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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
-
-
?
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)
-
-
?
BODIPY-casein + 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
-
-
?
elastin Congo red + H2O
?
elastin-agarose + H2O
?
-
-
-
?
elastin-Congo red
?
-
-
-
?
elastin-fluorescein
?
37°C
-
-
?
Fe2-transferrin + H2O
?
25°C, pH 7.4
-
-
?
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
pH 7.5, 23-25°C
-
-
?
furylacryloyl-glycyl-L-leucyl-L-alanine + H2O
furylacryloyl-glycine + L-leucyl-L-alanine
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 A + H2O
?
-
-
-
?
immunoglobulin G + H2O
?
-
-
-
?
monocyte-derived alpha1-antitrypsin + H2O
?
37°C
51-kD polypeptide
-
?
N-chlorosuccinimide-oxidized inhibitor + H2O
?
25°C, pH 7.4, cleavage occurs between Glu354 and Ala355
-
-
?
pentaalanine + H2O
?
30°C, pH 8.6
-
-
?
pentaalanine + H2O
Ala-Ala + Ala-Ala-Ala
-
-
-
?
proteinase-activated receptor 2 + H2O
?
the enzyme cleaves proteinase-activated receptor 2 to remove the extracellular Flag epitope
-
-
?
secretory immunoglobulin A + H2O
?
-
-
-
?
surfactant protein A + H2O
?
37°C
-
-
?
surfactant protein D + H2O
?
37°C
-
-
?
tetraalanine + H2O
?
30°C, pH 8.6
-
-
?
tetraalanine + H2O
Ala-Ala + Ala-Ala
-
-
-
?
transferrin
?
25°C, pH 7.4
-
-
?
unnicked heat-labile enterotoxin + H2O
?
-
-
-
?
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
3-(2-furylacryloyl)glycyl-L-leucine amide + H2O
?
-
-
-
-
?
AAF-7-amido-4-methylcoumarin + H2O
AAF + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-L-alanyl-L-alanyl-L-alanine-methyl ester + H2O
?
-
-
-
-
?
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
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
carbobenzoxy-Gly-Tyr-NH2 + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
colostral S-IgA + 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 + ?
-
-
-
-
?
elastase propeptide + H2O
elastase + ?
-
autocatalytically cleaved
-
?
elastin Congo red + H2O
?
elastin-orcin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
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
-
?
Gelatin + H2O
?
-
-
-
-
?
hide powder azure + H2O
?
-
pH 7.0
-
-
?
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
-
-
-
-
?
myeloma IgA1-kappa + H2O
?
myeloma IgA2-lamda of A2m(2) allotype + H2O
?
-
predominantly polymeric, 37°C
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-(Ala)3-p-nitroanilide + H2O
?
-
36°C, pH 7.5
-
-
?
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
-
?
PFR-7-amido-4-methylcoumarin + H2O
PFR + 7-amino-4-methylcoumarin
-
-
-
-
?
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
-
-
-
-
?
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
?
-
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
37°C
-
-
?
azocasein + H2O
?
37°C, pH 8.0
-
-
?
azocasein + H2O
?
pH 7.5, 37°C
-
-
?
azocasein + H2O
?
proteolytic activity is 8 to 9fold lower than in the wild-type strain
-
-
?
casein + H2O
?
-
-
-
?
casein + H2O
?
pH 7.4, 40°C
-
-
?
Elastin + H2O
?
-
-
-
?
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 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, 37°C
-
-
?
elastin Congo red + H2O
?
pH 8.0
-
-
?
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
-
-
?
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
-
-
?
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
?
-
37°C
-
-
?
azocasein + H2O
?
-
pH 7.5, 37°C
-
-
?
casein + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
-
-
-
?
Elastin + H2O
?
-
37°C
-
-
?
elastin Congo red + H2O
?
-
-
-
-
?
elastin Congo red + H2O
?
-
pH 7.0
-
-
?
myeloma IgA1-kappa + H2O
?
-
predominantly monomeric, 37°C
-
-
?
myeloma IgA1-kappa + H2O
?
-
predominantly polymeric, 37°C
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
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1,10-phenanthroline
non-specific
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
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
-
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
-
ClCH2CO-HOLeu-Ala-Gly-NH2
non-competitive
D-glucose
extracellular elastase activity decreases if cells are cultured in the presence of glucose
HSCH2(DL)CH[CH2CH(CH3)2]CO-Phe-Ala-NH2
2 isomeric forms
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
phosphoryl-L-leucyl-L-phenylalanine
S-homoPhe [N-alpha-alpha]Phe-IsoAsn
L-155542, competitive
specific polyclonal rabbit antielastase antiserum
-
-
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-mercaptoethanol
-
18.8% inhibition at 5 mM
Aprotinin
-
markedly decreases enzymatic activity
Ba2+
-
5 mM, slightly decreases activity
Cd2+
-
5 mM, decreases activity
cetyltrimethylammonium bromide
-
0.1%, 53% residual activity
ClCH2CO-N-hydroxyleucine-Ala-Gly-NH2
-
-
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
L-cysteine
-
complete inhibition at 1.25 mM
N-aryl mercaptoacetamide
-
-
N-mercaptoacetyl-Phe-Tyr-amide
-
-
Na2 EDTA
-
complete inhibition at 10 mM
o-phenanthroline
-
1 mM, 16% residual activity
peptides
-
containing the hydroxamic acid, N-hydroxypeptide and thiol functional groups
PMSF
-
markedly decreases enzymatic activity
sodium dodecylsulfate
-
0.1%, 61% residual activity
Soybean trypsin inhibitor
-
markedly decreases enzymatic activity
-
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
EDTA
-
phosphoramidon
-
phosphoramidon
N-(alpha-rhamnopyranosyloxyhydroxyphosphinyl)-Leu-Trp
phosphoryl-L-leucyl-L-phenylalanine
-
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
1,10-phenanthroline
-
-
1,10-phenanthroline
-
slight inhibition
1,10-phenanthroline
-
1 mM, complete inhibition
1,10-phenanthroline
-
complete inhibition at 1 mM
1,10-phenanthroline
-
5 mM, 0% residual activity
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+
-
complete inhibition at 5 mM
Cu2+
-
5 mM, 21% residual activity
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
EGTA
-
-
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
phosphoramidon
-
-
phosphoramidon
-
N-(alpha-L-rhamnopyranosyloxyhydroxyphosphinyl)-L-leucyl-L-tryptophan
phosphoramidon
-
1 mM, 10% residual activity
phosphoramidon
-
powerful inhibition action on pseudolysin
Zn2+
-
slight inhibition
Zn2+
-
complete inhibition
Zn2+
-
complete inhibition at 10 mM
Zn2+
-
complete inhibition at 5 mM
Zn2+
-
5 mM, 63% residual activity
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 gentamicin
-
additional information
-
no inhibition by gentamicin
-
additional information
N-alpha mercaptoamide-containing dipeptides as inhibitors
-
additional information
-
N-alpha mercaptoamide-containing dipeptides as inhibitors
-
additional information
-
diisopropyl fluorophosphate
-
additional information
-
tosyl-L-Phe chloromethyl ketone, PCMB
-
additional information
-
not: ClCH2CO-N-hydroxyleucine-OCH3
-
additional information
-
not: ClCH2CO-N-hydroxyleucine-OCH3
-
additional information
-
no inhibition by diisopropylphosphofluoridate at 20 mM
-
additional information
-
no inhibition by dithio-bis(nitrobenzoic acid) and phenylmethylsulfonyl fluoride, and by K+ and Na+
-
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brenda
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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A comprehensive alanine-scanning mutagenesis study reveals roles for salt bridges in the structure and activity of Pseudomonas aeruginosa elastase
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High-level expression of pseudolysin, the extracellular elastase of Pseudomonas aeruginosa, in Escherichia coli and its purification
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2015
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brenda
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20
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2019
Pseudomonas aeruginosa
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Bioprocess technology for LasB protease (elastase) production from Pseudomonas aeruginosa MCCB 123
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2018
Pseudomonas aeruginosa (G1EMI7), Pseudomonas aeruginosa MCCB 123 (G1EMI7)
-
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Casilag, F.; Lorenz, A.; Krueger, J.; Klawonn, F.; Weiss, S.; Haeussler, S.
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2019
Pseudomonas aeruginosa (A7LI11)
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Isolation of a putative virulence agent, cytotoxic serine-elastase, from a newly isolated Pseudomonas aeruginosa ZuhP13
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Smith, K.; Rajendran, R.; Kerr, S.; Lappin, D.F.; Mackay, W.G.; Williams, C.; Ramage, G.
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van der Plas, M.J.; Bhongir, R.K.; Kjellstroem, S.; Siller, H.; Kasetty, G.; Moergelin, M.; Schmidtchen, A.
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