BRENDA - Enzyme Database show
show all sequences of 3.4.23.40

Activation, proteolytic processing, and peptide specificity of recombinant cardosin A

Castanheira, P.; Samyn, B.; Sergeant, K.; Clemente, J.C.; Dunn, B.M.; Pires, E.; Van Beeumen, J.; Faro, C.; J. Biol. Chem. 280, 13047-13054 (2005)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
D32A
active site mutant, inactive, no processing of proenzyme
Cynara cardunculus
Inhibitors
Inhibitors
Commentary
Organism
Structure
pepstatin
-
Cynara cardunculus
pepstatin A
-
Cynara cardunculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.3
-
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
37°C, pH 7.4
Cynara cardunculus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
11000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
26000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
37000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
47000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cynara cardunculus
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
proteolytic modification
autocatalytic processing, optimal processing at pH 4.0
Cynara cardunculus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
flower
-
Cynara cardunculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu + H2O
-
669314
Cynara cardunculus
?
-
-
-
?
additional information
preference for phenylalanine, leucine or norleucine at P! site, for tyrosine or phenylalanine at P1’ site
669314
Cynara cardunculus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
45
-
Cynara cardunculus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
65
-
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
37°C, pH 7.4
Cynara cardunculus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4
4.5
-
Cynara cardunculus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
2.5
6
-
Cynara cardunculus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.000001
-
pepstatin
37°C, pH 7.4
Cynara cardunculus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D32A
active site mutant, inactive, no processing of proenzyme
Cynara cardunculus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
pepstatin
-
Cynara cardunculus
pepstatin A
-
Cynara cardunculus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.000001
-
pepstatin
37°C, pH 7.4
Cynara cardunculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.3
-
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
37°C, pH 7.4
Cynara cardunculus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
11000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
26000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
37000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
47000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
proteolytic modification
autocatalytic processing, optimal processing at pH 4.0
Cynara cardunculus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
flower
-
Cynara cardunculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu + H2O
-
669314
Cynara cardunculus
?
-
-
-
?
additional information
preference for phenylalanine, leucine or norleucine at P! site, for tyrosine or phenylalanine at P1’ site
669314
Cynara cardunculus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
Cynara cardunculus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
45
-
Cynara cardunculus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
65
-
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
37°C, pH 7.4
Cynara cardunculus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4
4.5
-
Cynara cardunculus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
2.5
6
-
Cynara cardunculus
Other publictions for EC 3.4.23.40
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)
733194
Almeida
Engineering a cardosin B-deriv ...
Cynara cardunculus
Appl. Microbiol. Biotechnol.
99
269-281
2015
-
1
1
-
-
-
-
-
-
-
2
-
-
8
-
1
-
-
-
3
-
-
3
1
1
-
2
-
1
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
3
-
-
3
1
1
-
2
-
1
-
-
-
1
-
-
1
-
-
733901
Llorente
Use of artichoke (Cynara scoly ...
Cynara cardunculus var. scolymus
Food Chem.
159
55-63
2014
-
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
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-
-
-
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-
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-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
734555
Raimbault
A novel aspartic acid protease ...
Ananas comosus
J. Plant Physiol.
170
1536-1540
2013
-
1
-
-
-
-
-
-
-
-
1
-
-
3
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
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1
-
-
-
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1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
1
-
-
1
-
-
734915
Pereira
Cardosin A contains two vacuol ...
Cynara cardunculus
Plant J.
76
87-100
2013
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
669314
Castanheira
Activation, proteolytic proces ...
Cynara cardunculus
J. Biol. Chem.
280
13047-13054
2005
-
-
-
-
1
-
2
1
-
-
4
-
-
3
-
1
-
-
-
1
-
-
2
1
1
-
-
1
1
1
-
-
1
-
-
-
-
-
-
-
1
-
-
2
1
1
-
-
4
-
-
-
1
-
-
1
-
-
2
1
1
-
-
1
1
1
-
-
-
-
-
-
-
-
670515
Sidrach
Purification of cynarases from ...
Cynara cardunculus var. scolymus
Phytochemistry
66
41-49
2005
-
-
-
-
-
-
1
1
-
-
8
-
-
6
-
1
1
-
-
1
-
-
1
1
1
-
2
1
1
2
-
-
1
3
-
-
-
-
-
-
-
-
-
1
1
1
-
-
8
-
-
-
1
1
-
1
-
-
1
1
1
-
2
1
1
2
-
3
-
-
-
-
-
-
649256
Prasad
Role of water molecules in the ...
Hordeum vulgare
Acta Crystallogr. Sect. D
D58
250-259
2002
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
650630
Park
Autoproteolytic processing of ...
Helianthus annuus
Biosci. Biotechnol. Biochem.
65
702-705
2001
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
734130
Frazao
Crystal structure of cardosin ...
Cynara cardunculus
J. Biol. Chem.
274
27694-27701
1999
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30849
Belozersky
Aspartic proteinase from wheat ...
Triticum aestivum
Planta
177
321-326
1998
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
1
-
-
1
1
-
2
-
1
-
1
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
1
1
-
2
-
1
-
1
-
2
-
1
-
-
-
-
-
-
-
733764
Verissimo
Purification, characterization ...
Cynara cardunculus
Eur. J. Biochem.
235
762-768
1996
-
-
-
-
-
-
2
4
-
-
3
-
-
3
-
-
-
-
-
-
1
-
4
1
-
-
1
4
1
1
-
-
2
-
-
-
-
-
-
-
-
-
-
4
2
4
-
-
4
-
-
-
-
-
-
-
2
-
4
2
-
-
2
4
2
2
-
-
-
-
-
-
4
4
30844
Kervinen
Structure and possible functio ...
Brassica napus, Cannabis sativa, Cucumis sativus, Cucurbita maxima, Cynara cardunculus, Drosera peltata, Fagopyrum esculentum, Hordeum vulgare, Nelumbo nucifera, Nepenthes macfarlanei, Nicotiana tabacum, Oryza sativa, Pinus banksiana, Pinus sylvestris, Solanum lycopersicum, Sorghum bicolor, Theobroma cacao, Triticum aestivum, Triticum durum x Haynaldia villosa
Adv. Exp. Med. Biol.
362
241-254
1995
-
-
-
-
-
-
2
-
1
-
19
19
-
19
-
-
-
-
-
23
-
-
40
5
-
-
-
-
22
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
19
19
-
-
-
-
-
23
-
-
40
5
-
-
-
-
22
-
-
-
-
-
-
-
-
-
30845
Asakura
Rice aspartic proteinase, oryz ...
Oryza sativa
Eur. J. Biochem.
232
77-83
1995
-
-
1
-
-
-
-
-
-
-
-
-
-
11
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30847
Guruprasad
Comparative modelling of barle ...
Hordeum vulgare
FEBS Lett.
352
131-136
1994
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
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-
-
-
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-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30848
Runeberg-Roos
The aspartic proteinase is a v ...
Hordeum vulgare
Plant Physiol.
105
321-329
1994
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
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-
-
3
-
-
1
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-
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1
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3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30851
Törmäkangas
-
Tissue-specific localization o ...
Hordeum vulgare
Planta
195
116-125
1994
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
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-
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-
-
-
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-
-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30853
Galleschi
-
Purification, characterization ...
Triticum aestivum
Plant Sci.
98
15-24
1994
-
-
-
-
-
-
1
1
-
-
2
-
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
30843
Kervinen
Hydrolytic specifity of barley ...
Hordeum vulgare
Phytochemistry
32
799-803
1993
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
3
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30850
Sarkkinen
Aspartic proteinase from barle ...
Hordeum vulgare
Planta
186
317-323
1992
-
-
-
-
-
-
4
-
-
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4
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1
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1
1
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1
1
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4
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4
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1
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1
1
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1
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30846
Runeberg-Roos
Primary structure of a barley- ...
Hordeum vulgare
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1021-1027
1991
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1
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30852
Galleschi
-
A rapid and sensitive method o ...
Triticum aestivum, Triticum durum x Haynaldia villosa
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793-797
1990
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