HOME
login
history
all enzymes
BRENDA home
History
Information on EC 3.4.24.20 - peptidyl-Lys metalloendopeptidase
for references in articles please use BRENDA:EC3.4.24.20Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.24.20 peptidyl-Lys metalloendopeptidaseSpecify your search results
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
Armillaria mellea neutral proteinase, aspzincin metalloendopeptidase, EC 3.4.99.30, EC 3.4.99.32, GFMEP, Lys-N, MEP, peptidyl-Lys metalloendopeptidase, Peptidyllysine metalloproteinase, POMEP, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Armillaria mellea neutral proteinase
-
-
-
-
EC 3.4.99.30
-
-
formerly
-
EC 3.4.99.32
-
-
formerly
-
GFMEP
MEP
-
-
-
-
Peptidyllysine metalloproteinase
-
-
-
-
POMEP
Proteinase, peptidyllysine metallo-
-
-
-
-
GFMEP
-
-
-
-
POMEP
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage in proteins: -Xaa-/-Lys- (in which Xaa may be Pro)
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
65979-41-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Carboxymethylated aspartate aminotransferase + H2O
?
-
from pig heart muscle, cleavage at 12 of 19 Lys and 3 of 26 Arg
-
-
-
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
-
-
-
S-Carboxymethyl lysozyme + H2O
?
-
cleavage sites: -Xaa-Lys-, multiple products
-
-
-
S-Carboxymethyl pepsinogen + H2O
?
-
cleavage sites: -Xaa-Lys-, 9 peptide products
-
-
-
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
-
?
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
-
-
-
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
-
-
-
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 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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Zinc
Zn2+
Zinc
-
atomic absorption spectroscopy; requirement, 1 atom per molecule of native enzyme; Zn2+ activates zinc-depleted apoenzyme
Zinc
-
atomic absorption spectroscopy; requirement, 1 atom per molecule of native enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
fully restorable by Ca2+; fully restorable by Zn2+, Mn2+, Co2+; strong, caseinolytic activity
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
8.5
rather active with fluorogenic peptide substrates than at pH 5.0
9.5
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 9.3
-
about half-maximal activity at pH 4.8 and 9.3, azocoll as substrate
5.5 - 10
-
about half-maximal activity at pH 5.5 and 10, azocoll as substrate
6 - 10.5
6 - 10.5
exhibits more than 50% of the maximal activity over this range
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A0B7FQI5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
357
0
37819
TrEMBL
M5BLL1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
351
0
36893
TrEMBL
A0A0B7FYY1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
394
1
43795
TrEMBL
A0A0B7F5Y0_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
351
0
36905
TrEMBL
A0A0B7F3S8_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
351
0
37263
TrEMBL
M5CDQ5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
169
0
17863
TrEMBL
M5CA23_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
119
0
12700
TrEMBL
M5C0W7_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
378
0
40572
TrEMBL
M5C4U2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
359
0
38012
TrEMBL
B1KKF9_SHEWM
Shewanella woodyi (strain ATCC 51908 / MS32)
360
0
39052
TrEMBL
A0A0B7F2U4_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
0
37565
TrEMBL
M5BWC6_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
0
37539
TrEMBL
M5CBZ1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
0
38123
TrEMBL
M5CHA1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
352
0
38410
TrEMBL
M5C022_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
238
0
25333
TrEMBL
M5BLI1_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
88
0
9512
TrEMBL
A0A0B7F0Q3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
353
0
37174
TrEMBL
M5BKV9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
194
0
20512
TrEMBL
A0A0B7FYY2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
348
0
37157
TrEMBL
M5CC50_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
167
0
18262
TrEMBL
A0A0B7FPR2_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
357
0
37816
TrEMBL
H8FGJ2_XANCI
176
0
19012
TrEMBL
M5CCD9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
331
0
34916
TrEMBL
M5BPK4_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
161
0
17267
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16600
-
Myxobacter sp. AL-1, minimal MW deduced from amino acid composition
16650
-
Armillaria mellea, most probable MW deduced from amino acid composition
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
solved in 4 crystal forms, triclinic space group P1, unit cell parameters a : 30.8 A, b : 40.5 A, c : 30.5 A, monoclinic space group C2, unit cell parameters a : 43.6 A, b : 41.9 A, c : 76.9 A, tetragonal space group P4(3), unit cell parameters a : b : 30.2 A, c : 308.0 A, and hexangonal P6(5)22, unit cell parameters a : b 58.7 A, c : 145.2 A, hanging-drop vapour-diffusion method
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
-
3 h, stable at 70°C and below, 40% loss of activity at 80°C, inactivation within 30 min at 100°C
31047
9
-
3 h, about 30%, 55% and 90% loss of activity at 50°C, 60°C and 70°C, respectively
31047
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
70
80
-
3 h, 40% loss of activity at pH 7.2, 30 min, about 90% loss of activity with Mn2+ instead of zinc
70
-
3 h, about 40% loss of activity with Mn2+ instead of zinc; 3 h, about 90% loss of activity at pH 9; and below, 3 h stable at pH 7.2
70
-
2 h, inactivation; 30 min, about 50% loss of activity in Tris-HCl buffer, pH 7
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Stable to 5 h at 37°C in 0.1 M acetate buffer, pH 5, containing 2 M urea, 1 M guanidine-HCl or 0.01% SDS, inactivation at higher concentrations of urea, guanidine-HCl or SDS
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
molecular biology
-
proteolytic 18O labeling method employing enzyme for use in comparative proteomics. Enzyme incorporates only a single 18O atom into the carboxyl terminus of each proteolytically generated peptide. Method provides accurate quantification results for isotopically labeled peptides
molecular biology
-
biological application for enzyme-based proteolytic 18O labeling method characterizing the proteome changes of cytokine/lipolysaccharide-treated versus untreated human retinal pigment epithelium cell line
molecular biology
-
a method for detecting protein termini on both the amino and the carboxyl side, regardless of terminal modifications, such as N-acetylation is established. This method requires LC-MS/MS combined with two endopeptidases (lysyl endopeptidase) Lys-C and peptidyl-Lys metalloendopeptidase (Lys-N)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.4.24.20)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
