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2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
2-aminobenzoyl-Ala-Gly-Leu-Ala-4-nitrobenzylamide + H2O
2-aminobenzoyl-Ala-Gly + Leu-Ala-4-nitrobenzylamide
-
-
-
-
?
2-aminobenzoyl-Ala-Gly-Leu-Ala-4-nitrobenzylamide + H2O
?
25°C, pH 7.4
-
-
?
3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine + H2O
L-phenylalanyl-L-phenylalanine + 3-(2-furyl)acryloyl-glycine
at 37°C, pH 7.3
-
-
?
3-(2-furylacryloyl)glycyl-L-leucine amide + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
?
-
-
-
-
?
AAF-7-amido-4-methylcoumarin + H2O
AAF + 7-amino-4-methylcoumarin
-
-
-
-
?
Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide + H2O
?
-
-
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-L-alanyl-L-alanyl-L-alanine-methyl ester + H2O
?
-
-
-
-
?
Ala-Ala-Ala-Phe-Ala + H2O
?
30°C, pH 8.6
-
-
?
Ala-Ala-Phe-Ala-NH2 + H2O
?
30°C, pH 8.6
-
-
?
alpha1-proteinase inhibitor + H2O
?
25°C, pH 7.4, cleavage occurs at the Pro357-Met358 bond (wild-type and recombinant Met358 inhibitor) and at the Pro357-Leu358 bond (recombinant mutant M358L inhibitor)
-
-
?
benzyloxycarbonyl-Ala-Leu-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Gly + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Leu + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-NH2 + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Phe + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Phe-NH2 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu-Ala + H2O
?
-
-
-
-
?
Boc-GKR-7-amido-4-methylcoumarin + H2O
Boc-GKR + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-QAR-7-amido-4-methylcoumarin + H2O
Boc-QAR + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-VLK-7-amido-4-methylcoumarin + H2O
Boc-VLK + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-VPR-7-amido-4-methylcoumarin + H2O
Boc-VPR + 7-amino-4-methylcoumarin
-
-
-
-
?
BODIPY-casein + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
carbobenzooxydialanine-leucylalaninamide + H2O
?
30°C, pH 8.6
-
-
?
carbobenzooxydialanine-phenylalanylalaninamide + H2O
?
30°C, pH 8.6
-
-
?
carbobenzooxydialanine-tyrosylalaninamide + H2O
?
30°C, pH 8.6
-
-
?
carbobenzoxy-Gly-Leu-NH2 + H2O
?
-
-
-
?
carbobenzoxy-Gly-Phe-NH2 + H2O
?
-
-
-
?
carbobenzoxy-Gly-Tyr-NH2 + H2O
?
cartilage + H2O
?
major components proteoglycans and collagen
-
-
?
Collagen IV + H2O
?
37°C
-
-
?
dabsyl-Ala-Ala-Phe-Ala-EDANS + H2O
?
-
-
-
-
?
Denatured casein + H2O
?
-
-
-
-
?
Denatured fibrin + H2O
?
-
-
-
-
?
Denatured hemoglobin + H2O
?
-
-
-
-
?
Denatured ovalbumin + H2O
?
-
-
-
-
?
eggshell membrane + H2O
Val-Leu-Pro-Pro + (X)-Val-Pro-Pro + Trp + ?
-
-
-
-
?
eggshell-membrane + H2O
?
elastase propeptide + H2O
elastase + ?
elastin Congo red + H2O
?
elastin-agarose + H2O
?
-
-
-
?
elastin-Congo red
?
-
-
-
?
elastin-fluorescein
?
37°C
-
-
?
elastin-orcin + H2O
?
-
-
-
-
?
Fe2-transferrin + H2O
?
25°C, pH 7.4
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
furylacryloyl-Ala-Leu-Ala + H2O
?
pH 8.0, 30°C
-
-
?
furylacryloyl-Ala-Leu-Gly + H2O
?
pH 8.0, 30°C
-
-
?
furylacryloyl-Gly-Leu-Ala + H2O
?
pH 8.0, 30°C
-
-
?
furylacryloyl-Gly-Leu-Gly + H2O
?
pH 8.0, 30°C
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
?
-
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
furylacryloyl-glycyl-L-leucyl-L-alanine + H2O
furylacryloyl-glycine + L-leucyl-L-alanine
Gelatin + H2O
?
-
-
-
-
?
hide powder azure + H2O
?
hog gastric mucin + H2O
?
-
-
-
?
human alpha-1 proteinase inhibitor + H2O
?
-
-
-
?
human collagen + H2O
?
-
-
-
?
human fibronectin + H2O
?
-
-
-
?
human gamma-interferon + H2O
fragments of human gamma-interferon
-
-
-
?
human lactoferrin + H2O
?
-
-
-
?
human plasma alpha1-proteinase inhibitor + H2O
?
-
-
-
?
human type III collagen + H2O
?
25°C
-
-
?
human type IV collagen + H2O
?
25°C
-
-
?
immunoglobulin G + H2O
?
-
-
-
?
interleukin-6 + H2O
?
-
complete digestion
-
-
?
interleukin-8 + H2O
?
-
rapid processing to a 72 amino acid form, further degradation is slow
-
-
?
methyl-O-Suc-AAPV-7-amido-4-methylcoumarin + H2O
methyl-O-Suc-AAPV + 7-amino-4-methylcoumarin
-
-
-
-
?
monocyte-derived alpha1-antitrypsin + H2O
?
37°C
51-kD polypeptide
-
?
myeloma IgA1-kappa + H2O
?
myeloma IgA2-lamda of A2m(2) allotype + H2O
?
-
predominantly polymeric, 37°C
-
-
?
N-chlorosuccinimide-oxidized inhibitor + H2O
?
25°C, pH 7.4, cleavage occurs between Glu354 and Ala355
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-(Ala)3-p-nitroanilide + H2O
?
nucleoside diphosphate kinase + H2O
?
-
-
-
-
?
orcein-elastin + H2O
?
-
-
-
-
?
ovalbumin + H2O
?
-
-
-
-
?
PAR-1 peptide + H2O
?
-
cleavage at the R41-S42 site
-
-
?
PAR-2 peptide + H2O
?
-
cleavage at the R36-S37 site
-
-
?
PAR-4 peptide + H2O
?
-
cleavage at the R47-G48 site
-
-
?
PAR2 + H2O
?
-
i.e. proteinase-activated receptor 2, enzyme cleaves the N-terminal domain of PAR2 from the cell surface without triggering receptor endocytosis as trypsin does. Cleavage does not activate PAR2, but disarms the recptor for subsequent activation by trypsin
-
?
pentaalanine + H2O
?
30°C, pH 8.6
-
-
?
pentaalanine + H2O
Ala-Ala + Ala-Ala-Ala
-
-
-
?
PFR-7-amido-4-methylcoumarin + H2O
PFR + 7-amino-4-methylcoumarin
-
-
-
-
?
proteinase-activated receptor 2 + H2O
?
the enzyme cleaves proteinase-activated receptor 2 to remove the extracellular Flag epitope
-
-
?
secretory immunoglobulin A + H2O
?
-
-
-
?
Suc-AAF-7-amido-4-methylcoumarin + H2O
Suc-AAF + 7-amino-4-methylcoumarin
-
-
-
-
?
Suc-AFK-7-amido-4-methylcoumarin + H2O
Suc-AFK + 7-amino-4-methylcoumarin
-
-
-
-
?
Suc-GPLGP-7-amido-4-methylcoumarin + H2O
Suc-GPLGP + 7-amino-4-methylcoumarin
-
-
-
-
?
Suc-IIW-7-amido-4-methylcoumarin + H2O
Suc-IIW + 7-amino-4-methylcoumarin
-
-
-
-
?
Suc-LLVY-7-amido-4-methylcoumarin + H2O
Suc-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
surfactant protein A + H2O
?
37°C
-
-
?
surfactant protein D + H2O
?
37°C
-
-
?
tear fluid surfactant protein D + H2O
35000 Da fragment of tear fluid surfactant protein D + ?
-
purified elastase degrades tear fluid surfactant protein D in vitro and in vivo
-
-
?
tetraalanine + H2O
?
30°C, pH 8.6
-
-
?
tetraalanine + H2O
Ala-Ala + Ala-Ala
-
-
-
?
transferrin
?
25°C, pH 7.4
-
-
?
unnicked heat-labile enterotoxin + H2O
?
-
-
-
?
Vitronectin + H2O
?
-
-
-
-
?
Z-AAN-7-amido-4-methylcoumarin + H2O
Z-AAN + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-GAH-7-amido-4-methylcoumarin + H2O
Z-GAH + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-GAM-7-amido-4-methylcoumarin + H2O
Z-GAM + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-GGL-7-amido-4-methylcoumarin + H2O
Z-GGL + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-GGR-7-amido-4-methylcoumarin + H2O
Z-GGR + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-LLE-7-amido-4-methylcoumarin + H2O
Z-LLE + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-RLRGG-7-amido-4-methylcoumarin + H2O
Z-RLRGG + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
-
-
-
-
?
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
37°C
-
-
?
azocasein + H2O
?
37°C
-
-
?
azocasein + H2O
?
37°C, pH 8.0
-
-
?
azocasein + H2O
?
-
pH 7.5, 37°C
-
-
?
azocasein + H2O
?
pH 7.5, 37°C
-
-
?
azocasein + H2O
?
proteolytic activity is 8 to 9fold lower than in the wild-type strain
-
-
?
azocasein + H2O
?
-
37°C
-
-
?
azocasein + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
carbobenzoxy-Gly-Tyr-NH2 + H2O
?
-
-
-
-
?
carbobenzoxy-Gly-Tyr-NH2 + H2O
?
-
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
pH 7.4, 40°C
-
-
?
casein + H2O
?
WP_084338031.1
-
-
-
?
casein + H2O
?
WP_084338031.1
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
colostral S-IgA + H2O
?
-
37°C
-
-
?
colostral S-IgA + H2O
?
-
37°C
-
-
?
eggshell-membrane + H2O
?
WP_084338031.1
the enzyme can be applied to obtain bioactive soluble peptides from eggshell-membrane
-
-
?
eggshell-membrane + H2O
?
WP_084338031.1
the enzyme can be applied to obtain bioactive soluble peptides from eggshell-membrane
-
-
?
elastase propeptide + H2O
elastase + ?
-
autocatalytically cleaved
-
?
elastase propeptide + H2O
elastase + ?
-
autocatalytically cleaved
-
?
elasti-orcein + H2O
?
WP_084338031.1
-
-
-
?
elasti-orcein + H2O
?
WP_084338031.1
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
37°C
-
-
?
Elastin + H2O
?
37°C
-
-
?
Elastin + H2O
?
pH 7.5, 37°C
-
-
?
Elastin + H2O
?
pH 8.6, 30°C
-
-
?
Elastin + H2O
?
human tropoelastin
-
-
?
Elastin + H2O
?
pseudolysin bound to bovine elastin fibers and preferred to attack peptide bonds with hydrophobic residues at the P1 and P1' positions in the hydrophobic domains of elastin
-
-
?
Elastin + H2O
?
-
37°C
-
-
?
Elastin + H2O
?
-
-
-
-
?
elastin Congo red + H2O
?
-
-
-
-
?
elastin Congo red + H2O
?
elastolytic activity is 14fold lower than in the wild-type strain
-
-
?
elastin Congo red + H2O
?
elastolytic activity is 20fold lower than in the wild-type strain
-
-
?
elastin Congo red + H2O
?
-
pH 7.0
-
-
?
elastin Congo red + H2O
?
pH 7.0, 37°C
-
-
?
elastin Congo red + H2O
?
pH 8.0
-
-
?
elastin Congo red + H2O
?
-
pH 7.0
-
-
?
Fibrin + H2O
?
-
-
-
?
flagellin + H2O
?
the enzyme is capable of degrading exogenous flagellin under calcium-replete conditions and prevents flagellin-mediated immune recognition
-
-
?
flagellin + H2O
?
the enzyme is capable of degrading exogenous flagellin under calcium-replete conditions and prevents flagellin-mediated immune recognition
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
-
poor substrate
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
pH 7.5, 23-25°C
-
-
?
furylacryloyl-glycyl-L-leucyl-L-alanine + H2O
furylacryloyl-glycine + L-leucyl-L-alanine
25°C, pH 7.5
-
-
?
furylacryloyl-glycyl-L-leucyl-L-alanine + H2O
furylacryloyl-glycine + L-leucyl-L-alanine
pH 7.5, 25°C
-
-
?
Gliadin + H2O
?
-
-
-
-
?
Gliadin + H2O
?
-
-
-
-
?
gluten + H2O
?
-
-
-
-
?
hide powder azure + H2O
?
-
pH 7.0
-
-
?
hide powder azure + H2O
?
-
pH 7.0
-
-
?
human thrombin + H2O
?
-
-
-
?
human thrombin + H2O
?
digestion of thrombin by Pseudomonas aeruginosa elastase leads to the release of the C-terminal thrombin-derived peptide FYT21, which inhibits pro-inflammatory responses to several pathogen-associated molecular patterns in vitro and in vivo by preventing toll-like receptor dimerization and subsequent activation of down-stream signalling pathways the enzyme cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses
-
-
?
immunoglobulin A + H2O
?
-
-
-
?
immunoglobulin A + H2O
?
-
-
-
?
Laminin + H2O
?
-
-
-
?
myeloma IgA1-kappa + H2O
?
-
predominantly monomeric, 37°C
-
-
?
myeloma IgA1-kappa + H2O
?
-
predominantly polymeric, 37°C
-
-
?
myeloma IgA1-kappa + H2O
?
-
predominantly monomeric, 37°C
-
-
?
myeloma IgA1-kappa + H2O
?
-
predominantly polymeric, 37°C
-
-
?
N-succinyl-L-(Ala)3-p-nitroanilide + H2O
?
-
36°C, pH 7.5
-
-
?
N-succinyl-L-(Ala)3-p-nitroanilide + H2O
?
-
36°C, pH 7.5
-
-
?
additional information
?
-
-
pseudolysin eliminates epitopes recognized by the R5 antibody, while those detected by the G12 antibody remain intact, despite destruction of the nearby major T-cell epitope QPQLPY
-
-
?
additional information
?
-
-
pseudolysin eliminates epitopes recognized by the R5 antibody, while those detected by the G12 antibody remain intact, despite destruction of the nearby major T-cell epitope QPQLPY
-
-
?
additional information
?
-
-
with synthetic substrates of the general structure benzyloxycarbonyl-Phe-Xaa-Ala, the Phe-Xaa bond is cleaved, the decreasing order of preference for Xaa is as follows: Phe, Leu, Tyr, Val, Ile
-
-
?
additional information
?
-
-
specificity against aromatic or hydrophobic amino acid residues at the amino-side of the splitting point
-
-
?
additional information
?
-
-
probably responsible for the tissue destruction observed during pulmonary and corneal infections by the pathogen organism Pseudomonas aeruginosa
-
-
?
additional information
?
-
-
no activity with dabsyl-Leu-Gly-Gly-Gly-Ala-edans
-
-
?
additional information
?
-
key catalytic residues and residues at the S1 and S'1 binding subsites, reaction mechanism, overview
-
-
?
additional information
?
-
-
key catalytic residues and residues at the S1 and S'1 binding subsites, reaction mechanism, overview
-
-
?
additional information
?
-
-
enzyme prefers Ser at position P1, Lys at P2 and hydropobic amino acids at the P1' and P2' positions
-
-
?
additional information
?
-
-
large exopeptidase LepA activates nuclear factor kappa-kB-driven promoter through human protease activated receptors PAR-1, -2 or -4 and cleaves the peptides corresponding to the tethered ligand region of human PAR-1, -2 and -4 at a specific site with exposure of their tethered ligands
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-Ala-p-nitroanilide, N-succinyl-Ala-Pro-Ala-p-nitroanilide
-
-
?
additional information
?
-
-
non- and glycosylated isoforms of rPAE display similar kinetic parameters for hydrolyzing casein in aqueous medium, and when catalyzing bipeptide synthesis in 50% v/v DMSO, they exhibit identical substrate specificity and activity, and produce similar yields
-
-
?
additional information
?
-
-
the enzyme shows both hemolytic and hemorrhagic activities in vivo
-
-
?
additional information
?
-
-
enzyme prefers Ser at position P1, Lys at P2 and hydropobic amino acids at the P1' and P2' positions
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-Ala-p-nitroanilide, N-succinyl-Ala-Pro-Ala-p-nitroanilide
-
-
?
additional information
?
-
-
the enzyme shows both hemolytic and hemorrhagic activities in vivo
-
-
?
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1,4-dithiothreitol
-
5 mM, 0% residual activity
1-(biphenyl-4-ylmethyl)-3-hydroxy-2-methylpyridine-4(1H)-thione
-
-
2,2'-bipyridine
-
slight inhibition
2-mercaptoacetyl-L-phenyalanyl-L-leucine
-
-
2-mercaptoacetyl-L-phenylalanyl-L-leucine
prevents corneal perforation completely
2-mercaptoacetyl-Leu-Dphe
-
2-mercaptoacetyl-Leu-Phe
-
2-mercaptoacetyl-Phe-Leu
at 0.1 mM 96% inhibition with azocasein as substrate, 97% inhibition with elastin as substrate and 97% inhibition with cartilage as substrate, at 0.01 mM 77% inhibition with azocasein as substrate, 33% inhibition with elastin as substrate and 66% inhibition with cartilage as substrate
2-mercaptoacetylphenylalanylleucine
specific
2-mercaptoethanol
-
18.8% inhibition at 5 mM
2-[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
-
-
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
-
the phenyl group of the strong binder occupies the S'2-subpocket, while a second ring system occupy the S1-subpocket in both thermolysin, EC 3.4.24.27, and pseudolysin
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[3-(4-phenylpiperazin-1-yl)propyl]acetamide (non-preferred name)
-
the phenyl group of the strong binder occupies the S'2-subpocket, while a second ring system occupy the S1-subpocket in both thermolysin, EC 3.4.24.27, and pseudolysin
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
-
-
2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
-
-
3-(2-furyl)acryloyl-glycine
-
3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine
-
ammonium chloride
extracellular elastase activity decreases if cells are cultured in the presence of ammonium chloride
anti elastase monoclonal antibody
reduces PE activity significantly
-
Aprotinin
-
markedly decreases enzymatic activity
Ba2+
-
5 mM, slightly decreases activity
benzyloxycarbonyl-Gly-NHOH
at 14 mM 98% inhibition with azocasein as substrate, 95% inhibition with elastin as substrate and 95% inhibition with cartilage as substrate, at 1.4 mM 77% inhibition with azocasein as substrate, 84% inhibition with elastin as substrate and 67% inhibition with cartilage as substrate
benzyloxycarbonyl-L-leucine
-
benzyloxycarbonyl-L-leucyl-hydroxamate
-
benzyloxycarbonyl-L-phenylalanine
-
benzyloxycarbonyl-Leu-NHOH
at 5.0 mM 98% inhibition with azocasein as substrate, 100% inhibition with elastin as substrate and 94% inhibition with cartilage as substrate, at 0.5 mM 76% inhibition with azocasein as substrate, 93% inhibition with elastin as substrate and 57% inhibition with cartilage as substrate
benzyloxycarbonyl-Phe-NHOH
-
Cd2+
-
5 mM, decreases activity
cetyltrimethylammonium bromide
-
0.1%, 53% residual activity
CH2ICOOH
WP_084338031.1
3 mM,88 % inhibition
ClCH2CO-HOLeu-Ala-Gly-NH2
non-competitive
ClCH2CO-N-hydroxyleucine-Ala-Gly-NH2
-
-
D-glucose
extracellular elastase activity decreases if cells are cultured in the presence of glucose
DTT
WP_084338031.1
3 mM, 24% inhibition
Elastatinal
-
markedly decreases enzymatic activity
HS-CH2-CO-Phe-Tyr-NH2
-
at 0.2 mM and 0.025 mM inhibits the degradation of the pseudolysin natural substrates nucleoside diphosphate kinase and IgG, respectively
HSAc-Leu-Phe
-
0.1 mM, inhibits 97% of the degradation of azocasein and elastin substrates by pseudolysin
HSAc-Phe-Leu
-
0.1 mM, inhibits 97% of the degradation of azocasein and elastin substrates by pseudolysin
HSCH2(DL)CH[CH2CH(CH3)2]CO-Phe-Ala-NH2
2 isomeric forms
L-cysteine
-
complete inhibition at 1.25 mM
L-phenylalanyl-L-phenylalanine
-
N-(1-carboxy-3-phenylpropyl)-phenylalanyl-alpha-asparagine
enzyme binding structure analysis, PDB ID 1U4G. The inhibitor is bound in the S1-S1 sub-sites of pseudolysin by hydrogen bonding and hydrophobic and weak van der Waal's interactions
N-aryl mercaptoacetamide
-
-
N-mercaptoacetyl-Phe-Tyr-amide
-
-
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
-
-
Na2 EDTA
-
complete inhibition at 10 mM
peptides
-
containing the hydroxamic acid, N-hydroxypeptide and thiol functional groups
phosphoryl-L-leucyl-L-phenylalanine
S-homoPhe [N-alpha-alpha]Phe-IsoAsn
L-155542, competitive
sodium dodecylsulfate
-
0.1%, 61% residual activity
sodium sulfite
WP_084338031.1
3 mM, 94% inhibition
Soybean trypsin inhibitor
-
markedly decreases enzymatic activity
-
specific polyclonal rabbit antielastase antiserum
-
-
Streptomyces metalloproteinase inhibitor
-
i.e. SMPI, molecular dynamics study of enzyme-inhibitor complex. Inhibitor interacts with pseudolysin via the rigid active side loop and several contact sites outside this loop
-
TLCK
-
markedly decreases enzymatic activity
[(biphenyl-4-ylmethyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
-
-
[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
-
-
[1-[2-(hydroxyamino)-2-oxoethyl]-2-[3-(4-phenylpiperazin-1-yl)propyl]hydrazinyl]acetic acid
-
-
[[(4-methoxyphenyl)sulfonyl](2-oxo-2-[[2-(4-sulfamoylphenyl)ethyl]amino]ethyl)amino]acetic acid
-
-
[[2-(hydroxyamino)-2-oxoethyl](4-nitrobenzyl)amino]acetic acid
-
-
[[2-(hydroxyamino)-2-oxoethyl](4-phenoxybenzyl)amino]acetic acid
-
-
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
-
-
[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]acetic acid
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
complete inhibition at 1 mM
1,10-phenanthroline
non-specific
1,10-phenanthroline
-
5 mM, 0% residual activity
1,10-phenanthroline
-
1 mM, complete inhibition
1,10-phenanthroline
-
slight inhibition
Ca2+
-
5 mM, 54% residual activity
Ca2+
-
10.6% inhibition at 5 mM
Ca2+
-
5 mM, slightly decreases activity
Co2+
-
50% inhibition at 0.625 mM
Co2+
-
5 mM, slightly decreases activity
Cu2+
-
complete inhibition
Cu2+
-
5 mM, 21% residual activity
Cu2+
-
complete inhibition at 5 mM
Cu2+
-
5 mM, slightly decreases activity
EDTA
-
-
EDTA
-
complete inactivation at 6 mM
EDTA
-
5 mM, 25% residual activity
EDTA
-
1 mM, 28% residual activity
EDTA
-
57.7% inhibition at 2 mM, 68.5% inhibition at 5 mM
EDTA
WP_084338031.1
3 mM, 14% inhibition
EGTA
-
inhibition to a lesser extent than with EDTA
Fe3+
-
75% inhibition at 0.625 mM
Fe3+
-
5 mM, slightly decreases activity
Hg2+
-
complete inhibition at 5 mM
Hg2+
-
5 mM, slightly decreases activity
Mg2+
-
at 10 mM the activity is reduced by only 15%
Mg2+
-
5 mM, 56% residual activity
Mg2+
-
16.4% inhibition at 5 mM
Mg2+
-
5 mM, slightly decreases activity
Mn2+
-
complete inhibition at 10 mM
Mn2+
-
30% inhibition at 0.625 mM
Mn2+
-
5 mM, 40% residual activity
Mn2+
-
81.9% inhibition at 5 mM
Mn2+
-
5 mM, slightly decreases activity
Ni2+
-
complete inhibition at 10 mM
Ni2+
-
5 mM, 12% residual activity
o-phenanthroline
-
o-phenanthroline
-
1 mM, 16% residual activity
phosphoramidon
-
-
phosphoramidon
N-(alpha-rhamnopyranosyloxyhydroxyphosphinyl)-Leu-Trp
phosphoramidon
-
N-(alpha-L-rhamnopyranosyloxyhydroxyphosphinyl)-L-leucyl-L-tryptophan
phosphoramidon
-
1 mM, 10% residual activity
phosphoramidon
-
powerful inhibition action on pseudolysin
phosphoramidon
WP_084338031.1
3 mM, 13% inhibition
phosphoryl-L-leucyl-L-phenylalanine
at 0.1 mM 98% inhibition with azocasein as substrate, 94% inhibition with elastin as substrate and 98% inhibition with cartilage as substrate, at 0.01 mM 83% inhibition with azocasein as substrate, 87% inhibition with elastin as substrate and 89% inhibition with cartilage as substrate
phosphoryl-L-leucyl-L-phenylalanine
-
PMSF
-
markedly decreases enzymatic activity
PMSF
WP_084338031.1
5 mM, 27% inhibition
Zn2+
-
complete inhibition at 10 mM
Zn2+
-
complete inhibition
Zn2+
-
5 mM, 63% residual activity
Zn2+
-
complete inhibition at 5 mM
additional information
-
inhibitor synthesis, docking analysis and binding structure, molecular modeling and Molecular dynamics simulation of pseudolysin-ligand interactions, overview. When the compounds possess two ring systems, the largest and most electron rich ring system seems to occupy the S1-subpocket. The fourth zinc coordinating ligand in the free enzyme is a water molecule. Upon inhibitor binding this water molecule is replaced by a metal binding group of the inhibitor
-
additional information
-
not: ClCH2CO-N-hydroxyleucine-OCH3
-
additional information
-
diisopropyl fluorophosphate; not: ClCH2CO-N-hydroxyleucine-OCH3; tosyl-L-Phe chloromethyl ketone, PCMB
-
additional information
no inhibition by gentamicin
-
additional information
-
no inhibition by gentamicin
-
additional information
-
no inhibition by diisopropylphosphofluoridate at 20 mM
-
additional information
extracellular elastase activity decreases if cells are cultured in the presence of sub-inhibitory concentrations of certain antibiotics
-
additional information
-
extracellular elastase activity decreases if cells are cultured in the presence of sub-inhibitory concentrations of certain antibiotics
-
additional information
-
no inhibition by dithio-bis(nitrobenzoic acid) and phenylmethylsulfonyl fluoride, and by K+ and Na+
-
additional information
N-alpha mercaptoamide-containing dipeptides as inhibitors
-
additional information
-
N-alpha mercaptoamide-containing dipeptides as inhibitors
-
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Abscess
Suppression of polymorphonuclear leucocyte chemotaxis by Pseudomonas aeruginosa elastase in vitro: a study of the mechanisms and the correlation with ring abscess in pseudomonal keratitis.
Abscess
The role of Pseudomonas aeruginosa elastase in corneal ring abscess formation in pseudomonal keratitis.
Acute Lung Injury
Acute lung injury induced by Pseudomonas aeruginosa elastase in hamsters.
Aneurysm
Indomethacin prevents elastase-induced abdominal aortic aneurysms in the rat.
Aortic Aneurysm, Abdominal
Production and localization of 92-kilodalton gelatinase in abdominal aortic aneurysms. An elastolytic metalloproteinase expressed by aneurysm-infiltrating macrophages.
Arthritis, Rheumatoid
A trypsin sensitive stromelysin isolated from rheumatoid synovial fluid is an activator for matrix metalloproteinases.
Arthritis, Rheumatoid
Paradoxical derepression of collagenase gene expression by the antirheumatic gold compound aurothiomalate.
Celiac Disease
Identification of Pseudolysin (lasB) as an Aciduric Gluten-Degrading Enzyme with High Therapeutic Potential for Celiac Disease.
Cross Infection
Structural Requirements of N-alpha-Mercaptoacetyl Dipeptide (NAMdP) Inhibitors of Pseudomonas Aeruginosa Virulence Factor LasB: 3D-QSAR, Molecular Docking, and Interaction Fingerprint Studies.
Cystic Fibrosis
Colistin stimulates the activity of neutrophil elastase and Pseudomonas aeruginosa elastase.
Cystic Fibrosis
Evidence that Pseudomonas aeruginosa elastase does not inactivate the bronchial inhibitor in the presence of leukocyte elastase. Studies with cystic fibrosis sputum and with pure proteins.
Cystic Fibrosis
Functional importance of cystic fibrosis immunoglobulin G fragments generated by Pseudomonas aeruginosa elastase.
Cystic Fibrosis
Granulocyte neutral proteases and Pseudomonas elastase as possible causes of airway damage in patients with cystic fibrosis.
Cystic Fibrosis
Production of elastase, exotoxin A, and alkaline protease in sputa during pulmonary exacerbation of cystic fibrosis in patients chronically infected by Pseudomonas aeruginosa.
Cystic Fibrosis
Pseudomonas aeruginosa elastase disables proteinase-activated receptor 2 in respiratory epithelial cells.
Cystic Fibrosis
Pseudomonas aeruginosa LasB protease impairs innate immunity in mice and humans by targeting a lung epithelial cystic fibrosis transmembrane regulator-IL-6-antimicrobial-repair pathway.
Encephalomyelitis, Autoimmune, Experimental
Treatment of an encephalitogenic peptide from guinea pig myelin basic protein with alpha-protease and thermolysin. Isolation of fragments and determination of cleavage sites.
Hyperhomocysteinemia
Hyperhomocysteinemia induces elastolysis in minipig arteries: structural consequences, arterial site specificity and effect of captopril-hydrochlorothiazide.
Infections
Colistin stimulates the activity of neutrophil elastase and Pseudomonas aeruginosa elastase.
Infections
Diverse effects of Galleria mellonella infection with entomopathogenic and clinical strains of Pseudomonas aeruginosa.
Infections
Experimental studies of the pathogenesis of infections owing to Pseudomonas aeruginosa: elastase, an IgG protease.
Infections
Immunization with a Pseudomonas aeruginosa elastase peptide reduces severity of experimental lung infections due to P. aeruginosa Or Burkholderia cepacia.
Infections
Manipulation of the silkworm immune system by a metalloprotease from the pathogenic bacterium Pseudomonas aeruginosa.
Infections
N-Aryl-3-mercaptosuccinimides as Antivirulence Agents Targeting Pseudomonas aeruginosa Elastase and Clostridium Collagenases.
Infections
Neutrophil elastase cleaves C3bi on opsonized pseudomonas as well as CR1 on neutrophils to create a functionally important opsonin receptor mismatch.
Infections
Novel Inhibitors Of The Pseudomonas aeruginosa Virulence Factor Pseudolysin/LasB: A Potential Therapeutic Approach For The Attenuation Of Virulence Mechanisms In Pseudomonal Infection.
Infections
Pseudomonas aeruginosa Keratitis: Protease IV and PASP as Corneal Virulence Mediators.
Infections
Pseudomonas keratitis. The role of an uncharacterized exoprotein, protease IV, in corneal virulence.
Infections
Pseudomonas protease. Purification, partial characterization, and its effect on collagen, proteoglycan, and rabbit corneas.
Keratitis
Corneal virulence of Pseudomonas aeruginosa elastase B and alkaline protease produced by Pseudomonas putida.
Keratitis
Identification of a novel secreted protease from Pseudomonas aeruginosa that causes corneal erosions.
Keratitis
Inhibition of Pseudomonas aeruginosa elastase and Pseudomonas keratitis using a thiol-based peptide.
Keratitis
Pseudomonas aeruginosa small protease (PASP), a keratitis virulence factor.
Keratitis
Specific inhibitors of Pseudomonas aeruginosa elastase as potential drugs for the treatment of Pseudomonas keratitis.
Keratitis
Suppression of polymorphonuclear leucocyte chemotaxis by Pseudomonas aeruginosa elastase in vitro: a study of the mechanisms and the correlation with ring abscess in pseudomonal keratitis.
Keratitis
The effect of 2-mercaptoacetyl-L-phenylalanyl-L-leucine, a specific inhibitor of Pseudomonas aeruginosa elastase, on experimental Pseudomonas keratitis in rabbit eyes.
Keratitis
The role of Pseudomonas aeruginosa elastase in corneal ring abscess formation in pseudomonal keratitis.
Lung Neoplasms
Characterization of a connective tissue degrading metalloproteinase from human small cell lung cancer cells.
Neoplasms
Enhancement of neutral metalloproteinase in the dermis after one topical application of tumor-promoting phorbol ester.
Neoplasms
Synthesis and HPLC analysis of enzymatically cleavable linker consisting of poly(ethylene glycol) and dipeptide for the development of immunoconjugate.
Osteoarthritis
The effect of drugs used in the treatment of osteoarthrosis on stromelysin (proteoglycanase) of equine synovial cell origin.
Otitis Media
[The quantitation of Pseudomonas aeruginosa elastase in suppurative chronic otitis media using a sensitive ELISA method]
Otitis Media, Suppurative
ELISA to determine immunoreactive Pseudomonas aeruginosa elastase in chronic suppurative otitis media.
Otitis Media, Suppurative
[The quantitation of Pseudomonas aeruginosa elastase in suppurative chronic otitis media using a sensitive ELISA method]
Pseudomonas Infections
Pseudomonas aeruginosa elastase and its role in pseudomonas infections.
Pseudomonas Infections
Site-directed mutagenesis of Glu-141 and His-223 in Pseudomonas aeruginosa elastase: catalytic activity, processing, and protective activity of the elastase against Pseudomonas infection.
Small Cell Lung Carcinoma
Characterization of a connective tissue degrading metalloproteinase from human small cell lung cancer cells.
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0.00273
1-(biphenyl-4-ylmethyl)-3-hydroxy-2-methylpyridine-4(1H)-thione
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.031
2-[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.0004
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.0028 - 0.0067
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[3-(4-phenylpiperazin-1-yl)propyl]acetamide (non-preferred name)
0.015 - 0.033
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
0.016 - 0.276
2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
0.0000059
N-aryl mercaptoacetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.082 - 0.336
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
0.121
[(biphenyl-4-ylmethyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.15 - 0.241
[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
0.33
[1-[2-(hydroxyamino)-2-oxoethyl]-2-[3-(4-phenylpiperazin-1-yl)propyl]hydrazinyl]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.282
[[(4-methoxyphenyl)sulfonyl](2-oxo-2-[[2-(4-sulfamoylphenyl)ethyl]amino]ethyl)amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.02
[[2-(hydroxyamino)-2-oxoethyl](4-nitrobenzyl)amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.2 - 0.43
[[2-(hydroxyamino)-2-oxoethyl](4-phenoxybenzyl)amino]acetic acid
0.153 - 0.169
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
0.046 - 0.186
[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]acetic acid
0.0028
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[3-(4-phenylpiperazin-1-yl)propyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate 7-methoxycoumarin-4-yl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
0.0067
2-[benzyl[2-(hydroxyamino)-2-oxoethyl]amino]-N-[3-(4-phenylpiperazin-1-yl)propyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.015
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.033
2-[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate 7-methoxycoumarin-4-yl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
0.016
2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.276
2-[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]-N-[2-(4-sulfamoylphenyl)ethyl]acetamide (non-preferred name)
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate 7-methoxycoumarin-4-yl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
0.082
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.336
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate 7-methoxycoumarin-4-yl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
0.15
[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.241
[(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate 7-methoxycoumarin-4-yl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
0.2
[[2-(hydroxyamino)-2-oxoethyl](4-phenoxybenzyl)amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.43
[[2-(hydroxyamino)-2-oxoethyl](4-phenoxybenzyl)amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate 7-methoxycoumarin-4-yl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
0.153
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate 7-methoxycoumarin-4-yl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
0.169
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
0.046
[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate 7-methoxycoumarin-4-yl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
0.186
[[2-(hydroxyamino)-2-oxoethyl][(4-phenoxyphenyl)sulfonyl]amino]acetic acid
Bacillus thermoproteolyticus
-
pH 7.8, 37°C, versus substrate Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide
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Nishino, N.; Powers, J.C.
Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand
J. Biol. Chem.
255
3482-3486
1980
Pseudomonas aeruginosa
brenda
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Mun, J.J.; Tam, C.; Kowbel, D.; Hawgood, S.; Barnett, M.J.; Evans, D.J.; Fleiszig, S.M.
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Pseudomonas aeruginosa PAO1
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Pseudomonas aeruginosa
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Ghorbel-Bellaaj, O.; Khaled, H.B.; Bayoudh, A.; Younes, I.; Hmidet, N.; Jellouli, K.; Nasri, M.
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Pseudomonas aeruginosa, Pseudomonas aeruginosa A2
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Andrejko, M.; Mizerska-Dudka, M.
Elastase B of Pseudomonas aeruginosa stimulates the humoral immune response in the greater wax moth, Galleria mellonella
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Pseudomonas aeruginosa
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Identification of pseudolysin (lasB) as an aciduric gluten-degrading enzyme with high therapeutic potential for celiac disease
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Site-specific pegylation of an antimicrobial peptide increases resistance to Pseudomonas aeruginosa elastase
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Pseudomonas aeruginosa
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Han, M.; Wang, X.; Ding, H.; Jin, M.; Yu, L.; Wang, J.; Yu, X.
The role of N-glycosylation sites in the activity, stability, and expression of the recombinant elastase expressed by Pichia pastoris
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Pseudomonas aeruginosa
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Wildeboer, D.; Hill, K.E.; Jeganathan, F.; Williams, D.W.; Riddell, A.D.; Price, P.E.; Thomas, D.W.; Stephens, P.; Abuknesha, R.A.; Price, R.G.
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Pseudomonas aeruginosa
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Bacillus thermoproteolyticus
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A comprehensive alanine-scanning mutagenesis study reveals roles for salt bridges in the structure and activity of Pseudomonas aeruginosa elastase
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Pseudomonas aeruginosa
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Odunuga, O.; Adekoya, O.; Sylte, I.
High-level expression of pseudolysin, the extracellular elastase of Pseudomonas aeruginosa, in Escherichia coli and its purification
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Pseudomonas aeruginosa
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Yang, J.; Zhao, H.; Ran, L.; Li, C.; Zhang, X.; Su, H.; Shi, M.; Zhou, B.; Chen, X.; Zhang, Y.
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Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
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Galdino, A.C.M.; de Oliveira, M.P.; Ramalho, T.C.; de Castro, A.A.; Branquinha, M.H.; Santos, A.L.S.
Anti-virulence strategy against the multidrug-resistant bacterial pathogen Pseudomonas aeruginosa pseudolysin (elastase B) as a potential druggable target
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Pseudomonas aeruginosa
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Jose, D.; Mohandas, A.; Bright Singh, I.
Bioprocess technology for LasB protease (elastase) production from Pseudomonas aeruginosa MCCB 123
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Pseudomonas aeruginosa (G1EMI7), Pseudomonas aeruginosa MCCB 123 (G1EMI7)
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Casilag, F.; Lorenz, A.; Krueger, J.; Klawonn, F.; Weiss, S.; Haeussler, S.
The LasB elastase of Pseudomonas aeruginosa acts in concert with alkaline protease AprA to prevent flagellin-mediated immune recognition
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Pseudomonas aeruginosa (Q02RJ6), Pseudomonas aeruginosa UCBPP-PA14 (Q02RJ6)
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Said, Z.S.A.M.; Arifi, F.A.M.; Salleh, A.B.; Rahman, R.N.Z.R.A.; Leow, A.T.C.; Latip, W.; Ali, M.S.M.
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Pseudomonas aeruginosa (A7LI11)
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Kotb, E.; El-Zawahry, Y.; Saleh, G.
Isolation of a putative virulence agent, cytotoxic serine-elastase, from a newly isolated Pseudomonas aeruginosa ZuhP13
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Pseudomonas aeruginosa, Pseudomonas aeruginosa ZuhP13
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Smith, K.; Rajendran, R.; Kerr, S.; Lappin, D.F.; Mackay, W.G.; Williams, C.; Ramage, G.
Aspergillus fumigatus enhances elastase production in Pseudomonas aeruginosa co-cultures
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Pseudomonas aeruginosa
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Li, Y.; Bai, F.; Xia, H.; Zhuang, L.; Xu, H.; Jin, Y.; Zhang, X.; Bai, Y.; Qiao, M.
A novel regulator PA5022 (aefA) is involved in swimming motility, biofilm formation and elastase activity of Pseudomonas aeruginosa
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Pseudomonas aeruginosa, Pseudomonas aeruginosa PA68
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van der Plas, M.J.; Bhongir, R.K.; Kjellstroem, S.; Siller, H.; Kasetty, G.; Moergelin, M.; Schmidtchen, A.
Pseudomonas aeruginosa elastase cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses
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Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
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Shinji, T.; Moe, Y.; Yukihiro, K.; Yoko, Y.; Hitoshi, A.
Characterization of an organic-solvent-stable elastase from Pseudomonas indica and its potential use in eggshell membrane hydrolysis
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