05 mM
IA3 inhibitor
-
-
-
iodoacetate
-
weak inhibitor
leupeptin
-
strong inhibitor
natural aspartic proteinase inhibitor IA3
-
-
-
natural aspartic proteinase inhibitor IA4
-
-
-
p-chloromercuribenzoic acid
-
complete inhibition at 0.1 mM
PD-129,541
pepstatin A
-
-
PMSF
-
weak inhibitor
potato aspartic proteinase inhibitor
-
-
-
protein IA3
-
Saccharomyces cerevisiae protein
-
protein IA3 mutant 2-34
-
-
-
protein IA3 mutant M31-M32
-
-
-
Specific proteinase inhibitor from yeast
-
tomato aspartic proteinase inhibitor
-
-
-
additional information
-
insensitive to diisopropylphosphofluoridate, metal chelating agents and thiol poisons
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Urea
-
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00618
(7-methoxycoumarin-4-yl)acetyl-A-P-A-K-F-F-R-L-K(2,4-dinitrophenyl)-NH2
-
pH 4.5, 30C
0.01
Ala-Leu-Ser-Ala-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.012
Ala-Pro-Ala-Lys-Phe-(NO2)-Phe-Arg-Leu
-
pH 4.5, 30C
0.012
Ala-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.02
Arg-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.026
Asp-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.019
Gly-Ala-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.017
hemoglobin
-
-
-
0.014
Leu-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.037
Lys-Ala-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.094
Lys-Arg-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.033
Lys-Asp-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.031
Lys-Leu-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.02
Lys-Pro-Ala-Ala-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.097
Lys-Pro-Ala-Arg-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.017
Lys-Pro-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.017
Lys-Pro-Ala-Leu-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.042
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Ala -Leu
-
pH 4.5, 30C
0.095
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Ala
-
pH 4.5, 30C
0.126
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Arg
-
pH 4.5, 30C
0.024
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Asp
-
pH 4.5, 30C
0.03
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.25
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Ser
-
pH 4.5, 30C
0.068
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Asp-Leu
-
pH 4.5, 30C
0.017
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Leu-Leu
-
pH 4.5, 30C
0.073
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Ser-Leu
-
pH 4.5, 30C
0.015
Lys-Pro-Ala-Ser-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.028
Lys-Pro-Arg-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.028
Lys-Pro-Asp-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.1 - 0.25
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
0.038
Lys-Pro-Leu-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.037
Lys-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.015
Ser-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
-
pH 4.5, 30C
0.00607
Suc-APAKFFRL-4-methylcoumarin 7-amide
-
pH 4.5, 30C
0.0181
Suc-LFAEVAYD-4-methylcoumarin 7-amide
-
pH 4.5, 30C
0.0393
Suc-RFFHLLVY-4-methylcoumarin 7-amide
-
pH 4.5, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.1
(7-methoxycoumarin-4-yl)acetyl-APAKFFRLK(2,4-dinitrophenyl)-NH2
Saccharomyces cerevisiae
-
pH 4.5, 30C
10.9
Ala-Leu-Ser-Ala-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
0.012 - 14.4
Ala-Pro-Ala-Lys-Phe-(NO2)-Phe-Arg-Leu
14.4
Ala-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
14.7
Arg-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
18.6
Asp-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
19.7
Gly-Ala-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
13.8
Leu-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
6.7
Lys-Ala-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
5.8
Lys-Arg-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
2.4
Lys-Asp-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
3.5
Lys-Leu-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
15.9
Lys-Pro-Ala-Ala-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
9.4
Lys-Pro-Ala-Arg-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
1.7
Lys-Pro-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
8.4
Lys-Pro-Ala-Leu-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
1.5
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Ala -Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
6.7
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Ala
Saccharomyces cerevisiae
-
pH 4.5, 30C
2.7
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Arg
Saccharomyces cerevisiae
-
pH 4.5, 30C
1.7
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Asp
Saccharomyces cerevisiae
-
pH 4.5, 30C
4
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
4.7
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Arg-Ser
Saccharomyces cerevisiae
-
pH 4.5, 30C
2
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Asp-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
1.7
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Leu-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
0.9
Lys-Pro-Ala-Lys-Phe-4-(NO2)Phe-Ser-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
6.7
Lys-Pro-Ala-Ser-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
3.3
Lys-Pro-Arg-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
1.9
Lys-Pro-Asp-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
21 - 66
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu
10.6
Lys-Pro-Leu-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
10.4
Lys-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
6.6
Ser-Ser-Ala-Asp-Phe-4-(NO2)Phe-Arg-Leu
Saccharomyces cerevisiae
-
pH 4.5, 30C
18.5
Suc-APAKFFRL-4-methylcoumarin 7-amide
Saccharomyces cerevisiae
-
pH 4.5, 30C
3.13 - 3.73
Suc-LFAEVAYD-4-methylcoumarin 7-amide
8.25
Suc-RFFHLLVY-4-methylcoumarin 7-amide
Saccharomyces cerevisiae
-
pH 4.5, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000398
CP-108,420
-
pH 4.7, 37C
0.003742
CP-72,647
-
pH 4.7, 37C
0.0009418
CP-81,198
-
pH 4.7, 37C
0.0000071
CP-81,282
-
pH 4.7, 37C
0.0000017
IA3
-
pH 4.5
-
0.0000006 - 0.0021
IA3 inhibitor
-
0.000004
PD-129,541
-
pH 4.7, 37C
0.0000137
PD-133,450
-
pH 4.7, 37C
0.0000002
potato aspartic proteinase inhibitor
-
pH 4.7, 37C
-
0.0000011
protein IA3
-
pH 4.7, 37C
-
0.000003
protein IA3 mutant 2-34
-
pH 4.7, 37C
-
0.0000009
protein IA3 mutant M31-M32
-
pH 4.7, 37C
-
0.00003
tomato aspartic proteinase inhibitor
-
pH 4.7, 37C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
IA3
Saccharomyces cerevisiae
-
below 0.1 nM, exact detection impossible
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.4 - 2.8
-
and 5.5-6.0, casein
2.4
-
casein, azocasein
2.7 - 3.2
-
hemoglobin
3.2
-
hemoglobin
4.7
-
inactivation of nucleosidase
5 - 5.5
-
succinyl-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
5.5 - 6
-
and 2.4-2.8, casein
6
-
casein, azocasein
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 hide
LITERATURE
4 - 8
-
very low activity at other pH
4 - 6.5
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4: about 50% of activity maximum, 6.5: about 30% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
overexpression results in secretion
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
41400
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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
55000
-
gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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 hide
LITERATURE
glycoprotein
proteolytic modification
presence of putative propeptide of 55 amino acids with dibasic peptide processing site
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bound to inhibitor protein IA3, vapor diffusion, space group P6(2)22, unit cell dimensions a = b = 192.66 A, c = 52.09 A
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crystallized with and without non-hydrolyzable transition-state analogue inhibitors
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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
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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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
25C, 48 h, 80% loss of activity
30697
3.6 - 6.8
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37C, optimal pH for stability
30710
4 - 6
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25C, stable
30697
5.5
-
2 h, stable below 45C
30697
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
pH 4-6: stable, pH 3: 80% loss of activity
45
-
pH 5.5, 2 h, stable below
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilization inactivates
-
Quite stable in concentrated solutions of urea, retains full activity after 1 h at 4C in 6 M urea at pH 6.0, significant loss of activity at pH 5.0 and 7.0
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repeated freezing and thawing inactivates
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C or 0C, 0.05 M potassium phosphate buffer, pH 6.7, stable for many months
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-20C, 50 mM imidazole buffer, pH 7.0, after 3 years, 40% of the original activity is retained
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of different PEP4, PRB1, and PRC1 deficiency mutants
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expression in Xenopus oocytes
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overproduction-induced mislocation of the enzyme protein allows isolation of its structural gene
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A213I
-
increased Km and 50% higher turnover than wild type enzyme
D294A
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inactive
T222A
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50% of wild type turnover
T287A/P288G
-
50% of wild type turnover
additional information
enzyme disruption mutant, significantly reduced level of carboxypeptidase Y activity. Overproduction of enzyme leads to sectretion into growth medium
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
medicine