BRENDA - Enzyme Database show
show all sequences of 3.4.23.20

Purification and properties of the thermostable acid protease of Penicillium duponti

Emi, S.; Myers, D.V.; Iacobucci, G.A.; Biochemistry 15, 842-848 (1976)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
alpha-Diazo-p-bromoacetophenone
in presence of Cu2+
Penicillium duponti
Diazoacetyl DL-norleucine methyl ester
in presence of Cu2+
Penicillium duponti
Diazoacetylglycine ethyl ester
in presence of Cu2+
Penicillium duponti
additional information
p-bromophenacylbromide
Penicillium duponti
Specific pepsin inhibitor produced by Streptomyces naniwaensis
-
Penicillium duponti
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41590
-
Penicillium duponti, calculated from amino acid composition
Penicillium duponti
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Penicillium duponti
-
K 1014
-
Penicillium duponti K 1014
-
K 1014
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
contains 4.33% carbohydrate expressed as glucose
Penicillium duponti
Purification (Commentary)
Commentary
Organism
-
Penicillium duponti
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Penicillium duponti
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Egg albumin + H2O
best substrate, 30% of the peptide bonds are split after 48 h, at 37C, pH 3.0
30586
Penicillium duponti
?
-
-
-
-
Egg albumin + H2O
best substrate, 30% of the peptide bonds are split after 48 h, at 37C, pH 3.0
30586
Penicillium duponti K 1014
?
-
-
-
-
Hemoglobin + H2O
best substrate, 30% of the peptide bonds are split after 48 h, at 37C, pH 3.0
30586
Penicillium duponti
?
-
-
-
-
Hemoglobin + H2O
best substrate, 30% of the peptide bonds are split after 48 h, at 37C, pH 3.0
30586
Penicillium duponti K 1014
?
-
-
-
-
Milk casein + H2O
-
30586
Penicillium duponti
?
-
-
-
-
Milk casein + H2O
-
30586
Penicillium duponti K 1014
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
60
-
at pH 2.5, 10 min incubation
Penicillium duponti
75
-
at pH 3.7, 10 min incubation
Penicillium duponti
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
pH 2.5-6.5, 24 h, stable
Penicillium duponti
60
-
pH 3.5-5.5, 1 h, stable
Penicillium duponti
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.5
-
milk casein
Penicillium duponti
3
3.5
hemoglobin, egg albumin
Penicillium duponti
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
2.5
6.5
30C, 24 h, stable
Penicillium duponti
2.5
-
65C, complete loss of activity after 15 min, 60C, complete loss of activity after 60 min
Penicillium duponti
3.5
5.5
60C, 1 h, stable
Penicillium duponti
4.5
-
at 65C, stable for 15 min, at 60C, stable for 60 min
Penicillium duponti
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
alpha-Diazo-p-bromoacetophenone
in presence of Cu2+
Penicillium duponti
Diazoacetyl DL-norleucine methyl ester
in presence of Cu2+
Penicillium duponti
Diazoacetylglycine ethyl ester
in presence of Cu2+
Penicillium duponti
additional information
p-bromophenacylbromide
Penicillium duponti
Specific pepsin inhibitor produced by Streptomyces naniwaensis
-
Penicillium duponti
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41590
-
Penicillium duponti, calculated from amino acid composition
Penicillium duponti
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
contains 4.33% carbohydrate expressed as glucose
Penicillium duponti
Purification (Commentary) (protein specific)
Commentary
Organism
-
Penicillium duponti
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Penicillium duponti
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Egg albumin + H2O
best substrate, 30% of the peptide bonds are split after 48 h, at 37C, pH 3.0
30586
Penicillium duponti
?
-
-
-
-
Egg albumin + H2O
best substrate, 30% of the peptide bonds are split after 48 h, at 37C, pH 3.0
30586
Penicillium duponti K 1014
?
-
-
-
-
Hemoglobin + H2O
best substrate, 30% of the peptide bonds are split after 48 h, at 37C, pH 3.0
30586
Penicillium duponti
?
-
-
-
-
Hemoglobin + H2O
best substrate, 30% of the peptide bonds are split after 48 h, at 37C, pH 3.0
30586
Penicillium duponti K 1014
?
-
-
-
-
Milk casein + H2O
-
30586
Penicillium duponti
?
-
-
-
-
Milk casein + H2O
-
30586
Penicillium duponti K 1014
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
60
-
at pH 2.5, 10 min incubation
Penicillium duponti
75
-
at pH 3.7, 10 min incubation
Penicillium duponti
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
pH 2.5-6.5, 24 h, stable
Penicillium duponti
60
-
pH 3.5-5.5, 1 h, stable
Penicillium duponti
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.5
-
milk casein
Penicillium duponti
3
3.5
hemoglobin, egg albumin
Penicillium duponti
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
2.5
6.5
30C, 24 h, stable
Penicillium duponti
2.5
-
65C, complete loss of activity after 15 min, 60C, complete loss of activity after 60 min
Penicillium duponti
3.5
5.5
60C, 1 h, stable
Penicillium duponti
4.5
-
at 65C, stable for 15 min, at 60C, stable for 60 min
Penicillium duponti
Other publictions for EC 3.4.23.20
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
670005
Vidossich
Binding of phosphinate and pho ...
Penicillium janthinellum
J. Phys. Chem. B
110
1437-1442
2006
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-
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2
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2
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2
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668813
Hofmann
-
Penicillopepsin ...
Penicillium camemberti, Penicillium duponti, Penicillium duponti K1014, Penicillium janthinellum, Penicillium roqueforti
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
99-104
2004
-
-
1
1
4
-
4
1
-
-
5
-
-
7
-
3
4
-
-
-
-
-
16
5
-
-
-
1
-
-
-
-
-
2
-
-
-
3
-
1
4
-
-
4
-
1
-
-
5
-
-
-
5
5
-
-
-
-
16
6
-
-
-
1
-
-
-
2
-
-
-
-
-
-
653829
Cao
Penicillopepsin-JT2, a recombi ...
Penicillium janthinellum, Penicillium janthinellum NRRL 905
Protein Sci.
9
991-1001
2000
-
-
1
-
4
-
1
47
-
-
1
-
-
5
-
1
1
-
-
-
-
-
15
-
-
-
-
47
-
-
-
-
5
-
-
-
-
1
-
-
4
-
-
1
5
47
-
-
1
-
-
-
1
1
-
-
-
-
15
-
-
-
-
47
-
-
-
-
-
-
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-
649272
Fraser
Overcoming the unfavourable en ...
Penicillium sp.
Adv. Exp. Med. Biol.
436
355-359
1998
-
-
-
1
-
-
3
-
-
-
-
-
-
1
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-
-
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-
-
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-
1
-
-
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-
-
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-
3
-
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-
1
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-
-
3
3
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-
1
-
-
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-
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-
-
-
649841
Khan
Lowering the entropic barrier ...
Penicillium janthinellum
Biochemistry
37
16839-16845
1998
-
1
-
1
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-
2
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2
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1
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1
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1
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2
1
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-
30601
James
Crystallographic analysis of t ...
Penicillium janthinellum
Biochemistry
31
3872-3886
1992
-
-
-
1
-
-
1
-
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1
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1
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1
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-
-
30602
Fraser
Crystallographic analysis of t ...
Penicillium janthinellum
Biochemistry
31
5201-5214
1992
-
-
-
1
-
-
1
-
-
-
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-
-
1
-
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1
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1
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30588
Hofmann
Effect of secondary substrate ...
Penicillium janthinellum
Biochemistry
27
1140-1146
1988
-
-
-
-
-
-
-
7
-
-
-
-
-
1
-
-
-
-
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-
6
-
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-
4
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7
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6
-
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-
4
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30589
Dunn
A systematic series of synthet ...
Penicillium janthinellum
Biochem. J.
237
899-906
1986
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2
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1
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1
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2
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2
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1
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2
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30597
Blum
Penicillopepsin, the aspartic ...
Penicillium janthinellum
Biochem. Soc. Trans.
13
1044-1046
1985
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-
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2
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1
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2
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3
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1
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2
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1
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3
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1
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30598
James
Stereochemical analysis of pep ...
Penicillium janthinellum
Biochemistry
24
3701-3713
1985
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1
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1
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30599
Hofmann
Effect of pH on the activities ...
Penicillium janthinellum
Biochemistry
23
635-643
1984
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4
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2
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3
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5
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30600
James
Structure and refinement of pe ...
Penicillium janthinellum
J. Mol. Biol.
163
299-361
1983
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30603
Houmard
Further characterization of th ...
Penicillium roqueforti
Biochimie
61
979-982
1979
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30587
Hsu
Penicillopepsin from Penicilli ...
Penicillium janthinellum
Nature
266
140-145
1977
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1
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1
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3
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30590
James
Mechanism of acid protease cat ...
Penicillium janthinellum
Nature
267
808-813
1977
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1
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30592
Wang
Acyl and amino intermediates i ...
Penicillium janthinellum
Can. J. Biochem.
55
286-294
1977
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1
1
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1
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1
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1
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1
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30585
Hofmann
Penicillopepsin ...
Penicillium janthinellum
Methods Enzymol.
45
434-452
1976
1
-
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9
1
1
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2
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1
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1
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1
1
4
-
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2
1
3
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4
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1
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9
-
1
1
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2
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1
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1
1
4
-
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2
1
3
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4
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30586
Emi
Purification and properties of ...
Penicillium duponti, Penicillium duponti K 1014
Biochemistry
15
842-848
1976
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6
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2
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30593
Hsu
The crystal structure of penic ...
Penicillium janthinellum
Biochem. Biophys. Res. Commun.
72
363-368
1976
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1
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30594
Mabrouk
-
A rennin-like enzyme from Peni ...
Penicillium expansum
Agric. Biol. Chem.
40
419-420
1976
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30604
Gripon
Inactivation of Penicillium ro ...
Penicillium roqueforti
Biochimie
58
747-749
1976
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4
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30591
Mains
The inactivation of penicillop ...
Penicillium janthinellum
Can. J. Biochem.
52
1018-1023
1974
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30595
Hashimoto
Some properties of acid protea ...
Penicillium duponti, Penicillium duponti K 1014
Appl. Microbiol.
25
578-583
1973
1
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4
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30596
Hashimoto
Production and purification of ...
Penicillium duponti, Penicillium duponti K 1014
Appl. Microbiol.
25
584-588
1973
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4
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1
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