3.4.24.20: peptidyl-Lys metalloendopeptidase
This is an abbreviated version!
For detailed information about peptidyl-Lys metalloendopeptidase, go to the full flat file.
Word Map on EC 3.4.24.20
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3.4.24.20
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frondosa
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collision
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grifola
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collision-induced
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pleurotus
-
ostreatus
-
b-ions
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molecular biology
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silac
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lysine-specific
-
synthesis
- 3.4.24.20
- frondosa
-
collision
-
grifola
-
collision-induced
-
pleurotus
- ostreatus
-
b-ions
- molecular biology
-
silac
-
lysine-specific
- synthesis
Reaction
Preferential cleavage in proteins: -Xaa-/-Lys- (in which Xaa may be Pro) =
Synonyms
Am-LysN, Armillaria mellea neutral proteinase, aspzincin metalloendopeptidase, aspzincin metalloprotease, EC 3.4.99.30, EC 3.4.99.32, GFMEP, Lys-N, LysN, MEP, peptidyl-Lys metalloendopeptidase, peptidyl-Lys metallopeptidase, Peptidyllysine metalloproteinase, POMEP, Proteinase, peptidyllysine metallo-
ECTree
3.4.24.20 peptidyl-Lys metalloendopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.20 - peptidyl-Lys metalloendopeptidase
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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
2,4-dinitrophenyl-APKLSW + H2O
2,4-dinitrophenyl-Ala-Pro + KLSW
-
-
-
?
2,4-dinitrophenyl-ARKLSW + H2O
2,4-dinitrophenyl-Ala-Arg + KLSW
-
-
-
?
2,4-dinitrophenyl-ATKDSW + H2O
2,4-dinitrophenyl-Ala-Thr + KDSW
-
-
-
?
2,4-dinitrophenyl-ATKLSTSW + H2O
2,4-dinitrophenyl-Ala-Thr + KLSTSW
-
-
-
?
2,4-dinitrophenyl-ATKLSW + H2O
2,4-dinitrophenyl-Ala-Thr + KLSW
-
-
-
?
2,4-dinitrophenyl-ATKRSW + H2O
2,4-dinitrophenyl-Ala-Thr + KRSW
-
-
-
?
2,4-dinitrophenyl-STATKLSW + H2O
2,4-dinitrophenyl-STAT + KLSW
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-
-
?
Carboxymethylated aspartate aminotransferase + H2O
?
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from pig heart muscle, cleavage at 12 of 19 Lys and 3 of 26 Arg
-
-
?
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
-
-
?
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
?
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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
?
-
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major peptide bond specificity of Armillaria mellea enzyme towards bonds where Lys residue contributes an alpha-amino group
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-
?
additional information
?
-
substrate specificity of wild-type and mutant enzymes, overview
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-
?
additional information
?
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substrate specificity of wild-type and mutant enzymes, overview
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-
?
additional information
?
-
substrate specificity profiling of peptidyl-Lys metallopeptidase of Armillaria mellea by FRET based peptide library
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-
?
additional information
?
-
-
substrate specificity profiling of peptidyl-Lys metallopeptidase of Armillaria mellea by FRET based peptide library
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-
?
additional information
?
-
-
specific cleavage of acyl-Lys bonds (-X-Lys-) in polypeptides
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-
?
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
?
-
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similar specificity is shown by Myxobacter sp. AL-1 proteinase II
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-
?
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
?
-
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similar specificity is shown by Myxobacter sp. AL-1 proteinase II
-
-
?
additional information
?
-
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no cell-wall lytic activity
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-
?
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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-
?
