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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
Vibrio cholerae serotype O1
-
-
-
-
?
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-S1â 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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0.034
2-mercaptoacetyl-Leu-Dphe
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0015
2-mercaptoacetyl-Leu-Phe
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0002
2-mercaptoacetyl-Phe-Leu
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
4
3-(2-furyl)acryloyl-glycine
-
5
3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine
-
0.028
benzyloxycarbonyl-Gly-NHOH
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
6.2
benzyloxycarbonyl-L-leucine
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
5
benzyloxycarbonyl-L-phenylalanine
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.011
benzyloxycarbonyl-Leu-NHOH
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.021
benzyloxycarbonyl-Phe-NHOH
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
1.5
L-phenylalanyl-L-phenylalanine
-
1.1
Leu-Phe
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.000041
N-mercaptoacetyl-Phe-Tyr-amide
-
pH and temperature not specified in the publication
0.4
Phe-Leu
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0002
phosphoryl-L-leucyl-L-phenylalanine
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0004
rapidly eluting isomer of HSCH2(DL)CH[CH2CH(CH3)2]CO-Phe-Ala-NH2
-
-
0.00003
S-homoPhe [N-alpha-alpha]Phe-IsoAsn
-
0.0003
slowly eluting isomer of HSCH2(DL)CH[CH2CH(CH3)2]CO-Phe-Ala-NH2
-
-
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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
0.0067
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
0.0028
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
0.015
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
0.43
[[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
0.2
[[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
0.169
[[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
0.153
[[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
0.046
[[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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malfunction
-
the exosecretome of the LasB-deficient pseudomonal strain PAO1lasBDELTA has limited impact on human vascular cell adherence and viability
physiological function

-
elastase B of Pseudomonas aeruginosa stimulates the humoral immune response in larvae of the greater wax moth, Galleria mellonella. The insects exhibit increased antibacterial activity with appearance of antimicrobial peptides and a higher level of lysozyme in cell-free hemolymph
physiological function
-
Pseudomonal LasB cleaves extracellular matrix proteins involved in adherence of vascular stromal cells in human host. LasB can induce vascular cell anoikis in human cells through simultaneous proteolysis of extracellular matrix components and cell receptors, suggesting the uPAR-vitronectin axis as a major target in this process. In heart valves of patients occurs extensive, LasB-dependent degradation of extracellular matrix-associated fibronectin and vitronectin, that preceeds cell de-adherence, whereas type I collagen shows limited degradation. Disruption of cell/ECM interactions resulting from uncontrolled pericellular proteolysis leads to detachment-induced cell apoptosis, anoikis, contributing to the morbid evolution of inflammatory vascular diseases, overview
physiological function
pseudolysin is the most abundant protease secreted by Pseudomonas aeruginosa and is the major extracellular virulence factor of this opportunistic human pathogen. Pseudolysin destroys human tissues by solubilizing elastin
physiological function
-
the protease is a virulence factor that acts by destroying peptides of the native immune system
physiological function
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 pathwaysthe enzyme cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses
physiological function
-
the enzyme is produced during the course of clinical infections and plays an important role in the virulence of Pseudomonas aeruginosa in chronic lung infections
physiological function
-
the enzyme outstands as a pivotal virulence attribute during the infectious process, playing multifunctional roles in different aspects of the pathogen-host interaction. Most abundant peptidase found in pseudomonal secretions, which contributes to the invasiveness of Pseudomonas aeruginosa due to its ability to cleave several extracellular matrix proteins and to disrupt the basolateral intercellular functions present in the host tissues. Pseudolysin makes Pseudomonas aeruginosa able to overcome host defenses by the hydrolysis of many immunologically relevant molecules, including antibodies and complement components
physiological function
virulence factor
physiological function
-
the enzyme is produced during the course of clinical infections and plays an important role in the virulence of Pseudomonas aeruginosa in chronic lung infections
-
physiological function
-
virulence factor
-
evolution

-
the typical metalloendopeptidases consensus zinc-binding sequence HEXXH and the catalytic residues in the active site are conserved in the A2 elastase
evolution
-
pseudolysin belongs to the thermolysin-like family of metallopeptidases
evolution
-
pseudolysin is a metalloprotease belonging to the thermolysin (M4) family proteases
evolution
pseudolysin is a Zn2+ metalloprotease of the thermolysin family
evolution
-
the enzyme is an M4 family metalloprotease
evolution
-
thermolysin and pseudolysin belong to subclan MA(E) of peptidases, also known as the Glu-zincins, of the matrix metalloproteinases family of zinc-containing endoproteinases with broad substrate specificity and extracellular matrix components are among the substrates
evolution
-
pseudolysin is a metalloprotease belonging to the thermolysin (M4) family proteases
-
evolution
-
the typical metalloendopeptidases consensus zinc-binding sequence HEXXH and the catalytic residues in the active site are conserved in the A2 elastase
-
additional information

-
the N-terminal signal peptide consists of 23 residues bordered with the signal peptidase recognition site Ala-Phe-Ala-Ala
additional information
mechanism of action of endopeptidase pseudolysin on elastin binding and degradation, pseudolysin has a preference for aromatic and/or large aliphatic amino acids at the P1' position and a distinct bias against acidic residues at the P2' position, overview
additional information
-
mechanism of action of endopeptidase pseudolysin on elastin binding and degradation, pseudolysin has a preference for aromatic and/or large aliphatic amino acids at the P1' position and a distinct bias against acidic residues at the P2' position, overview
additional information
-
salt bidges in the enzyme, structure overview. Relationship between salt bridges and stability/enzymatic activity, structure analysis and molecular dynamics using crystal structure with PDB ID 1EZM, overview
additional information
-
the enzyme is synthesized in the cytoplasm as a pre-proenzyme consisting of a 2.4-kDa signal peptid, an 18.1-kDa pro-peptide and the 33.1-kDa mature protein. The signal peptide is cleaved from the pre-proenzyme during translocation across the inner membrane, leaving a 51.2-kDa proenzyme (consisting of the pro-peptide and the mature protein). In the periplasm, the proenzymeis folded, guided by the pro-peptide, and a disulfide bond between Cys270 and Cys297 is formed. The pro-peptide is then removed by autoproteolysis, but remains non-covalently attached to mature pseudolysin. A second disulfide bond between Cys30 and Cys58 of the enzyme is then formed. The pro-peptide and mature enzyme are secreted from the cell together, where they dissociate, and the liberated pro-peptide is degraded by the active enzyme
additional information
-
the glutamic acid of the HEXXH motif is catalytically important
additional information
-
the N-terminal signal peptide consists of 23 residues bordered with the signal peptidase recognition site Ala-Phe-Ala-Ala
-
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?

-
x * 33000, mature enzyme, SDS-PAGE
?
-
x * 33000, mature enzyme, SDS-PAGE
-
?
-
x * 32926, calculated from amino acid sequence
?
x * 33000, SDS-PAGE, mature elastase
?
-
x * 33000, SDS-PAGE, recombinant protein from Escherichia coli
?
x * 36000, SDS-PAGE, mature elastase
?
x * 51000, SDS-PAGE, precursor form of elastase
?
x * 52000, SDS-PAGE, pro-elastase, enzymatically inactive
?
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
?
-
x * 34160, sequence calculation
?
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
-
?
-
x * 33000, SDS-PAGE
-
?
-
x * 32926, calculated from amino acid sequence
-
?
-
x * 33000, SDS-PAGE, recombinant protein from Escherichia coli
-
?
-
x * 33000, SDS-PAGE
-
?
-
x * 33000, SDS-PAGE
-
?
-
x * 48000, SDS-PAGE
-
additional information

comparison of the 3D structures of PAE and Vibrio cholerae zinc-containing and calcium-stabilized soluble hemagglutinin/protease, HA/P, i.e. vibriolysin, reveals a remarkable similarity having a conserved alpha + beta domain, modelling, overview
additional information
-
comparison of the 3D structures of PAE and Vibrio cholerae zinc-containing and calcium-stabilized soluble hemagglutinin/protease, HA/P, i.e. vibriolysin, reveals a remarkable similarity having a conserved alpha + beta domain, modelling, overview
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D201A
-
site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly decreased activity compared to the wild-type enzyme
R279A
-
site-directed mutagenesis, inactive mutant
R198A
-
site-directed mutagenesis, inactive mutant
H223Y
no proteolytic or elastolytic activity
D168A
-
site-directed mutagenesis, inactive mutant
R205A
-
site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly decreased activity compared to the wild-type enzyme
R179A
-
site-directed mutagenesis, the mutant shows decreased thermal stabilities and increased activities compared to the wild-type enzyme
N212Q
-
site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
D189A
-
site-directed mutagenesis, the mutant shows decreased thermal stabilities and increased activities compared to the wild-type enzyme
R253A
-
site-directed mutagenesis, inactive mutant
H223D
no proteolytic or elastolytic activity
E249A
-
site-directed mutagenesis, the mutant shows both decreased thermal stability and decreased activity compared to the wild-type enzyme
R245A
-
site-directed mutagenesis
N43Q
-
site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
N280Q
-
site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
N212Q/N280Q
-
site-directed mutagenesis, 90.6% decreased activity compared to the wild-type enzyme
N43Q/N212Q/N280Q
-
site-directed mutagenesis, 90.6% decreased activity compared to the wild-type enzyme
N43Q/N212Q
-
site-directed mutagenesis, 68.7% decreased activity compared to the wild-type enzyme
N43Q/N280Q
-
site-directed mutagenesis, 73.6% decreased activity compared to the wild-type enzyme
additional information
-
mutation of any potential N-glycosylation site was detrimental to its expression in Pichia pastoris with 23.9% decrease in expression of the N43Q mutant, 63.6% of the N212Q mutant, and 63.7% of the N280Q mutant compared with the wild type
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benzene
-
25% v/v, 30°C, stable for at least 72 h
chloroform
-
pH 7.0, 30°C, 4 days, 95.6% activity remaining for the nonglycosylated recombinant enzyme, 91.5% for the glycosylated recombinant enzyme
cyclohexane
-
25% v/v, 30°C, stable for at least 72 h
isopropanol
-
pH 7.0, 30°C, 4 days, 39.2% activity remaining for the nonglycosylated recombinant enzyme, 17.5% for the glycosylated recombinant enzyme
Methanol
-
pH 7.0, 30°C, 4 days, 102% activity remaining for the nonglycosylated recombinant enzyme, 96.5% for the glycosylated recombinant enzyme
n-Butanol
-
pH 7.0, 30°C, 4 days, 89.5% activity remaining for the nonglycosylated recombinant enzyme, 78.5% for the glycosylated recombinant enzyme
toluene
-
25% v/v, 30°C, stable for at least 72 h
2-propanol

-
25% v/v, 36% residual activity
2-propanol
-
25% v/v, 36% residual activity
-
2-propanol
WP_084338031.1
25% (v/v), 1 week, stable
2-propanol
-
25% (v/v), 1 week, stable
-
Acetone

-
25% v/v, 31% residual activity
Acetone
-
25% v/v, 31% residual activity
-
Acetone
WP_084338031.1
25% (v/v), 1 week, stable
Acetone
-
25% (v/v), 1 week, stable
-
dimethyl sulfoxide

-
25% v/v, 11% residual activity
dimethyl sulfoxide
-
25% v/v, 11% residual activity
-
DMSO

-
pH 7.0, 30°C, 4 days, 95.1% activity remaining for the nonglycosylated recombinant enzyme, 83.2% for the glycosylated recombinant enzyme
DMSO
WP_084338031.1
25% (v/v), 1 week, stable
Ethanol

-
25% v/v, 24% residual activity
Ethanol
-
pH 7.0, 30°C, 4 days, 71.5% activity remaining for the nonglycosylated recombinant enzyme, 62.1% for the glycosylated recombinant enzyme
Ethanol
-
25% v/v, 24% residual activity
-
Ethanol
WP_084338031.1
25% (v/v), 1 week, stable
Ethanol
-
25% (v/v), 1 week, stable
-
Ethyl acetate

WP_084338031.1
25% (v/v), 1 week, stable
Ethyl acetate
-
25% (v/v), 1 week, stable
-
hexane

-
25% v/v, 30°C, stable for at least 72 h
hexane
WP_084338031.1
25% (v/v), 1 week, stable
hexane
-
25% (v/v), 1 week, stable
-
additional information

-
the enzyme is stable in the presence of organic solvents mainly diethyl ether and DMSO
additional information
-
the enzyme is stable in the presence of organic solvents mainly diethyl ether and DMSO
-
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diagnostics
-
specific protease activity of the enzyme as indicator for the degree of Pseudomonas aeruginosa infection in chronic infected wounds
pharmacology
-
branched antimicrobial peptide M33 pegylation at the C-terminus of the three lysine-branching core with a Peg4 molecule and the resulting increase in stability to Pseudomonas aeruginosa elastase, peptide resistance to this protease is an important feature for M33-Peg activity against Pseudomonas aeruginosa
biotechnology

-
A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin
biotechnology
-
A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin
-
industry

-
A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin
industry
-
pseudolysin is a biotechnologically important enzyme in the tanning industry
industry
potential application in the leather industry and as a therapeutic agent
industry
-
A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin
-
industry
-
potential application in the leather industry and as a therapeutic agent
-
medicine

2-mercaptoacetyl-L-phenylalanyl-L-leucine represents a class of potent elastase inhibitors that might prove useful in the management of Pseudomonas aeruginosa infections
medicine
application of the inhibitors may be helpful in the management of corneal infections with Pseudomonas aeruginosa
medicine
Inflammation and consequent lung dysfunction are hallmarks of recurrent Pseudomonas aeruginosa infections in cystic fibrosis lungs. The continued presence of bacterial components, including PE, can evoke an ongoing host inflammatory response by induction of inflammatory cytokinines and chemokinines such as interleukin-8. Although this cytokinine is essential for an effective host defense, continuous neutrophil transmigration and degranulation will damage the lung tissue through neutrophil-derived proteases. Therefore, the use of specific antibody against Pseudomonas elastase as adjuvant therapy along with antibacterial agents can prove an effective approach in the treatment of chronic Pseudomonas aeruginosa infection.
medicine
-
phosphoramidon, the inhibitor of the enzyme, may prove beneficial in the treatment of Pseudomonas aeruginosa corneal infections
medicine
the inhibitor may have a therapeutic application by delaying the progression of corneal destruction in Pseudomonas keratitis
medicine
-
the inhibitor of the enzyme, 2-mercaptoacetyl-L-phenyalanyl-L-leucine, has therapeutic potential as an adjunct to antibiotics treatment of Pseudomonas keratitis in rabbits
medicine
the protective activity of elastase mutants against Pseudomonas infections may be useful in producing vaccines
medicine
enzyme can silence the function of proteinase-activated receptor-2 in the respiratory tract, thereby altering the host innate defense mechanisms and respiratory functions, and thus contributing to the setting of a disease like cystic fibrosis
medicine
-
Pseudomonas aeruginosa cytotoxic elastase is enhanced in the presence of the filamentous fungi Aspergillus fumigatus, suggesting that this may have a role to play in the damaging pathology associated with the lung tissue in this disease. This indicates that patients who have a co-colonisation with these two organisms may have a poorer prognosis
medicine
-
the enzyme is a promising target for the development of new anti-virulence compounds
nutrition

-
pseudolysin is an enzyme cleaving gluten effectively at extremely low as well as near neutral pH values. The potential to degrade gluten during gastric transport opens possibilities for its application as a therapeutic agent for the treatment of celiac disease
nutrition
-
pseudolysin is an enzyme cleaving gluten effectively at extremely low as well as near neutral pH values. The potential to degrade gluten during gastric transport opens possibilities for its application as a therapeutic agent for the treatment of celiac disease
-
synthesis

-
the Pseudomonas aeruginosa elastase, produced by Pichia pastoris, is a promising biocatalyst for peptide synthesis in organic solvents
synthesis
WP_084338031.1
the enzyme can be applied to obtain bioactive soluble peptides from eggshell-membrane. Potential applicability of its peptides as functional food and cosmetic additives
synthesis
-
the enzyme can be applied to obtain bioactive soluble peptides from eggshell-membrane. Potential applicability of its peptides as functional food and cosmetic additives
-
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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
Black, W.J.; Quinn, F.; Tompkins, L.S.
Legionella pneumophila zinc metalloprotease is structurally and functionally homologous to Pseudomonas aeruginosa elastase
J. Bacteriol.
172
2608-2613
1990
Legionella pneumophila
brenda
Morihara, K.; Tsuzuki, H.
Pseudomonas aeruginosa elastase. Affinity chromatography and some properties as a metalloneutral proteinase
Agric. Biol. Chem.
39
1123-1128
1975
Pseudomonas aeruginosa
-
brenda
Morihara, K.
Pseudolysin and other pathogen endopeptidases of thermolysin family
Methods Enzymol.
248
242-253
1995
Pseudomonas aeruginosa, Vibrio cholerae serotype O1
brenda
Bever, R.A.; Iglewski, B.H.
Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene
J. Bacteriol.
170
4309-4314
1988
Pseudomonas aeruginosa
brenda
Kessler, E.; Safrin, M.; Gustin, J.K.; Ohman, D.E.
Elastase and the LasA protease of Pseudomonas aeruginosa are secreted with their propeptides
J. Biol. Chem.
273
30225-30231
1998
Pseudomonas aeruginosa
brenda
Mariencheck, W.I.; Alcorn, J.F.; Palmer, S.M.; Wright, J.R.
Pseudomonas aeruginosa elastase degrades surfactant proteins A and D
Am. J. Respir. Cell Mol. Biol.
28
528-537
2003
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
brenda
Dulon, S.; Leduc, D.; Cottrell, G.S.; D'Alayer, J.; Hansen, K.K.; Bunnett, N.W.; Hollenberg, M.D.; Pidard, D.; Chignard, M.
Pseudomonas aeruginosa elastase disables proteinase-activated receptor 2 in respiratory epithelial cells
Am. J. Respir. Cell Mol. Biol.
32
411-419
2005
Pseudomonas aeruginosa, Pseudomonas aeruginosa (P14756)
brenda
Besson, C.; Saulnier, J.; Wallach, J.M.
Synthetic peptide substrates for a conductimetric assay of Pseudomonas aeruginosa elastase
Anal. Biochem.
237
216-223
1996
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa