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((7-methoxycoumarin-4-yl)acetyl)-Lys-Lys-Pro-Ala-Glu-Phe-Phe-Ala-Leu-Lys-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
Acid denatured bovine hemoglobin + H2O
?
-
-
-
-
?
alpha-casein + H2O
?
-
formation of two cleavage products of about 30 and 23 kDa
-
?
Barley lectin + H2O
?
-
removal of 13 amino acids from the C-terminus
-
-
?
beta-casein + H2O
?
-
formation of one single product of about 23 kDa
-
?
Edestin + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
-
-
-
?
Insulin B-chain + H2O
?
-
-
-
-
?
kappa-casein + H2O
?
-
digestion of kappa-casein results in the appearance of a product of about 16 kDa
-
?
kappa-casein + H2O
para-kappa-casein + ?
-
-
-
?
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu + H2O
?
-
-
-
-
?
L-Pro-L-Thr-L-Glu-L-Phe(p-NO2)-L-Phe-L-Arg-L-Leu + H2O
?
-
-
-
-
?
Leu-Ser-Phe(NO2)-Ahx-Ala-Leu-OMe + H2O
?
Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu + H2O
?
Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe-Phe + Phe(NO2)-Ala-Leu + H2O
-
-
-
?
Lys-Pro-Ile-Glu-(4-nitro)Phe-Arg-Leu + H2O
?
-
-
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
?
Melittin + H2O
?
-
-
-
-
?
Pro-Pro-Thr-Ile-(4-nitro)Phe-Arg-Leu + H2O
?
-
-
-
-
?
skimmed milk + H2O
?
-
-
-
?
additional information
?
-
Albumin + H2O
?
-
-
-
-
?
Albumin + H2O
?
-
-
-
-
?
Albumin + H2O
?
-
-
-
-
?
Albumin + H2O
?
-
-
-
-
?
Albumin + H2O
?
-
-
-
-
?
casein + H2O
?
-
-
-
-
?
Gliadin + H2O
?
-
-
-
-
?
Gliadin + H2O
?
-
gliadin subunits with MW of 66800-9500 and 31000 are processed to fragemnts of 57000-63000 and 24000-26600, respectively
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
Triticum durum x Haynaldia villosa
-
-
-
-
?
Leu-Ser-Phe(NO2)-Ahx-Ala-Leu-OMe + H2O
?
-
-
-
?
Leu-Ser-Phe(NO2)-Ahx-Ala-Leu-OMe + H2O
?
substrate of cardosin B
-
-
?
Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu + H2O
?
substrate of cardosin A
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
?
-
modelling of enzyme-substrate complex
-
-
?
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
may participate in the processing of the C-terminus of barley prolectin
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
contribution to the digestion of trapped insects
-
-
?
Protein + H2O
?
-
hydrolysis of pathogenesis-related proteins
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
hydrolysis of pathogenesis-related proteins
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
-
-
-
-
?
Protein + H2O
?
Triticum durum x Haynaldia villosa
-
-
-
-
?
additional information
?
-
-
preference for phenylalanine, leucine or norleucine at P! site, for tyrosine or phenylalanine at P1Ā site
-
-
?
additional information
?
-
the enzyme shows a preference for accommodating large hydrophobic amino acids at position P1, such as phenylalanine, tyrosine, and leucine. In P1', the enzyme prefers rather small amino acids like valine, alanine, and serine
-
-
?
additional information
?
-
-
no hydrolysis of denatured alpha-hordothionin
-
-
?
additional information
?
-
-
endopeptidase activity, aliphatic or aromatic amino acids at P1 and P1' possible, e.g. Leu, Val, Phe, Thr
-
-
?
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ASPR_HORVU
508
0
54226
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A151SU18_CAJCA
510
0
55457
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5B6Z931_DAVIN
545
0
59333
TrEMBL
Mitochondrion (Reliability: 3)
A0A5B6ZR64_DAVIN
365
2
40030
TrEMBL
other Location (Reliability: 5)
A0A2H9ZVA5_9ASPA
511
0
55161
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0D3MWV2_ARCMI
509
1
55223
TrEMBL
Secretory Pathway (Reliability: 1)
B9S023_RICCO
500
1
55147
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9HBC8_9LAMI
297
0
31858
TrEMBL
other Location (Reliability: 3)
S4TAM1_9GENT
506
1
54394
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B6ZNP1_DAVIN
535
0
58097
TrEMBL
Mitochondrion (Reliability: 5)
A0A5B6Z786_DAVIN
541
0
58842
TrEMBL
Mitochondrion (Reliability: 2)
A0A2I0BFI3_9ASPA
506
1
55120
TrEMBL
Secretory Pathway (Reliability: 3)
A0A151TX99_CAJCA
482
0
52658
TrEMBL
Mitochondrion (Reliability: 2)
H6UWY9_CIRVU
509
1
55073
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B2PY44_GLYSO
508
1
55362
TrEMBL
Secretory Pathway (Reliability: 2)
A0A072VYH6_MEDTR
508
1
55683
TrEMBL
Secretory Pathway (Reliability: 3)
B9SFR8_RICCO
456
1
49694
TrEMBL
Secretory Pathway (Reliability: 1)
S4TA71_FICCA
385
0
41460
TrEMBL
Mitochondrion (Reliability: 5)
A0A5B7BH62_DAVIN
413
0
44991
TrEMBL
Mitochondrion (Reliability: 2)
A0A5B6ZNB4_DAVIN
298
0
31941
TrEMBL
other Location (Reliability: 3)
A0A0B2P617_GLYSO
128
0
14072
TrEMBL
other Location (Reliability: 2)
A0A151RMQ7_CAJCA
119
1
13264
TrEMBL
other Location (Reliability: 2)
A0A2P6Q2H2_ROSCH
518
1
55945
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6QZS1_ROSCH
504
0
55839
TrEMBL
Secretory Pathway (Reliability: 2)
K9MPT9_EIMTE
135
0
13329
TrEMBL
other Location (Reliability: 3)
A0A5B6Z7E0_DAVIN
301
1
33242
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0B2QX92_GLYSO
507
1
56078
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2I0B3W5_9ASPA
292
0
31631
TrEMBL
other Location (Reliability: 3)
A0A2P6R801_ROSCH
508
1
54956
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0B2QWQ7_GLYSO
229
0
25293
TrEMBL
Mitochondrion (Reliability: 3)
A0A2I0B2K9_9ASPA
510
1
55701
TrEMBL
Secretory Pathway (Reliability: 1)
S4TAU0_FICCA
386
0
41803
TrEMBL
Mitochondrion (Reliability: 5)
Q70BT3_PHYPA
504
1
54464
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0B2RVB1_GLYSO
514
0
55671
TrEMBL
Secretory Pathway (Reliability: 1)
K9MN50_EIMTE
175
0
19011
TrEMBL
other Location (Reliability: 2)
B9RXH6_RICCO
511
0
55367
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B6ZPV5_DAVIN
291
1
32609
TrEMBL
Mitochondrion (Reliability: 4)
A0A072V2S8_MEDTR
497
0
55578
TrEMBL
Secretory Pathway (Reliability: 4)
A0A072V4J6_MEDTR
510
1
55075
TrEMBL
Secretory Pathway (Reliability: 1)
B9RFR2_RICCO
494
0
54280
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0B2QD39_GLYSO
496
0
54645
TrEMBL
Mitochondrion (Reliability: 4)
A0A396JBK7_MEDTR
502
0
56273
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6S236_ROSCH
516
0
55384
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B6ZTH8_DAVIN
484
0
52705
TrEMBL
Mitochondrion (Reliability: 5)
A0A0B2P5X3_GLYSO
496
0
54928
TrEMBL
Mitochondrion (Reliability: 5)
S4TA51_9GENT
507
1
55006
TrEMBL
Secretory Pathway (Reliability: 4)
A0A151SSN8_CAJCA
507
0
56374
TrEMBL
Secretory Pathway (Reliability: 3)
A0A151RMJ6_CAJCA
508
1
55563
TrEMBL
Secretory Pathway (Reliability: 1)
W5QMH7_SILMA
509
1
55797
TrEMBL
Secretory Pathway (Reliability: 1)
A0A084G9U0_PSEDA
399
0
43326
TrEMBL
Secretory Pathway (Reliability: 2)
G7KWE8_MEDTR
504
1
55237
TrEMBL
Secretory Pathway (Reliability: 1)
W5QMD3_SILMA
506
1
54989
TrEMBL
Secretory Pathway (Reliability: 1)
G7JJA2_MEDTR
519
1
55932
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B6ZN88_DAVIN
490
1
53340
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6QCL4_ROSCH
514
1
55718
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7CC83_DAVIN
101
0
11138
TrEMBL
Secretory Pathway (Reliability: 5)
A0A0B2SKM8_GLYSO
351
0
38134
TrEMBL
other Location (Reliability: 1)
B7Q6Z1_IXOSC
921
0
102937
TrEMBL
other Location (Reliability: 2)
B9SVA7_RICCO
514
0
55834
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7C5W1_DAVIN
539
0
58638
TrEMBL
Secretory Pathway (Reliability: 1)
K7P8F2_ANACO
514
0
55159
TrEMBL
-
CARDA_CYNCA
504
0
55504
Swiss-Prot
-
CARDB_CYNCA
506
0
54951
Swiss-Prot
-
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11500
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
13300
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
20000
-
ultracentirfugation
26000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
29700
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
31000
x * 31000, and x * 15000, SDS-PAGE
32000
-
1 * 32000 + 1 * 16000 (48-kDa aspartic proteinase, precursor of the 40-k-Da aspartic proteinase), 1 * 29000 + 1 * 11000 (40-k-Da aspartic proteinase), SDS-PAGE
32300
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
34500
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
36000 - 37000
-
ultracentrifugation, gel filtration
36000 - 40000
-
gel filtration
40000
-
2 * 40000, sequence of cDNA
40800
-
gel filtration, cynarase A
43400
-
gel filtration, cynarase B
46000
-
gel filtration, cynarase C
47000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
50000
-
seeds, gel filtration
52600
x * 37000, SDS-PAGE, mature enzyme. x * 52600, calculated for proenzyme
55230
x * 55230, calculated
58000
-
1 * 58000, SDS-PAGE
60000 - 65000
-
gel filtration
66000
Triticum durum x Haynaldia villosa
-
gel filtration
66500
-
1 * 66500, SDS-PAGE
89000
-
leaf, gel filtration
9000
-
1 * 29000 + 1 * 9000, SDS-PAGE
11000
-
1 * 32000 + 1 * 16000 (48-kDa aspartic proteinase, precursor of the 40-k-Da aspartic proteinase), 1 * 29000 + 1 * 11000 (40-k-Da aspartic proteinase), SDS-PAGE
11000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
15000
x * 31000, and x * 15000, SDS-PAGE
15000
x * 34000, and x * 15000, SDS-PAGE
16000
-
1 * 32000 + 1 * 16000 (48-kDa aspartic proteinase, precursor of the 40-k-Da aspartic proteinase), 1 * 29000 + 1 * 11000 (40-k-Da aspartic proteinase), SDS-PAGE
16000
-
1 * 34000 + 1 * 16000, SDS-PAGE
29000
-
1 * 32000 + 1 * 16000 (48-kDa aspartic proteinase, precursor of the 40-k-Da aspartic proteinase), 1 * 29000 + 1 * 11000 (40-k-Da aspartic proteinase), SDS-PAGE
29000
-
1 * 29000 + 1 * 9000, SDS-PAGE
34000
-
1 * 34000 + 1 * 16000, SDS-PAGE
34000
x * 34000, and x * 15000, SDS-PAGE
37000
-
1 * 37000, SDS-PAGE
37000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
37000
x * 37000, SDS-PAGE, mature enzyme. x * 52600, calculated for proenzyme
40000 - 42000
-
gel filtration
40000 - 42000
-
gel filtration
48000
-
calculation from sequence of cDNA
48000
-
2 * 48000, SDS-PAGE
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Kervinen, J.; Sarkkinen, P.; Leena, N.K.; Saarma, M.
Hydrolytic specificity of barley grain aspartic proteinase
Phytochemistry
32
799-803
1993
Hordeum vulgare
brenda
Kervinen, J.; Törmäkangas, K.; Runeberg-Roos, P.; Guruprasad, K.; Blundell, T.; Teeri, T.H.
Structure and possible function of aspartic proteinases in barley and other plants
Adv. Exp. Med. Biol.
362
241-254
1995
Brassica napus, Cannabis sativa, Cucumis sativus, Cucurbita maxima, Cynara cardunculus, Drosera peltata, Fagopyrum esculentum, Hordeum vulgare, Solanum lycopersicum, Nelumbo nucifera, Nepenthes macfarlanei, Nicotiana tabacum, Oryza sativa, Pinus banksiana, Pinus sylvestris, Sorghum bicolor, Theobroma cacao, Triticum aestivum, Triticum durum x Haynaldia villosa
brenda
Asakura, T.; Watanabe, H.; Abe, K.; Arai, S.
Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases
Eur. J. Biochem.
232
77-83
1995
Oryza sativa
brenda
Runeberg-Roos, P.; Törmäkangas, K.; Ķstman, A.
Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D.
Eur. J. Biochem.
202
1021-1027
1991
Hordeum vulgare
brenda
Guruprasad, K.; Törmäkangas, K.; Kervinen, J.; Blundell, T.L.
Comparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity
FEBS Lett.
352
131-136
1994
Hordeum vulgare
brenda
Runeberg-Roos, P.; Kervinen, J.; Kovaleva, V.; Raikhel, N.V.; Gal, S.
The aspartic proteinase is a vacuolar enzyme that processes probarley lectin in vitro
Plant Physiol.
105
321-329
1994
Hordeum vulgare
brenda
Belozersky, M.A.; Sarbakanova, S.T.; Dunaevsky, Y.A.
Aspartic proteinase from wheat seeds: isolation, properties and action on gliadin
Planta
177
321-326
1998
Triticum aestivum
brenda
Sarkkinen, P.; Kalkkinen, N.; Tilgmenn, C.; siuro, J.; Mikola, L.
Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D
Planta
186
317-323
1992
Hordeum vulgare
brenda
Törmäkangas, K.; Kervinen, J.; Ķstman, A.; Teeri, T.
Tissue-specific localization of aspartic proteinase in developing and germinating barley grains
Planta
195
116-125
1994
Hordeum vulgare
-
brenda
Galleschi, L.; Andreoni, U.
A rapid and sensitive method of assaying the purified aspartic proteinase in cereals
Plant Physiol. Biochem.
28
793-797
1990
Triticum aestivum, Triticum durum x Haynaldia villosa
-
brenda
Galleschi, L.; Felicioli, F.
Purification, characterization and activation by anions of an aspartic proteinase isolated from soft wheat
Plant Sci.
98
15-24
1994
Triticum aestivum
-
brenda
Prasad, B.V.L.S.; Suguna, K.
Role of water molecules in the structure and function of aspartic proteinases
Acta Crystallogr. Sect. D
D58
250-259
2002
Hordeum vulgare
brenda
Park, H.; Kusakabe, I.; Sakakibara, Y.; Kobayashi, H.
Autoproteolytic processing of aspartic proteinase from sunflower seeds
Biosci. Biotechnol. Biochem.
65
702-705
2001
Helianthus annuus
brenda
Castanheira, P.; Samyn, B.; Sergeant, K.; Clemente, J.C.; Dunn, B.M.; Pires, E.; Van Beeumen, J.; Faro, C.
Activation, proteolytic processing, and peptide specificity of recombinant cardosin A
J. Biol. Chem.
280
13047-13054
2005
Cynara cardunculus
brenda
Sidrach, L.; Garcia-Canovas, F.; Tudela, J.; Rodriguez-Lopez, J.N.
Purification of cynarases from artichoke (Cynara scolymus L.): enzymatic properties of cynarase A
Phytochemistry
66
41-49
2005
Cynara cardunculus var. scolymus
brenda
Almeida, C.M.; Gomes, D.; Faro, C.; Simoes, I.
Engineering a cardosin B-derived rennet for sheep and goat cheese manufacture
Appl. Microbiol. Biotechnol.
99
269-281
2015
Cynara cardunculus (Q9XFX4), Cynara cardunculus
brenda
Verissimo, P.; Faro, C.; Moir, A.J.; Lin, Y.; Tang, J.; Pires, E.
Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L.
Eur. J. Biochem.
235
762-768
1996
Cynara cardunculus (Q9XFX3), Cynara cardunculus (Q9XFX4), Cynara cardunculus
brenda
Llorente, B.E.; Obregon, W.D.; Aviles, F.X.; Caffini, N.O.; Vairo-Cavalli, S.
Use of artichoke (Cynara scolymus) flower extract as a substitute for bovine rennet in the manufacture of Gouda-type cheese: characterization of aspartic proteases
Food Chem.
159
55-63
2014
Cynara cardunculus var. scolymus
brenda
Frazao, C.; Bento, I.; Costa, J.; Soares, C.M.; Verissimo, P.; Faro, C.; Pires, E.; Cooper, J.; Carrondo, M.A.
Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L.
J. Biol. Chem.
274
27694-27701
1999
Cynara cardunculus (Q9XFX3), Cynara cardunculus
brenda
Raimbault, A.K.; Zuily-Fodil, Y.; Soler, A.; Cruz de Carvalho, M.H.
A novel aspartic acid protease gene from pineapple fruit (Ananas comosus): cloning, characterization and relation to postharvest chilling stress resistance
J. Plant Physiol.
170
1536-1540
2013
Ananas comosus (K7P8F2), Ananas comosus
brenda
Pereira, C.; Pereira, S.; Satiat-Jeunemaitre, B.; Pissarra, J.
Cardosin A contains two vacuolar sorting signals using different vacuolar routes in tobacco epidermal cells
Plant J.
76
87-100
2013
Cynara cardunculus (Q9XFX3)
brenda
Almeida, C.M.; Manso, J.A.; Figueiredo, A.C.; Antunes, L.; Cruz, R.; Manadas, B.; Bur, D.; Pereira, P.J.B.; Faro, C.; Simoes, I.
Functional and structural characterization of synthetic cardosin B-derived rennet
Appl. Microbiol. Biotechnol.
101
6951-6968
2017
Cynara cardunculus (Q9XFX4)
brenda
Wu, H.; Castanheira, P.; Faro, C.; Tang, J.
Cardosin A endocytosis mediated by integrin leads to lysosome leakage and apoptosis of epithelial cells
Proteins
87
502-511
2019
Cynara cardunculus
brenda