BRENDA - Enzyme Database show
show all sequences of 3.4.23.20

Some properties of acid protease from the thermophilic fungus, Penicillium duponti K1014

Hashimoto, H.; Iwaasa, T.; Yokotsuka, T.; Appl. Microbiol. 25, 578-583 (1973)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Reagents converting sulfhydryl groups to mercaptides
activate
Penicillium duponti
Inhibitors
Inhibitors
Commentary
Organism
Structure
KMnO4
-
Penicillium duponti
additional information
chelating agents; potato inhibitor
Penicillium duponti
N-bromosuccinimide
-
Penicillium duponti
sodium lauryl sulfate
-
Penicillium duponti
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41000
-
Penicillium duponti, gel filtration
Penicillium duponti
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Penicillium duponti
-
K 1014
-
Penicillium duponti K 1014
-
K 1014
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Trypsinogen + H2O
-
30595
Penicillium duponti
?
-
-
-
-
Trypsinogen + H2O
-
30595
Penicillium duponti K 1014
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
at pH 2.5, hemoglobin, 30 min incubation
Penicillium duponti
70
-
at pH 3.6, hemoglobin, 30 min incubation
Penicillium duponti
75
-
at pH 4.6, hemoglobin, 30 min incubation
Penicillium duponti
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
pH 2.5-6.0, 20 h, stable
Penicillium duponti
60
-
pH 3.5-5.5, 1 h, stable
Penicillium duponti
70
-
pH 4.5, 1 h, more than 65% of activity is retained
Penicillium duponti
80
-
pH 4.5, 10 min, complete inactivation
Penicillium duponti
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3
-
hemoglobin, trypsinogen
Penicillium duponti
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
2.5
6
30°C, 20 h, stable
Penicillium duponti
3.5
5.5
60°C, 1 h, stable
Penicillium duponti
4.5
-
70°C, 1 h, more than 65% of the activity is retained; 80°C, 10 min, complete inactivation
Penicillium duponti
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Reagents converting sulfhydryl groups to mercaptides
activate
Penicillium duponti
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
KMnO4
-
Penicillium duponti
additional information
chelating agents; potato inhibitor
Penicillium duponti
N-bromosuccinimide
-
Penicillium duponti
sodium lauryl sulfate
-
Penicillium duponti
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
41000
-
Penicillium duponti, gel filtration
Penicillium duponti
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Trypsinogen + H2O
-
30595
Penicillium duponti
?
-
-
-
-
Trypsinogen + H2O
-
30595
Penicillium duponti K 1014
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
at pH 2.5, hemoglobin, 30 min incubation
Penicillium duponti
70
-
at pH 3.6, hemoglobin, 30 min incubation
Penicillium duponti
75
-
at pH 4.6, hemoglobin, 30 min incubation
Penicillium duponti
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
pH 2.5-6.0, 20 h, stable
Penicillium duponti
60
-
pH 3.5-5.5, 1 h, stable
Penicillium duponti
70
-
pH 4.5, 1 h, more than 65% of activity is retained
Penicillium duponti
80
-
pH 4.5, 10 min, complete inactivation
Penicillium duponti
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3
-
hemoglobin, trypsinogen
Penicillium duponti
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
2.5
6
30°C, 20 h, stable
Penicillium duponti
3.5
5.5
60°C, 1 h, stable
Penicillium duponti
4.5
-
70°C, 1 h, more than 65% of the activity is retained; 80°C, 10 min, complete inactivation
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
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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2
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-
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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
-
-
-
-
-
-
-
-
-
-
649272
Fraser
Overcoming the unfavourable en ...
Penicillium sp.
Adv. Exp. Med. Biol.
436
355-359
1998
-
-
-
1
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
3
3
-
-
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-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
649841
Khan
Lowering the entropic barrier ...
Penicillium janthinellum
Biochemistry
37
16839-16845
1998
-
1
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
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1
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-
1
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-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30601
James
Crystallographic analysis of t ...
Penicillium janthinellum
Biochemistry
31
3872-3886
1992
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
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-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30602
Fraser
Crystallographic analysis of t ...
Penicillium janthinellum
Biochemistry
31
5201-5214
1992
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
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-
1
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30588
Hofmann
Effect of secondary substrate ...
Penicillium janthinellum
Biochemistry
27
1140-1146
1988
-
-
-
-
-
-
-
7
-
-
-
-
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
30589
Dunn
A systematic series of synthet ...
Penicillium janthinellum
Biochem. J.
237
899-906
1986
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
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-
-
-
-
-
1
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-
-
2
-
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-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
30597
Blum
Penicillopepsin, the aspartic ...
Penicillium janthinellum
Biochem. Soc. Trans.
13
1044-1046
1985
-
-
-
-
-
-
2
-
1
-
-
-
-
2
-
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-
-
-
-
-
-
3
-
-
-
-
1
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-
-
-
-
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-
-
-
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-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
30598
James
Stereochemical analysis of pep ...
Penicillium janthinellum
Biochemistry
24
3701-3713
1985
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
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-
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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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4
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-
3
-
-
-
-
5
-
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-
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-
-
-
-
30600
James
Structure and refinement of pe ...
Penicillium janthinellum
J. Mol. Biol.
163
299-361
1983
-
-
-
1
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-
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1
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1
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-
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-
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-
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-
-
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-
-
-
-
30603
Houmard
Further characterization of th ...
Penicillium roqueforti
Biochimie
61
979-982
1979
-
-
-
-
-
-
-
-
-
-
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-
-
1
-
1
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2
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-
1
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30587
Hsu
Penicillopepsin from Penicilli ...
Penicillium janthinellum
Nature
266
140-145
1977
-
-
-
1
-
-
-
-
-
-
1
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3
-
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1
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1
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-
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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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1
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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
-
-
-
-
-
-
1
1
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1
-
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1
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1
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1
-
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
-
-
-
-
-
9
1
1
-
2
-
-
1
-
-
1
-
-
-
1
1
4
-
-
-
2
1
3
-
4
-
-
-
-
1
-
-
-
-
-
-
-
9
-
1
1
-
2
-
-
-
-
1
-
-
1
1
4
-
-
-
2
1
3
-
4
-
-
-
-
-
-
-
30586
Emi
Purification and properties of ...
Penicillium duponti, Penicillium duponti K 1014
Biochemistry
15
842-848
1976
-
-
-
-
-
-
5
-
-
-
1
-
-
4
-
1
1
-
-
-
1
-
6
-
2
-
2
-
2
-
4
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
1
-
-
-
1
1
-
-
1
-
6
-
2
-
2
-
2
-
4
-
-
-
-
-
-
-
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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1
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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
1
-
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4
-
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2
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1
-
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1
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-
1
-
1
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-
2
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1
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4
-
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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
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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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1
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30591
Mains
The inactivation of penicillop ...
Penicillium janthinellum
Can. J. Biochem.
52
1018-1023
1974
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1
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1
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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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1
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4
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4
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4
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3
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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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1
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