BRENDA - Enzyme Database
show all sequences of 3.4.23.29

Polyporopepsin

Kobayashi, H.; Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ) 1, 113-115 (2004)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
DNA and amino acid sequence determination and analysis
Irpex lacteus
Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystallization by hanging drop method with ammonium sulfate as precipitant, X-ray diffraction structure determination and analysis at 1.9 A resolution
Irpex lacteus
Inhibitors
Inhibitors
Commentary
Organism
Structure
1,2-epoxy-3-(4-nitrophenoxy)propane
inactivation, active site-directed inhibitor
Irpex lacteus
Diazoacetyl-DL-norleucine methyl ester
inactivation, active site-directed inhibitor
Irpex lacteus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
x * 36000, SDS-PAGE
Irpex lacteus
Organism
Organism
UniProt
Commentary
Textmining
Irpex lacteus
-
formerly Irpex lacteus
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
two possible N-glycosylation sites at Asn192 and Asn228, the enzyme shows affinity for concanavalin A, wheat germ agglutinin, and Ricinus communis agglutinin
Irpex lacteus
Purification (Commentary)
Purification (Commentary)
Organism
native enzyme by dehydroacetylpepstatin affinity chromatography
Irpex lacteus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
alpha1-casein + H2O
cleavage of Phe23-Phe24 and Lys103-Tyr104 bonds at pH 6.0
668788
Irpex lacteus
?
-
-
-
?
beta-casein + H2O
cleavage of Leu165-Ser166, Ala189-Phe190, and Leu192-Tyr193 bonds, no cleavage of Leu139-Leu140 and Ser142-Trp143 bonds
668788
Irpex lacteus
?
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
i.e. insulin B chain, cleavage site specificity at pH 3.0.the Ala14-Leu15 bond is preferred
668788
Irpex lacteus
FVNQHLCGSHL + VEA + LYLVCGERGF + FYT + PKA
-
-
-
?
Hemoglobin + H2O
-
668788
Irpex lacteus
?
-
-
-
?
kappa-casein + H2O
cleavage of Phe105-Met106 bond
668788
Irpex lacteus
?
-
-
-
?
additional information
the enzyme requires hydrophobic amino acids at P3 and/or P4 positions, the enzyme shows high milk-clotting activity, no activity with trypsinogen, pig pepsin, and mucorpepsins
668788
Irpex lacteus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 36000, SDS-PAGE
Irpex lacteus
Synonyms
Synonyms
Commentary
Organism
milk-clotting enzyme
-
Irpex lacteus
More
the enzyme belongs to the A1 peptidase family
Irpex lacteus
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
the enzyme is the least heat-stable among the milk-clotting enzymes
Irpex lacteus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.8
2.9
substrates casein and hemoglobin
Irpex lacteus
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Irpex lacteus
-
-
5.3
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis
Irpex lacteus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystallization by hanging drop method with ammonium sulfate as precipitant, X-ray diffraction structure determination and analysis at 1.9 A resolution
Irpex lacteus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,2-epoxy-3-(4-nitrophenoxy)propane
inactivation, active site-directed inhibitor
Irpex lacteus
Diazoacetyl-DL-norleucine methyl ester
inactivation, active site-directed inhibitor
Irpex lacteus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
36000
-
x * 36000, SDS-PAGE
Irpex lacteus
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
two possible N-glycosylation sites at Asn192 and Asn228, the enzyme shows affinity for concanavalin A, wheat germ agglutinin, and Ricinus communis agglutinin
Irpex lacteus
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme by dehydroacetylpepstatin affinity chromatography
Irpex lacteus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
alpha1-casein + H2O
cleavage of Phe23-Phe24 and Lys103-Tyr104 bonds at pH 6.0
668788
Irpex lacteus
?
-
-
-
?
beta-casein + H2O
cleavage of Leu165-Ser166, Ala189-Phe190, and Leu192-Tyr193 bonds, no cleavage of Leu139-Leu140 and Ser142-Trp143 bonds
668788
Irpex lacteus
?
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
i.e. insulin B chain, cleavage site specificity at pH 3.0.the Ala14-Leu15 bond is preferred
668788
Irpex lacteus
FVNQHLCGSHL + VEA + LYLVCGERGF + FYT + PKA
-
-
-
?
Hemoglobin + H2O
-
668788
Irpex lacteus
?
-
-
-
?
kappa-casein + H2O
cleavage of Phe105-Met106 bond
668788
Irpex lacteus
?
-
-
-
?
additional information
the enzyme requires hydrophobic amino acids at P3 and/or P4 positions, the enzyme shows high milk-clotting activity, no activity with trypsinogen, pig pepsin, and mucorpepsins
668788
Irpex lacteus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 36000, SDS-PAGE
Irpex lacteus
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
additional information
-
the enzyme is the least heat-stable among the milk-clotting enzymes
Irpex lacteus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.8
2.9
substrates casein and hemoglobin
Irpex lacteus
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Irpex lacteus
-
-
5.3
Other publictions for EC 3.4.23.29
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
Synonyms
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)
754813
Mayerhofer
Acid protease production in f ...
Irpex lacteus
Mycologia
107
1-11
2015
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2
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1
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1
1
3
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1
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2
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-
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-
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1
1
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-
1
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-
-
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-
-
-
-
-
668788
Kobayashi
-
Polyporopepsin ...
Irpex lacteus
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
113-115
2004
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-
1
1
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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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6
1
2
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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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2
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1
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1
1
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6
1
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1
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1
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1
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669833
Fujimoto
Crystal structure of aspartic ...
Irpex lacteus
J. Mol. Biol.
341
1227-1235
2004
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1
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1
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2
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1
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1
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3
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1
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1
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1
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30729
Kobayashi
-
Cloning and sequence analysis ...
Irpex lacteus
Agric. Biol. Chem.
53
1927-1933
1989
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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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1
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1
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1
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30730
Kobayashi
-
Purification and characterizat ...
Irpex lacteus
Agric. Biol. Chem.
49
2393-2397
1985
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-
-
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6
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1
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1
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1
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11
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2
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2
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1
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6
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1
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1
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11
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2
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2
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1
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-
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-
30728
Kobayashi
-
Substrate specificity of a car ...
Irpex lacteus
Agric. Biol. Chem.
47
1921-1923
1983
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3
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2
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1
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1
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4
1
1
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1
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3
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2
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1
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4
1
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1
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-
-
-
-
-
-
-
-
30731
Kawai
-
Studies on the milk-clotting e ...
Irpex lacteus
Agric. Biol. Chem.
40
1463-1469
1976
-
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1
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2
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3
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1
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1
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1
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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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3
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1
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1
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2
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1
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1
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