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2,4-dinitrophenyl-ADKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-APKLSW + H2O
2,4-dinitrophenyl-Ala-Pro + KLSW
-
-
-
?
2,4-dinitrophenyl-APKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-ARKLSW + H2O
2,4-dinitrophenyl-Ala-Arg + KLSW
-
-
-
?
2,4-dinitrophenyl-ARKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-ATKDSW + H2O
2,4-dinitrophenyl-Ala-Thr + KDSW
-
-
-
?
2,4-dinitrophenyl-ATKDSW + H2O
?
-
-
?
2,4-dinitrophenyl-ATKLSTSW + H2O
2,4-dinitrophenyl-Ala-Thr + KLSTSW
-
-
-
?
2,4-dinitrophenyl-ATKLSTSW + H2O
?
-
-
?
2,4-dinitrophenyl-ATKLSW + H2O
2,4-dinitrophenyl-Ala-Thr + KLSW
-
-
-
?
2,4-dinitrophenyl-ATKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-ATKRSW + H2O
2,4-dinitrophenyl-Ala-Thr + KRSW
-
-
-
?
2,4-dinitrophenyl-ATKRSW + H2O
?
-
-
?
2,4-dinitrophenyl-DADKLSW + H2O
2,4-dinitrophenyl-DAD + KLSW
-
-
-
?
2,4-dinitrophenyl-DADKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-DATKLSW + H2O
2,4-dinitrophenyl-DAT + KLSW
-
-
-
?
2,4-dinitrophenyl-DATKLSW + H2O
?
-
-
?
2,4-dinitrophenyl-Ser-Thr-Ala-Thr-Lys-Leu-Ser-Trp + H2O
?
2,4-dinitrophenyl-STATKLSW + H2O
2,4-dinitrophenyl-STAT + KLSW
-
-
-
?
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
-
-
?
K(2-aminobenzamide)MRFKRRRK(N-2,4-dinitrophenyl) + H2O
?
best substrate. LysN exhibits strict specificity for lysine in S1', and has less specificity moving further away from the scissile bond. Additivity between the subsites is observed. Based on a homology structure model, the reference substrate is fitted into the active site using molecular dynamics to propose peptide-enzyme interactions
-
-
?
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
-
-
?
SAQKFVS + H2O
SAQ + KFVS
-
-
-
?
SAQKIVS + H2O
SAQ + KIVS
-
-
-
?
SAQKLVS + H2O
SAQ + KLVS
-
-
-
?
SAQKMFS + H2O
SAQ + KMFS
-
-
-
?
SAQKMIS + H2O
SAQ + KMIS
-
-
-
?
SAQKMLS + H2O
SAQ + KMLS
-
-
-
?
SAQKMNS + H2O
SAQ + KMNS
-
-
-
?
SAQKMRS + H2O
SAQ + KMRS
-
-
-
?
SAQKMRVR + H2O
SAQ + KMRVR
-
-
-
?
SAQKMRVS + H2O
SAQ + KMRVS
-
-
-
?
SAQKMSS + H2O
SAQ + KMSS
-
-
-
?
SAQKMVF + H2O
SAQ + KMVF
-
-
-
?
SAQKMVL + H2O
SAQ + KMVL
-
-
-
?
SAQKMVR + H2O
SAQ + KMVR
-
-
-
?
SAQKMVS + H2O
SAQ + KMVS
-
-
-
?
SAQKMVV + H2O
SAQ + KMVV
-
-
-
?
SAQKNVS + H2O
SAQ + KNVS
-
-
-
?
SAQKRVS + H2O
SAQ + KRVS
-
-
-
?
SAQKSVS + H2O
SAQ + KSVS
-
-
-
?
SAQKVVS + H2O
SAQ + KVVS
-
-
-
?
SFQKMVS + H2O
SFQ + KMVS
-
-
-
?
SLQKMVS + H2O
SLQ + KMVS
-
-
-
?
SMQKMVS + H2O
SMQ + KMVS
-
-
-
?
SNQKMVS + H2O
SNQ + KMVS
-
-
-
?
SSQKMVS + H2O
SSQ + KMVS
-
-
-
?
SVQKMVS + H2O
SVQ + KMVS
-
-
-
?
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
?
-
substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
substrate specificity profiling of peptidyl-Lys metallopeptidase of Armillaria mellea by FRET based peptide library
-
-
?
additional information
?
-
-
substrate specificity profiling of peptidyl-Lys metallopeptidase of Armillaria mellea by FRET based peptide library
-
-
?
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
?
-
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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malfunction
mutants with extended S1' binding pocket show specificity towards arginine in subsites S2'-S4' compared to the wild-type protease resulting from the additional negative charge which attract and interact with positively charged residues better than the wild-type. The strict lysine specificity at P1' is preserved in the recombinant rAm-LysN. Relative specificity of site-directed mutants in the substrate binding sites of rAm-LysN compared to the wild-type enzyme with the reference peptide SAQKMVS, overview
physiological function
peptidyl-Lys metallopeptidase (LysN) from Armillaria mellea is an aspzincin metalloprotease, which cleaves in front of lysines
additional information
identification of catalytic residues (Y85, E120, H123, T130, D132, Y135, G136, and D156) and mechanism of work, overview. The S1' binding pocket of LysN is quite narrow and lined with negative charge to specifically accommodate lysine. Residues M65, D83, V88, A101, T105, Q131, Q137, and E159 are involved in substrate specificity. Homology model of Am-LysN based on the crystal structure of Gf-LysN, molecular dynamic simulations, proposed subsite interaction, structure-function analysis, overview
additional information
-
identification of catalytic residues (Y85, E120, H123, T130, D132, Y135, G136, and D156) and mechanism of work, overview. The S1' binding pocket of LysN is quite narrow and lined with negative charge to specifically accommodate lysine. Residues M65, D83, V88, A101, T105, Q131, Q137, and E159 are involved in substrate specificity. Homology model of Am-LysN based on the crystal structure of Gf-LysN, molecular dynamic simulations, proposed subsite interaction, structure-function analysis, overview
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PLMP_ARMME
351
0
37551
Swiss-Prot
Secretory Pathway (Reliability: 1)
PLMP_GRIFR
348
0
36879
Swiss-Prot
Secretory Pathway (Reliability: 1)
PLMP_PLEOS
168
0
17925
Swiss-Prot
Mitochondrion (Reliability: 4)
A0A7W6L1C6_XANCA
365
0
38431
TrEMBL
-
A0A2S7BKQ3_9XANT
365
0
38483
TrEMBL
-
M5BKV9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
194
0
20512
TrEMBL
Mitochondrion (Reliability: 3)
M5BLI1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
88
0
9512
TrEMBL
other Location (Reliability: 4)
A0A0B7FYY2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
348
0
37157
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7W9K230_9XANT
364
1
38728
TrEMBL
-
A0A0S2FPI6_9GAMM
368
1
39222
TrEMBL
-
A0A7W5FW53_9BURK
354
1
37819
TrEMBL
-
A0A0S2G887_9GAMM
367
1
38860
TrEMBL
-
M5C4B3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
160
0
17228
TrEMBL
Secretory Pathway (Reliability: 1)
M5CDQ5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
169
0
17863
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0S2FQJ9_9GAMM
366
0
38225
TrEMBL
-
A0A7Y9U7R8_9BURK
351
0
37159
TrEMBL
-
A0A7X0CFH9_9BURK
351
0
37418
TrEMBL
-
A0A840S4E3_9BURK
344
0
36922
TrEMBL
-
A0A0B7F2U4_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
0
37565
TrEMBL
Secretory Pathway (Reliability: 2)
M5CBZ1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
0
38123
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0B4LCF0_9BURK
363
1
37971
TrEMBL
-
A0A0S2G235_9GAMM
372
1
39039
TrEMBL
-
A0A0B7FPR2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
357
0
37816
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B7F1B4_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
350
0
36849
TrEMBL
Secretory Pathway (Reliability: 2)
M5C4U2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
359
0
38012
TrEMBL
Secretory Pathway (Reliability: 1)
M5CC50_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
167
0
18262
TrEMBL
Mitochondrion (Reliability: 3)
A0A7W9JRX0_9XANT
365
0
38431
TrEMBL
-
A0A7W9BJ93_9RHOB
202
0
22041
TrEMBL
-
M5C0W7_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
378
0
40572
TrEMBL
Secretory Pathway (Reliability: 1)
M5BPK4_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
161
0
17267
TrEMBL
Secretory Pathway (Reliability: 1)
M5CHA1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
0
38410
TrEMBL
Secretory Pathway (Reliability: 2)
M5BLL1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
351
0
36893
TrEMBL
Secretory Pathway (Reliability: 1)
H8FGJ2_XANCI
176
0
19012
TrEMBL
-
V5NF71_LEUGO
348
0
37507
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7X0KR04_9XANT
364
1
38686
TrEMBL
-
A0A7W7MJD9_9ACTN
363
1
37895
TrEMBL
-
A0A0S2F9T5_LYSAN
369
1
38973
TrEMBL
-
M5CCD9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
331
0
34916
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B7FYY1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
394
1
43795
TrEMBL
Secretory Pathway (Reliability: 3)
M5CA23_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
119
0
12700
TrEMBL
Secretory Pathway (Reliability: 2)
A0A840J8I6_9XANT
365
0
38554
TrEMBL
-
A0A0S2F9W9_LYSAN
357
0
37611
TrEMBL
-
A0A840S9F1_9BURK
345
0
37045
TrEMBL
-
A0A0B7F5Y0_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
351
0
36905
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B7F3S8_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
351
0
37263
TrEMBL
Secretory Pathway (Reliability: 1)
W0A2V7_AERHY
345
0
37255
TrEMBL
-
A3QCB5_SHELP
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
361
0
38907
TrEMBL
-
A0A0B7FQI5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
357
0
37819
TrEMBL
Secretory Pathway (Reliability: 1)
G8S6Y6_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
370
1
38429
TrEMBL
-
A0A839F3F5_9GAMM
355
0
37556
TrEMBL
-
A0A0B7FX68_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
348
0
37162
TrEMBL
Secretory Pathway (Reliability: 2)
V5ND37_LEUGO
348
0
37207
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B7FU75_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
353
0
36990
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0B7F0Q3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
353
0
37174
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7W7KTP6_XANEU
365
0
38554
TrEMBL
-
B1KKF9_SHEWM
Shewanella woodyi (strain ATCC 51908 / MS32)
360
0
39052
TrEMBL
-
A0A7R7AEQ6_9GAMM
Methyloprofundus sp
895
0
97739
TrEMBL
-
M5BWC6_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
0
37539
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7Y9SMC7_9XANT
363
0
38844
TrEMBL
-
A0A7W9QL71_9XANT
364
1
38728
TrEMBL
-
A0A0B7FZL9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
360
0
37850
TrEMBL
Secretory Pathway (Reliability: 1)
M5C022_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
238
0
25333
TrEMBL
other Location (Reliability: 2)
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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 (P81054), Grifola frondosa, 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
Oedum, A.S.; Oestergaard, S.; Noerby, I.; Meldal, M.; Olesen, K.
Heterologous expression of peptidyl-Lys metallopeptidase of Armillaria mellea and mutagenic analysis of the recombinant peptidase
J. Biochem.
159
461-470
2016
Armillaria mellea (Q9Y7F7), Armillaria mellea
brenda
Oedum, A.S.; Olesen, K.; Oestergaard, S.; Thim, L.; Noerby, I.; Meldal, M.
Substrate specificity profiling of peptidyl-Lys metallopeptidase of Armillaria mellea by FRET based peptide library
Protein Pept. Lett.
22
514-524
2015
Armillaria mellea (Q9Y7F7), Armillaria mellea
brenda