BRENDA - Enzyme Database show
show all sequences of 3.4.21.25

Religiosin C, a cucumisin-like serine protease from Ficus religiosa

Sharma, A.; Kumari, M.; Jagannadham, M.; Process Biochem. 47, 914-921 (2012)
No PubMed abstract available

Data extracted from this reference:

Application
Application
Commentary
Organism
food industry
the high milk-clotting ability of religiosin C supports its use in the food industry
Ficus religiosa
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetonitrile
60.03% residual activity at 50% (v/v)
Ficus religiosa
butanol
68.24% residual activity at 50% (v/v)
Ficus religiosa
chymostatin
2.45% residual activity at 5 mM
Ficus religiosa
diisopropylfluorophosphate
2.34% residual activity at 1 mM
Ficus religiosa
dioxane
65.35% residual activity at 50% (v/v)
Ficus religiosa
ethanol
75.09% residual activity at 50% (v/v)
Ficus religiosa
additional information
not inhibited by EDTA, EGTA, iodoacetic acid, 2-phenanthroline, SBTI, and dithiothreitol
Ficus religiosa
phenylmethylsulfonyl fluoride
5.12% residual activity at 5 mM
Ficus religiosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
0.004
-
L-alanyl-L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
0.093
-
L-leucyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
0.273
-
L-gamma-glutamyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
the enzyme is not influenced by Hg2+, Na+, K+, Mg2+, Ca2+, Rb+, and Li+
Ficus religiosa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
80000
-
1 * 80000, SDS-PAGE
Ficus religiosa
Organic Solvent Stability
Organic Solvent
Commentary
Organism
additional information
the enzyme is not influenced by urea, methanol, and guanidine hydrochloride
Ficus religiosa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ficus religiosa
-
-
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Superdex 200 gel filtration
Ficus religiosa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
latex
-
Ficus religiosa
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
enzyme from crude latex shows a specific activity of 23.99 units/mg at pH 8.0 and 37°C. After 2.29fold purification, the enzyme shows a specific activity of 55.01 units/mg at pH 8.0 and 37°C. One unit of enzyme activity is defined as the amount of enzyme that gives rise to an increase in one unit of absorbance at 280 nm per min of casein digestion
Ficus religiosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
casein + H2O
-
732844
Ficus religiosa
?
-
-
-
?
L-alanyl-4-nitroanilide + H2O
-
732844
Ficus religiosa
L-alanine + 4-nitroaniline
-
-
-
?
L-alanyl-L-alanyl-4-nitroanilide + H2O
-
732844
Ficus religiosa
L-alanyl-L-alanine + 4-nitroaniline
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
-
732844
Ficus religiosa
L-glutamate + 4-nitroaniline
-
-
-
?
L-leucyl-4-nitroanilide + H2O
-
732844
Ficus religiosa
L-leucine + 4-nitroaniline
-
-
-
?
additional information
no activity toward Nalpha-benzoyl-DL-arginyl-4-nitroanilide and N-succinyl-L-phenylalanyl-4-nitroanilide
732844
Ficus religiosa
?
-
-
-
-
skim milk + H2O
-
732844
Ficus religiosa
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 80000, SDS-PAGE
Ficus religiosa
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
50
-
Ficus religiosa
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
40
55
more than 80% of the activity is observed from 40 to 55°C. The activity decreases steadily as the temperature rises over 60°C and no activity is observed at 80°C
Ficus religiosa
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
20
70
the enzyme shows more than 90% activity up to 60°C for 30 min. 87% of activity is observed at 70°C when incubated for 30 min
Ficus religiosa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
25.48
-
L-alanyl-L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
32.13
-
L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
207.8
-
L-gamma-glutamyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
749.7
-
L-leucyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8
-
Ficus religiosa
pH Range
pH Minimum
pH Maximum
Commentary
Organism
3.5
11.5
the enzyme retains more than 80% of activity from pH 3.5 to 11.5. No activity is observed at or below pH 2.0
Ficus religiosa
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
4
11.5
the enzyme shows more than 90% activity when incubated at pH 4.5 to 11.5 for 30 min
Ficus religiosa
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Ficus religiosa
isoelectric focusing
-
4.6
Application (protein specific)
Application
Commentary
Organism
food industry
the high milk-clotting ability of religiosin C supports its use in the food industry
Ficus religiosa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetonitrile
60.03% residual activity at 50% (v/v)
Ficus religiosa
butanol
68.24% residual activity at 50% (v/v)
Ficus religiosa
chymostatin
2.45% residual activity at 5 mM
Ficus religiosa
diisopropylfluorophosphate
2.34% residual activity at 1 mM
Ficus religiosa
dioxane
65.35% residual activity at 50% (v/v)
Ficus religiosa
ethanol
75.09% residual activity at 50% (v/v)
Ficus religiosa
additional information
not inhibited by EDTA, EGTA, iodoacetic acid, 2-phenanthroline, SBTI, and dithiothreitol
Ficus religiosa
phenylmethylsulfonyl fluoride
5.12% residual activity at 5 mM
Ficus religiosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
0.004
-
L-alanyl-L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
0.093
-
L-leucyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
0.273
-
L-gamma-glutamyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
the enzyme is not influenced by Hg2+, Na+, K+, Mg2+, Ca2+, Rb+, and Li+
Ficus religiosa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
80000
-
1 * 80000, SDS-PAGE
Ficus religiosa
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
additional information
the enzyme is not influenced by urea, methanol, and guanidine hydrochloride
Ficus religiosa
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Superdex 200 gel filtration
Ficus religiosa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
latex
-
Ficus religiosa
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
enzyme from crude latex shows a specific activity of 23.99 units/mg at pH 8.0 and 37°C. After 2.29fold purification, the enzyme shows a specific activity of 55.01 units/mg at pH 8.0 and 37°C. One unit of enzyme activity is defined as the amount of enzyme that gives rise to an increase in one unit of absorbance at 280 nm per min of casein digestion
Ficus religiosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
casein + H2O
-
732844
Ficus religiosa
?
-
-
-
?
L-alanyl-4-nitroanilide + H2O
-
732844
Ficus religiosa
L-alanine + 4-nitroaniline
-
-
-
?
L-alanyl-L-alanyl-4-nitroanilide + H2O
-
732844
Ficus religiosa
L-alanyl-L-alanine + 4-nitroaniline
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + H2O
-
732844
Ficus religiosa
L-glutamate + 4-nitroaniline
-
-
-
?
L-leucyl-4-nitroanilide + H2O
-
732844
Ficus religiosa
L-leucine + 4-nitroaniline
-
-
-
?
additional information
no activity toward Nalpha-benzoyl-DL-arginyl-4-nitroanilide and N-succinyl-L-phenylalanyl-4-nitroanilide
732844
Ficus religiosa
?
-
-
-
-
skim milk + H2O
-
732844
Ficus religiosa
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 80000, SDS-PAGE
Ficus religiosa
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
50
-
Ficus religiosa
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
40
55
more than 80% of the activity is observed from 40 to 55°C. The activity decreases steadily as the temperature rises over 60°C and no activity is observed at 80°C
Ficus religiosa
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
20
70
the enzyme shows more than 90% activity up to 60°C for 30 min. 87% of activity is observed at 70°C when incubated for 30 min
Ficus religiosa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
25.48
-
L-alanyl-L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
32.13
-
L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
207.8
-
L-gamma-glutamyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
749.7
-
L-leucyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8
-
Ficus religiosa
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
3.5
11.5
the enzyme retains more than 80% of activity from pH 3.5 to 11.5. No activity is observed at or below pH 2.0
Ficus religiosa
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
4
11.5
the enzyme shows more than 90% activity when incubated at pH 4.5 to 11.5 for 30 min
Ficus religiosa
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Ficus religiosa
isoelectric focusing
-
4.6
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
422.2
-
L-leucyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
749.7
-
L-gamma-glutamyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
6888
-
L-alanyl-L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
13910
-
L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
422.2
-
L-leucyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
749.7
-
L-gamma-glutamyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
6888
-
L-alanyl-L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
13910
-
L-alanyl-4-nitroanilide
at pH 8.0 and 37°C
Ficus religiosa
Other publictions for EC 3.4.21.25
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)
732337
Murayama
Crystal structure of cucumisin ...
Cucumis melo
J. Mol. Biol.
423
386-396
2012
-
-
-
1
-
-
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1
-
-
-
-
4
-
1
1
-
-
2
-
-
1
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1
-
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1
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1
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1
1
-
2
-
-
1
-
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-
1
-
-
-
-
-
-
-
-
-
-
-
732643
Tan-Wilson
The PA domain is crucial for d ...
Glycine max
Plant Physiol. Biochem.
53
27-32
2012
-
-
-
-
-
-
-
1
-
-
-
1
-
3
-
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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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-
-
-
-
-
-
-
-
1
1
732844
Sharma
-
Religiosin C, a cucumisin-like ...
Ficus religiosa
Process Biochem.
47
914-921
2012
-
1
-
-
-
-
8
4
-
1
1
-
1
1
-
-
1
-
-
1
1
-
7
1
1
1
1
4
1
1
1
-
-
1
-
-
1
-
-
-
-
-
-
8
-
4
-
1
1
-
1
-
-
1
-
1
1
-
7
1
1
1
1
4
1
1
1
1
-
-
-
-
4
4
717062
Sankian
Molecular cloning and expressi ...
Cucumis melo
Allergol. Int.
60
61-67
2011
-
-
1
-
-
-
-
-
-
-
1
-
-
3
-
-
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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-
-
-
717802
Nakagawa
Functional analysis of the cuc ...
Cucumis melo
J. Biol. Chem.
285
29797-29807
2010
-
-
1
-
-
-
4
-
1
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4
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1
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1
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1
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3
-
1
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1
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1
4
3
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1
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1
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1
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-
1
-
-
-
-
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-
-
-
-
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-
-
-
-
-
683714
He
Protein storage vacuole acidif ...
Glycine max
J. Exp. Bot.
58
1059-1070
2007
-
1
-
-
-
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-
2
-
1
-
-
4
-
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1
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4
1
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1
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1
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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4
1
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1
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-
1
1
-
-
-
-
-
-
-
-
670521
Asif-Ullah
Purification and characterizat ...
Cucumis trigonus
Phytochemistry
67
870-875
2006
-
1
-
-
-
-
2
-
-
-
1
-
-
3
-
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1
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3
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5
-
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
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-
3
-
5
-
1
-
1
-
1
-
1
-
-
-
-
-
-
-
670222
Choi
Cloning of genes differentiall ...
Cucumis melo
Mol. Cells
17
237-241
2004
-
1
-
-
-
-
-
-
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1
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1
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-
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-
-
-
-
-
-
650612
Yonezawa
Substrate specificity of cucum ...
Cucumis melo
Biosci. Biotechnol. Biochem.
64
2104-2108
2000
-
-
-
-
-
-
-
12
-
-
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-
1
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-
26
-
1
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-
12
1
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12
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-
26
-
1
-
-
12
1
-
-
-
-
-
-
-
-
-
95355
Kaneda
Purification and some properti ...
Cucumis melo
Biosci. Biotechnol. Biochem.
61
2100-2102
1997
-
-
-
-
-
-
5
8
-
1
-
1
-
1
-
-
1
-
-
1
-
-
11
-
-
-
-
8
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
5
-
8
-
1
-
1
-
-
-
1
-
1
-
-
11
-
-
-
-
8
1
1
1
-
-
-
-
-
-
-
95356
Uchikoba
Milk-clotting activity of cucu ...
Cucumis melo
Appl. Biochem. Biotechnol.
56
325-330
1996
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95357
Kaneda
Improved isolation, stability ...
Cucumis melo
Biotechnol. Appl. Biochem.
22
215-222
1995
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4
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2
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1
1
4
2
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1
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9
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5
2
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4
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1
1
4
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1
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9
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5
2
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95358
Uchikoba
Cleavage specificity of cucumi ...
Cucumis melo
J. Biochem.
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1126-1130
1995
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1
3
6
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1
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3
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1
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20
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1
6
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1
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1
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3
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6
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1
1
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1
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20
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1
6
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1
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95353
Yamagata
Cucumisin, a serine protease f ...
Cucumis melo
J. Biol. Chem.
269
32725-32731
1994
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1
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1
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95354
Yamagata
-
Isolation and characterization ...
Cucumis melo
Agric. Biol. Chem.
53
1009-1017
1989
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4
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1
2
1
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1
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3
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1
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3
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1
1
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4
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1
2
1
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1
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1
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3
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1
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3
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1
1
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95347
Kaneda
-
Properties of a new plant seri ...
Cucumis melo
Agric. Biol. Chem.
51
489-492
1987
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1
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1
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1
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3
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2
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2
2
1
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95348
Kaneda
-
Photochemical oxidation of cuc ...
Cucumis melo
Agric. Biol. Chem.
51
1159-1161
1987
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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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95349
Kaneda
-
Active site titration of the s ...
Cucumis melo
Phytochemistry
25
2407-2408
1986
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1
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3
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1
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95352
Kaneda
-
Specificity of cucumisin in hy ...
Cucumis melo
Agric. Biol. Chem.
50
1075-1076
1986
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1
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1
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14
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11
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1
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14
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11
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95350
Kaneda
Amino acid sequence around the ...
Cucumis melo
J. Biochem.
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825-829
1984
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1
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1
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1
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1
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3
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95351
Kaneda
Isolation and characterization ...
Cucumis melo
J. Biochem.
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1287-1296
1975
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4
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1
1
1
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1
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1
1
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2
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7
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1
1
1
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1
1
2
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4
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1
1
1
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1
1
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2
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7
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1
1
1
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1
1
2
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