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2,4-dinitrophenyl-ADKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-APKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-ARKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-ATKDSW + H2O
?
-
-
?
2,4-dinitrophenyl-ATKLSTSW + H2O
?
-
-
?
2,4-dinitrophenyl-ATKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-ATKRSW + H2O
?
-
-
?
2,4-dinitrophenyl-DADKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-DATKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-Ser-Thr-Ala-Thr-Lys-Leu-Ser-Trp + H2O
?
2,4-dinitrophenyl-STATKLSW + H2O
?
-
-
?
Azoalbumin + H2O
?
-
-
-
-
-
Bovine insulin B-chain + H2O
?
Bovine serum albumin + H2O
?
Carboxymethylated aspartate aminotransferase + H2O
?
-
from pig heart muscle, cleavage at 12 of 19 Lys and 3 of 26 Arg
-
-
-
Congo red elastin + H2O
?
-
-
-
-
-
Equine heart cytochrome c + H2O
?
Glucagon + H2O
?
-
cleavage site: Ser11-Lys12, 2 products
-
-
-
Lysozyme + H2O
?
-
-
-
-
-
Melittin + H2O
?
-
i.e. bee venom peptide, native or formylated, cleaves at Lys7, Lys21 and Lys23 residues or formyl-Lys residues
-
-
-
Oxidized ribonuclease A + H2O
?
-
cleavage sites: -Xaa-Lys-, multiple products
-
-
-
Polylysine + H2O
?
-
best substrate
-
-
-
protamine sulfate + H2O
?
S-Carboxymethyl lysozyme + H2O
?
-
cleavage sites: -Xaa-Lys-, multiple products
-
-
-
S-Carboxymethyl pepsinogen + H2O
?
-
cleavage sites: -Xaa-Lys-, 9 peptide products
-
-
-
additional information
?
-
2,4-dinitrophenyl-Ser-Thr-Ala-Thr-Lys-Leu-Ser-Trp + H2O

?
fluorescent peptide substrate
-
?
2,4-dinitrophenyl-Ser-Thr-Ala-Thr-Lys-Leu-Ser-Trp + H2O
?
fluorescent peptide substrate
-
?
azocasein + H2O

?
-
-
-
-
-
azocasein + H2O
?
-
-
-
-
-
Azocoll + H2O

?
-
general protease substrate
-
-
-
Azocoll + H2O
?
-
general protease substrate
-
-
-
Azocoll + H2O
?
-
general protease substrate
-
-
-
Azocoll + H2O
?
-
general protease substrate
-
-
-
Bovine insulin B-chain + H2O

?
-
cleavage site: Pro29-Lys30, yielding 2 fragments: dipeptide Lys-Ala and substrate devoid of 2 C-terminal amino acids
-
-
-
Bovine insulin B-chain + H2O
?
-
cleaves only at Pro-Lys bond of oxidized insulin B-chain
-
-
-
Bovine serum albumin + H2O

?
-
-
-
-
-
Bovine serum albumin + H2O
?
-
-
-
-
-
Bovine serum albumin + H2O
?
-
-
-
-
-
Equine heart cytochrome c + H2O

?
-
cleaves-X-Lys bonds
-
-
-
Equine heart cytochrome c + H2O
?
-
-
-
-
-
Equine heart cytochrome c + H2O
?
-
-
-
-
-
Penicillopepsin + H2O

?
-
cleaves on N-terminal side of Lys residues, yielding peptides of 144, 125, 110, 63, 20 and 16 amino acid residues
-
-
-
Penicillopepsin + H2O
?
-
cleaves on N-terminal side of Lys residues, yielding peptides of 144, 125, 110, 63, 20 and 16 amino acid residues
-
-
-
Polyarginine + H2O

?
-
-
-
-
-
Polyarginine + H2O
?
-
-
-
-
-
protamine sulfate + H2O

?
-
-
-
-
-
protamine sulfate + H2O
?
-
-
-
-
-
Vasopressin + H2O

?
-
lysine-vasopressin
-
-
-
Vasopressin + H2O
?
-
native and oxidized form, cleavage site: Pro7-Lys8, 2 product peptides
-
-
-
Vasopressin + H2O
?
-
i.e. Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Lys-Gly
-
-
-
additional information

?
-
-
major peptide bond specificity of Armillaria mellea enzyme towards bonds where Lys residue contributes an alpha-amino group
-
-
-
additional information
?
-
-
specific cleavage of acyl-Lys bonds (-X-Lys-) in polypeptides
-
-
-
additional information
?
-
peptides with aspartic acid adjacent to the Lys residue are poor substrates, 2,4-dinitrophenyl-Thr-Lys-Trp and peptides with substitution of L-Arg, L-ornithine, or D-Lys are no substrates
-
?
additional information
?
-
peptides with aspartic acid adjacent to the Lys residue are poor substrates, 2,4-dinitrophenyl-Thr-Lys-Trp and peptides with substitution of L-Arg, L-ornithine, or D-Lys are no substrates
-
?
additional information
?
-
-
similar specificity is shown by Myxobacter sp. AL-1 proteinase II
-
-
-
additional information
?
-
-
similar specificity is shown by Myxobacter sp. AL-1 proteinase II
-
-
-
additional information
?
-
-
no cell-wall lytic activity
-
-
-
additional information
?
-
-
No substrates are Lys-Lys, Lys-Lys-Lys
-
-
-
additional information
?
-
-
No substrates are Gly-DL-Leu, Gly-DL-Val, Gly-DL-Ser, Gly-DL-Phe, Gly-DL-ethionine, Gly-DL-Nor, Gly-L-Tyr, L-Leu-L-Tyr, D-Leu-Gly, L-Leu-L-Leu, DL-Leu-DL-Ala, DL-Leu-DL-Ile, DL-Leu-Gly, D-Leu-L-Tyr, D-Leu-Gly-Gly, N-benzyloxycarbonyl-L-Leu-Gly-Gly, Gly-Gly-Gly, N-benzyloxycarbonyl-Gly-L-Phe, N-benzyloxycarbonyl-L-Ala-L-Leu amide, N-benzyloxycarbonyl-Gly-Gly 4-nitrophenyl ester, N-benzyloxycarbonyl-L-Pro-Gly-Gly-Met, N-benzyloxycarbonyl-L-Ala-Gly methyl ester, Pro-Phe-Pro-Gly, polyproline, polyglycine, poly-D-lysine, Ala-Pro-Lys, Ala-Pro-Ala-Asp-Gly-Leu-Lys
-
-
-
additional information
?
-
-
similar specificity is shown by Myxobacter sp. AL-1 proteinase II
-
-
-
additional information
?
-
-
no cell-wall lytic activity
-
-
-
additional information
?
-
-
No substrates are Lys-Lys, Lys-Lys-Lys
-
-
-
additional information
?
-
-
similar specificity is shown by Myxobacter sp. AL-1 proteinase II
-
-
-
additional information
?
-
-
No substrates are Gly-DL-Leu, Gly-DL-Val, Gly-DL-Ser, Gly-DL-Phe, Gly-DL-ethionine, Gly-DL-Nor, Gly-L-Tyr, L-Leu-L-Tyr, D-Leu-Gly, L-Leu-L-Leu, DL-Leu-DL-Ala, DL-Leu-DL-Ile, DL-Leu-Gly, D-Leu-L-Tyr, D-Leu-Gly-Gly, N-benzyloxycarbonyl-L-Leu-Gly-Gly, Gly-Gly-Gly, N-benzyloxycarbonyl-Gly-L-Phe, N-benzyloxycarbonyl-L-Ala-L-Leu amide, N-benzyloxycarbonyl-Gly-Gly 4-nitrophenyl ester, N-benzyloxycarbonyl-L-Pro-Gly-Gly-Met, N-benzyloxycarbonyl-L-Ala-Gly methyl ester, Pro-Phe-Pro-Gly, polyproline, polyglycine, poly-D-lysine, Ala-Pro-Lys, Ala-Pro-Ala-Asp-Gly-Leu-Lys
-
-
-
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2,4-dinitrophenyl-Ala-Thr-D-lysine-Leu-Ser-Try
-
6-aminohexanoic acid
-
caseinolytic activity
agmatine
-
caseinolytic activity
Ba2+
-
1 mM, weak, caseinolytic activity
Ca2+
-
1 mM, weak, caseinolytic activity
Co2+
-
0.1 mM, caseinolytic activity
DL-homoarginine
-
caseinolytic activity
Guanidine-HCl
-
2 M and above, not at 1 M
L-aminobutyric acid
-
caseinolytic activity
L-Lysine ethylester
-
caseinolytic activity
S-2-aminoethylcysteine
-
-
SDS
-
0.1% and above, not at 0.01%
Sodium citrate
-
0.1 M, not 0.01 M
tosyl-Lys chloromethyl ketone
tosyl-Phe chloromethyl ketone
-
weak, caseinolytic activity
1,10-phenanthroline

-
-
1,10-phenanthroline
-
strong, caseinolytic activity
2,2'-bipyridine

-
-
2,2'-bipyridine
-
strong, caseinolytic activity
2,2'-bipyridine
-
1 mM, weak
2-mercaptoethanol

-
weak, caseinolytic activity
antipain

-
weak, caseinolytic activity
Cu2+

-
1 mM, caseinolytic activity
Cu2+
-
1 mM, caseinolytic activity; strong
dithiothreitol

-
caseinolytic activity; strong
dithiothreitol
-
caseinolytic activity; weak
EDTA

-
fully restorable by Ca2+; fully restorable by Zn2+, Mn2+, Co2+; strong, caseinolytic activity
EDTA
-
50 mM, weak at 1 mM; fully restorable by Zn2+, Mn2+, Co2+
Hg2+

-
strong, caseinolytic activity
Hg2+
-
1 mM; strong, caseinolytic activity
L-arginine

-
weak
L-arginine
-
caseinolytic activity
L-lysine

-
-
L-lysine
-
caseinolytic activity
L-ornithine

-
weak
L-ornithine
-
caseinolytic activity
Mg2+

-
1 mM, weak, caseinolytic activity
N-ethylmaleimide

-
weak, caseinolytic activity
p-chloromercuribenzoate

-
not
p-chloromercuribenzoate
-
weak, caseinolytic activity
phosphoramidon

-
weak, caseinolytic activity
tosyl-Lys chloromethyl ketone

-
not
tosyl-Lys chloromethyl ketone
-
weak, caseinolytic
additional information

-
no inhibition (of caseinolytic activity) by chymostatin, iodoacetate, leupeptin; PMSF; zinc acetate, elastatinal, Lys-Lys, 4 M urea
-
additional information
-
L-cysteine; no inhibition (of caseinolytic activity) by chymostatin, iodoacetate, leupeptin; PMSF
-
additional information
-
MnCl2 or soybean trypsin inhibitor; PMSF
-
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PLMP_PLEOS
168
17925
Swiss-Prot
PLMP_ARMME
351
37551
Swiss-Prot
PLMP_GRIFR
348
36879
Swiss-Prot
A0A0B7F5Y0_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
351
36905
TrEMBL
A0A0S2FPI6_9GAMM
368
39222
TrEMBL
W0A2V7_AERHY
345
37255
TrEMBL
B1KKF9_SHEWM
Shewanella woodyi (strain ATCC 51908 / MS32)
360
39052
TrEMBL
M5BKV9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
194
20512
TrEMBL
M5C0W7_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
378
40572
TrEMBL
M5BLL1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
351
36893
TrEMBL
A3QCB5_SHELP
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
361
38907
TrEMBL
M5BLI1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
88
9512
TrEMBL
M5CHA1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
38410
TrEMBL
A0A0B7FYY2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
348
37157
TrEMBL
M5C4B3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
160
17228
TrEMBL
A0A0B7FZL9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
360
37850
TrEMBL
M5CCD9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
331
34916
TrEMBL
G8S6Y6_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
370
38429
TrEMBL
A0A0B7FYY1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
394
43795
TrEMBL
M5CDQ5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
169
17863
TrEMBL
A0A0B7F3S8_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
351
37263
TrEMBL
M5BPK4_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
161
17267
TrEMBL
A0A0S2G235_9GAMM
372
39039
TrEMBL
A0A0B7F1B4_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
350
36849
TrEMBL
A0A0B7F0Q3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
353
37174
TrEMBL
M5CC50_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
167
18262
TrEMBL
M5C022_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
238
25333
TrEMBL
A0A0S2F9T5_9GAMM
369
38973
TrEMBL
A0A0B7FX68_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
348
37162
TrEMBL
M5CA23_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
119
12700
TrEMBL
V5NF71_LEUGO
348
37507
TrEMBL
A0A0B7F2U4_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
37565
TrEMBL
A0A0B7FQI5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
357
37819
TrEMBL
M5C4U2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
359
38012
TrEMBL
A0A0B7FPR2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
357
37816
TrEMBL
A0A0S2G887_9GAMM
367
38860
TrEMBL
A0A0S2FQJ9_9GAMM
366
38225
TrEMBL
A0A0B7FU75_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
353
36990
TrEMBL
M5CBZ1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
38123
TrEMBL
V5ND37_LEUGO
348
37207
TrEMBL
H8FGJ2_XANCI
176
19012
TrEMBL
A0A0B4LCF0_9BURK
363
37971
TrEMBL
A0A0S2F9W9_9GAMM
357
37611
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Doonan, S.; Doonan, H.J.; Hanford, R.; Vernon, C.A.; Walker, J.M.; Da S.Airoldi, L.P.; Bossa, F.; Barra, D.; Carloni, M.; Fasella, P.; Riva, F.
The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues
Biochem. J.
149
497-506
1975
Armillaria mellea
brenda
Lewis, W.G.; Basford, J.M.; Wlatoon, P.L.
Specificity and inhibition studies of Armillaria mellea protease
Biochim. Biophys. Acta
522
551-560
1978
Armillaria mellea
brenda
Barry, F.P.; Doonan, S.; Ross, C.A.
Cleavage by trypsin and by the proteinase from Armillaria mellea at epsilon-N-formyl-lysine residues
Biochem. J.
193
737-742
1981
Armillaria mellea
brenda
Nonaka, T.; Ishikawa, H.; Tsumuraya, Y.; Hashimoto, Y.; Dohmae, N.; Takio, K.
Characterization of a thermostable lysine-specific metalloendopeptidase from the fruiting bodies of a basidiomycete, Grifola frondosa
J. Biochem.
118
1014-1020
1995
Grifola frondosa
brenda
Dohmae, N.; Hayashi, K.; Miki, K.; Tsumuraya, Y.; Hashimoto, Y.
Purification and characterization of intracellular proteinases in Pleurotus ostreatus fruiting bodies
Biosci. Biotechnol. Biochem.
59
2074-2080
1995
Pleurotus ostreatus
brenda
Wingard, M.; Matsueda, G.; Wolfe, R.S.
Myxobacter AL-1 protease II: specific peptide bond cleavage on the amino side of lysine
J. Bacteriol.
112
940-949
1972
unidentified myxobacterium, unidentified myxobacterium AL-1
brenda
Cunningham, A.; Wang, H.M.; Jones, S.R.; Kurosky, A.; Rao, L.; Harris, I.; Rhee, S.H.; Hofmann, T.
Amino acid sequence of penicillopepsin. IV. Myxobacter AL-1 protease II and Staphylococcus aureus protease fragments and homology with pig pepsin and chymosin
Can. J. Biochem.
54
902-914
1976
unidentified myxobacterium, unidentified myxobacterium AL-1
brenda
Hori, T.; Kumasaka, T.; Yamamoto, M.; Nonaka, T.; Tanaka, N.; Hashimoto, Y.; Ueki, T.; Takio, K.
Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa: implications for the catalytic mechanism and substrate specificity based on several different crystal forms
Acta Crystallogr. Sect. D
D57
361-368
2001
Grifola frondosa
brenda
Nonaka, T.; Hashimoto, Y.; Takio, K.
Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies
J. Biochem.
124
157-162
1998
Grifola frondosa, Grifola frondosa (P81054), Pleurotus ostreatus (P81055), Pleurotus ostreatus
brenda
Rao, K.C.; Carruth, R.T.; Miyagi, M.
Proteolytic 18O labeling by peptidyl-Lys metalloendopeptidase for comparative proteomics
J. Proteome Res.
4
507-514
2005
Grifola frondosa
brenda
Rao, K.C.; Palamalai, V.; Dunlevy, J.R.; Miyagi, M.
Peptidyl-Lys metalloendopeptidase-catalyzed 18O labeling for comparative proteomics: application to cytokine/lipolysaccharide-treated human retinal pigment epithelium cell line
Mol. Cell. Proteomics
4
1550-1557
2005
Grifola frondosa
brenda
Coussot, G.; Hawke, D.H.; Mularz, A.; Koomen, J.M.; Kobayashi, R.
A method for the isolation of blocked N-terminal peptides
Anal. Biochem.
361
302-304
2007
Bos taurus
brenda
Kishimoto, T.; Kondo, J.; Takai-Igarashi, T.; Tanaka, H.
Accurate mass comparison coupled with two endopeptidases enables identification of protein termini
Proteomics
11
485-489
2011
Grifola frondosa
brenda