Information on EC 3.4.24.20 - peptidyl-Lys metalloendopeptidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.4.24.20
-
RECOMMENDED NAME
GeneOntology No.
peptidyl-Lys metalloendopeptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Preferential cleavage in proteins: -Xaa-/-Lys- (in which Xaa may be Pro)
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Armillaria mellea neutral proteinase
-
-
-
-
aspzincin metalloendopeptidase
-
-
EC 3.4.99.30
-
-
formerly
-
EC 3.4.99.32
-
-
formerly
-
GFMEP
-
-
-
-
GFMEP
P81054
-
MEP
-
-
-
-
peptidyl-Lys metalloendopeptidase
-
-
Peptidyllysine metalloproteinase
-
-
-
-
POMEP
-
-
-
-
POMEP
P81055
-
Proteinase, peptidyllysine metallo-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
65979-41-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
basidomycete, honey fungus
-
-
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
edible mushroom
-
-
Manually annotated by BRENDA team
edible mushroom
SwissProt
Manually annotated by BRENDA team
i.e. Maitake, var. S.F.Gray
-
-
Manually annotated by BRENDA team
edible mushroom
SwissProt
Manually annotated by BRENDA team
unidentified myxobacterium AL-1
AL-1
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl-ADKLSW + H2O
?
show the reaction diagram
P81054
-
-
?
2,4-dinitrophenyl-APKLSW + H2O
?
show the reaction diagram
P81054
-
-
?
2,4-dinitrophenyl-ARKLSW + H2O
?
show the reaction diagram
P81054
-
-
?
2,4-dinitrophenyl-ATKDSW + H2O
?
show the reaction diagram
P81054
-
-
?
2,4-dinitrophenyl-ATKLSTSW + H2O
?
show the reaction diagram
P81054
-
-
?
2,4-dinitrophenyl-ATKLSW + H2O
?
show the reaction diagram
P81054
-
-
?
2,4-dinitrophenyl-ATKRSW + H2O
?
show the reaction diagram
P81054
-
-
?
2,4-dinitrophenyl-DADKLSW + H2O
?
show the reaction diagram
P81054
-
-
?
2,4-dinitrophenyl-DATKLSW + H2O
?
show the reaction diagram
P81054
-
-
?
2,4-dinitrophenyl-Ser-Thr-Ala-Thr-Lys-Leu-Ser-Trp + H2O
?
show the reaction diagram
P81054
fluorescent peptide substrate
-
?
2,4-dinitrophenyl-Ser-Thr-Ala-Thr-Lys-Leu-Ser-Trp + H2O
?
show the reaction diagram
P81055
fluorescent peptide substrate
-
?
2,4-dinitrophenyl-STATKLSW + H2O
?
show the reaction diagram
P81054
-
-
?
Azoalbumin + H2O
?
show the reaction diagram
-
-
-
-
-
azocasein + H2O
?
show the reaction diagram
-
-
-
-
-
azocasein + H2O
?
show the reaction diagram
-
-
-
-
-
azocasein + H2O
?
show the reaction diagram
P81054
-
-
?
azocasein + H2O
?
show the reaction diagram
P81055
-
-
?
Azocoll + H2O
?
show the reaction diagram
-
general protease substrate
-
-
-
Azocoll + H2O
?
show the reaction diagram
-
general protease substrate
-
-
-
Azocoll + H2O
?
show the reaction diagram
unidentified myxobacterium, unidentified myxobacterium AL-1
-
general protease substrate
-
-
-
Bovine insulin B-chain + H2O
?
show the reaction diagram
-
cleaves only at Pro-Lys bond of oxidized insulin B-chain
-
-
-
Bovine insulin B-chain + H2O
?
show the reaction diagram
-
cleavage site: Pro29-Lys30, yielding 2 fragments: dipeptide Lys-Ala and substrate devoid of 2 C-terminal amino acids
-
-
-
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
-
Bovine serum albumin + H2O
?
show the reaction diagram
unidentified myxobacterium, unidentified myxobacterium AL-1
-
-
-
-
-
Carboxymethylated aspartate aminotransferase + H2O
?
show the reaction diagram
-
from pig heart muscle, cleavage at 12 of 19 Lys and 3 of 26 Arg
-
-
-
Congo red elastin + H2O
?
show the reaction diagram
-
-
-
-
-
Equine heart cytochrome c + H2O
?
show the reaction diagram
-
-
-
-
-
Equine heart cytochrome c + H2O
?
show the reaction diagram
-
-
-
-
-
Equine heart cytochrome c + H2O
?
show the reaction diagram
-
cleaves-X-Lys bonds
-
-
-
Glucagon + H2O
?
show the reaction diagram
-
cleavage site: Ser11-Lys12, 2 products
-
-
-
Lysozyme + H2O
?
show the reaction diagram
-
-
-
-
-
Oxidized ribonuclease A + H2O
?
show the reaction diagram
-
cleavage sites: -Xaa-Lys-, multiple products
-
-
-
Penicillopepsin + H2O
?
show the reaction diagram
unidentified myxobacterium, unidentified myxobacterium AL-1
-
cleaves on N-terminal side of Lys residues, yielding peptides of 144, 125, 110, 63, 20 and 16 amino acid residues
-
-
-
Polyarginine + H2O
?
show the reaction diagram
-
-
-
-
-
Polyarginine + H2O
?
show the reaction diagram
-
-
-
-
-
Polylysine + H2O
?
show the reaction diagram
-
best substrate
-
-
-
protamine sulfate + H2O
?
show the reaction diagram
-
-
-
-
-
protamine sulfate + H2O
?
show the reaction diagram
-
-
-
-
-
S-Carboxymethyl lysozyme + H2O
?
show the reaction diagram
-
cleavage sites: -Xaa-Lys-, multiple products
-
-
-
S-Carboxymethyl pepsinogen + H2O
?
show the reaction diagram
-
cleavage sites: -Xaa-Lys-, 9 peptide products
-
-
-
Vasopressin + H2O
?
show the reaction diagram
-
lysine-vasopressin, native and oxidized form, cleavage site: Pro7-Lys8, 2 product peptides
-
-
-
Vasopressin + H2O
?
show the reaction diagram
-
i.e. Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Lys-Gly
-
-
-
Melittin + H2O
?
show the reaction diagram
-
i.e. bee venom peptide, native or formylated, cleaves at Lys7, Lys21 and Lys23 residues or formyl-Lys residues
-
-
-
additional information
?
-
-
specific cleavage of acyl-Lys bonds (-X-Lys-) in polypeptides
-
-
-
additional information
?
-
-
similar specificity is shown by Myxobacter sp. AL-1 proteinase II
-
-
-
additional information
?
-
-
no cell-wall lytic activity, 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
?
-
-
major peptide bond specificity of Armillaria mellea enzyme towards bonds where Lys residue contributes an alpha-amino group
-
-
-
additional information
?
-
P81054
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
?
-
P81055
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
?
-
unidentified myxobacterium AL-1
-
similar specificity is shown by Myxobacter sp. AL-1 proteinase II, no cell-wall lytic activity, No substrates are Lys-Lys, Lys-Lys-Lys
-
-
-
additional information
?
-
unidentified myxobacterium AL-1
-
similar specificity is shown by Myxobacter sp. AL-1 proteinase II, 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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activation, zinc-depleted apoenzyme
Co2+
-
activation, zinc-depleted apoenzyme
Co2+
P81055
can substitute for Zn2+, enhances activity
Mn2+
-
activation, 0.1 mM, native enzyme and zinc-depleted apoenzyme
Zinc
-
requirement, 1 atom per molecule of native enzyme
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
Zn2+
-
contains 2 zinc ligands
Zn2+
P81054
zinc-metalloendopetidase
Zn2+
P81055
zinc-metalloendopetidase
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
strong, caseinolytic activity
1,10-phenanthroline
-
-
2,2'-Bipyridine
-
-
2,2'-Bipyridine
-
strong, caseinolytic activity
2,2'-Bipyridine
-
1 mM, weak
2,4-dinitrophenyl-Ala-Thr-D-lysine-Leu-Ser-Try
P81054
-
2-mercaptoethanol
-
weak, caseinolytic activity
2-mercaptoethanol
-
not
6-Aminohexanoic acid
-
caseinolytic activity
Ag2+
-
1 mM, strong
agmatine
-
caseinolytic activity
antipain
-
weak, caseinolytic activity
Ba2+
-
1 mM, weak, caseinolytic activity
Ca2+
-
1 mM, weak, caseinolytic activity
Co2+
-
0.1 mM, caseinolytic activity
Cu2+
-
1 mM, caseinolytic activity
Cu2+
-
1 mM, caseinolytic activity; strong
dithiothreitol
-
caseinolytic activity; strong
dithiothreitol
-
caseinolytic activity; weak
DL-Homoarginine
-
caseinolytic activity
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+
Guanidine-HCl
-
2 M and above, not at 1 M
Hg2+
-
strong, caseinolytic activity
Hg2+
-
1 mM; strong, caseinolytic activity
L-aminobutyric acid
-
caseinolytic activity
L-arginine
-
weak
L-arginine
-
caseinolytic activity
L-lysine
-
caseinolytic activity
L-Lysine ethylester
-
caseinolytic activity
L-ornithine
-
weak
L-ornithine
-
caseinolytic activity
Methylamine
-
-
Mg2+
-
1 mM, weak, caseinolytic activity
N-ethylmaleimide
-
weak, caseinolytic activity
N-ethylmaleimide
-
not
n-Propylamine
-
-
p-chloromercuribenzoate
-
not
p-chloromercuribenzoate
-
weak, caseinolytic activity
phosphoramidon
-
weak, caseinolytic activity
phosphoramidon
-
not
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
-
not
tosyl-Lys chloromethyl ketone
-
weak, caseinolytic
tosyl-Phe chloromethyl ketone
-
weak, caseinolytic activity
Urea
-
5 M, not at 2 M
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0116
-
2,4-dinitrophenyl-ADKLSW
P81054
pH 9.5, 37C
0.0111
-
2,4-dinitrophenyl-APKLSW
P81054
pH 9.5, 37C
0.0152
-
2,4-dinitrophenyl-ARKLSW
P81054
pH 9.5, 37C
0.0249
-
2,4-dinitrophenyl-ATKDSW
P81054
pH 9.5, 37C
0.0133
-
2,4-dinitrophenyl-ATKLSTSW
P81054
pH 9.5, 37C
0.0121
-
2,4-dinitrophenyl-ATKLSW
P81054
pH 9.5, 37C
0.0177
-
2,4-dinitrophenyl-ATKRSW
P81054
pH 9.5, 37C
0.0155
-
2,4-dinitrophenyl-DADKLSW
P81054
pH 9.5, 37C
0.0088
-
2,4-dinitrophenyl-DATKLSW
P81054
pH 9.5, 37C
0.0114
-
2,4-dinitrophenyl-STATKLSW
P81054
pH 9.5, 37C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.3
-
2,4-dinitrophenyl-ADKLSW
P81054
pH 9.5, 37C
5.5
-
2,4-dinitrophenyl-APKLSW
P81054
pH 9.5, 37C
54.7
-
2,4-dinitrophenyl-ARKLSW
P81054
pH 9.5, 37C
0.25
-
2,4-dinitrophenyl-ATKDSW
P81054
pH 9.5, 37C
0.99
-
2,4-dinitrophenyl-ATKLSTSW
P81054
pH 9.5, 37C
17.6
-
2,4-dinitrophenyl-ATKLSTSW
P81054
pH 9.5, 37C
3
-
2,4-dinitrophenyl-ATKLSW
P81054
pH 9.5, 37C
3.7
-
2,4-dinitrophenyl-ATKRSW
P81054
pH 9.5, 37C
0.12
-
2,4-dinitrophenyl-DADKLSW
P81054
pH 9.5, 37C
5.1
-
2,4-dinitrophenyl-DATKLSW
P81054
pH 9.5, 37C
21
-
2,4-dinitrophenyl-STATKLSW
P81054
pH 9.5, 37C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0399
-
2,4-dinitrophenyl-Ala-Thr-D-lysine-Leu-Ser-Try
P81054
pH 9.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.6
-
-
azocoll or azocasein as substrate
5.6
-
P81055
azocasein hydrolysis
6.5
7.5
-
broad, azocoll as substrate
8.5
9
-
azocoll as substrate
8.5
-
P81055
rather active with fluorogenic peptide substrates than at pH 5.0
9
-
-
congo red elastin as substrate
9.5
-
-
azocoll or azocasein as substrate
9.5
-
P81054
-
additional information
-
-
pI: 7.46
additional information
-
-
pI: 8.35
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-
more than 50% of maximal activity at pH 6 and 10.5
6
10.5
P81054
exhibits more than 50% of the maximal activity over this range
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
unidentified myxobacterium AL-1
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
unidentified myxobacterium AL-1
-
-
-
-
Manually annotated by BRENDA team
unidentified myxobacterium AL-1
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
14000
-
-
Armillaria mellea, gel filtration
16600
-
-
Myxobacter sp. AL-1, minimal MW deduced from amino acid composition
16650
-
-
Armillaria mellea, most probable MW deduced from amino acid composition
17000
-
-
Myxobacter sp. AL-1, sedimentation velocity experiments
additional information
-
-
amino acid composition
additional information
-
-
amino acid composition
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 20000, Grifola frondosa, SDS-PAGE
monomer
-
1 * 13500, Armillaria mellea, SDS-PAGE
monomer
-
1 * 18000, Pleurotus ostreatus, SDS-PAGE
monomer
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
Myxobacter sp. AL-1
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
11
-
1 h, stable at 37C, azocoll as substrate
4
7
-
18 h stable at 37C, azocoll as substrate
4
9
-
18 h, 10% loss of caseinolytic activity at 4C
5
10
-
18 h, about 20% loss of activity at 4C
7.2
-
-
3 h, stable at 70C and below, 40% loss of activity at 80C, inactivation within 30 min at 100C
9
-
-
3 h, about 30%, 55% and 90% loss of activity at 50C, 60C and 70C, respectively
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
1 h stable at pH 3-11, 18 h stable at pH 4-7
50
-
-
3 h, about 30% loss of activity at pH 9
50
-
-
15 min, 10% loss of caseinolytic activity
50
-
-
18 h stable, about 10% loss of activity after 24 h
60
-
-
3 h, about 55% loss of activity at pH 9
60
-
-
4 h, about 50% loss of activity
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
-
-
15 min, inactivation
70
-
-
2 h, inactivation; 30 min, about 50% loss of activity in Tris-HCl buffer, pH 7
80
-
-
3 h, 40% loss of activity at pH 7.2, 30 min, about 90% loss of activity with Mn2+ instead of zinc
100
-
-
30 min, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Stable to 5 h at 37C 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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-40C, pH 7, at least a year
-
4C, in various buffers, pH 5-10, about 20% loss of activity within 18 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
isolation of blocked N-terminal peptides
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
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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
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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)