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Enzyme Nomenclature
Information on EC 3.4.24.26 - pseudolysin
for references in articles please use BRENDA:EC3.4.24.26
Word Map on EC 3.4.24.26
- 3.4.24.26
-
metalloproteinases
- thermolysin
- collagenase
- metalloprotease
- elastin
-
elastases
-
pseudomonal
- stromelysin
- phosphoramidon
- medicine
-
intrastromal
-
hageman
- vibriolysin
-
thermolysin-like
-
1-proteinase
-
procollagenase
-
preproenzyme
- industry
- nutrition
- biotechnology
- diagnostics
- pharmacology
- synthesis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.24.26
-
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RECOMMENDED NAME
GeneOntology No.
pseudolysin
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
171715-23-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
exhibits greatly reduced amounts of elastolytic activity
SwissProt
-
31113, 31115, 31116, 31117, 651900, 663600, 664291, 664680, 664681, 665249, 665910, 667880, 669613, 670044, 697198, 699056, 733072, 733746, 733774, 735037, 735209
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-
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663597, 663600, 663610, 663749, 664157, 664238, 664848, 665153, 665156, 665158, 665159, 665160, 665163, 665182, 665250, 665354, 665463, 666225, 666234, 666263, 666382, 666533, 689886, 735268
SwissProt
; exhibits greatly reduced amounts of elastolytic activity
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
the exosecretome of the LasB-deficient pseudomonal strain PAO1lasBDELTA has limited impact on human vascular cell adherence and viability
physiological function
additional information
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 is a metalloprotease belonging to the thermolysin (M4) family proteases
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 belongs to the thermolysin-like family of metallopeptidases
evolution
-
pseudolysin is a Zn2+ metalloprotease of the thermolysin family
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
-
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
-
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
-
the protease is a virulence factor that acts by destroying peptides of the native immune system
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
additional information
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the N-terminal signal peptide consists of 23 residues bordered with the signal peptidase recognition site Ala-Phe-Ala-Ala
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
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the glutamic acid of the HEXXH motif is catalytically important
additional information
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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
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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
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the N-terminal signal peptide consists of 23 residues bordered with the signal peptidase recognition site Ala-Phe-Ala-Ala
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-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
-
-
?
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
-
-
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
alpha1-proteinase inhibitor + H2O
?
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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)
-
-
?
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
-
-
-
-
?
carbobenzooxydialanine-phenylalanylalaninamide + H2O
?
-
30°C, pH 8.6
-
-
?
carbobenzooxydialanine-tyrosylalaninamide + H2O
?
-
30°C, pH 8.6
-
-
?
cartilage + H2O
?
major components proteoglycans and collagen
-
-
?
eggshell membrane + H2O
Val-Leu-Pro-Pro + (X)-Val-Pro-Pro + Trp + ?
-
-
-
-
?
human gamma-interferon + H2O
fragments of human gamma-interferon
-
-
-
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interleukin-8 + H2O
?
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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
?
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37°C
51-kD polypeptide
-
?
myeloma IgA2-lamda of A2m(2) allotype + H2O
?
-
predominantly polymeric, 37°C
-
-
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N-chlorosuccinimide-oxidized inhibitor + H2O
?
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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
-
-
-
-
?
PAR2 + H2O
?
-
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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
-
-
-
-
?
proteinase-activated receptor 2 + H2O
?
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the enzyme cleaves proteinase-activated receptor 2 to remove the extracellular Flag epitope
-
-
?
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
-
-
-
-
?
tear fluid surfactant protein D + H2O
35000 Da fragment of tear fluid surfactant protein D + ?
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purified elastase degrades tear fluid surfactant protein D in vitro and in vivo
-
-
?
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
-
-
-
-
?
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
-
-
-
-
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2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
-
-
-
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azocasein + H2O
?
proteolytic activity is 8 to 9fold lower than in the wild-type strain
-
-
?
elastase propeptide + H2O
elastase + ?
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autocatalytically cleaved
-
?
elastase propeptide + H2O
elastase + ?
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autocatalytically cleaved
-
?
Elastin + H2O
?
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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
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
-
poor substrate
-
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furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
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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
-
-
?
myeloma IgA1-kappa + H2O
?
-
predominantly monomeric, 37°C
-
-
-
myeloma IgA1-kappa + H2O
?
-
predominantly polymeric, 37°C
-
-
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N-succinyl-L-(Ala)3-p-nitroanilide + H2O
?
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36°C, pH 7.5
-
-
?
additional information
?
-
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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
?
-
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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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
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
?
-
-
probably responsible for the tissue destruction observed during pulmonary and corneal infections by the pathogen organism Pseudomonas aeruginosa
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
a calcium ion is also required for enzyme activity, and stabilizes its tertiary structure. Contact with the calcium ion is made by the carboxyl groups of Asp136, Glu172, Glu175, and Asp183, the carbonyl group of Leu185, and one water molecule
Zinc
Zn2+
additional information
Zinc
-
contains 1 atom Zn per molecule; contains zinc; essential for activity
Zn2+
-
the enzyme has a catalytic zinc ion at the active site cleft with a tetrahedral coordination formed by the two histidines of a HEXXH motif, and a glutamic acid located 18-72 residues C-terminal of the HEXXH motif. The fourth zinc coordinating ligand in the free enzyme is a water molecule
Zn2+
-
PAE contains zinc, binding site structure, HEXXH is the putative signature of Zn-metalloproteases, overview
Zn2+
-
the enzyme is a metalloprotease that requires a zinc atom, bound to His140, His144, and Glu164, for its activity
additional information
-
Mg2+ and Ca2+ at 0.625 mM have no effect on the activity, Mn2+, Co2+, and Fe3+ at 0.625 mM partly inhibit the enzyme, Zn2+ and Cu2+ inhibit the enzyme completely
additional information
-
metalloprotease, the enzynme contains the typical metalloendopeptidases consensus zinc-binding sequence HEXXH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoacetyl-L-phenylalanyl-L-leucine
-
prevents corneal perforation completely
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-[(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)
-
-
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-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
D-glucose
extracellular elastase activity decreases if cells are cultured in the presence of glucose
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-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
-
-
peptides
-
containing the hydroxamic acid, N-hydroxypeptide and thiol functional groups
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
-
[(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
-
-
phosphoramidon
-
N-(alpha-rhamnopyranosyloxyhydroxyphosphinyl)-Leu-Trp
phosphoramidon
-
N-(alpha-L-rhamnopyranosyloxyhydroxyphosphinyl)-L-leucyl-L-tryptophan
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
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
-
diisopropyl fluorophosphate; not: ClCH2CO-N-hydroxyleucine-OCH3; tosyl-L-Phe chloromethyl ketone, PCMB
-
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
-
no inhibition by dithio-bis(nitrobenzoic acid) and phenylmethylsulfonyl fluoride, and by K+ and Na+
-
additional information
-
N-alpha mercaptoamide-containing dipeptides as inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no stimulation by ceftazidime and gentamycin
-
additional information
-
the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
Benzyloxycarbonyl-Gly-Leu-Ala
-
benzyloxycarbonyl-Gly-Leu-Leu, benzyloxycarbonyl-Phe-Leu-Ala
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
1.1
Leu-Phe
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
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
-
-
0.0003
slowly eluting isomer of HSCH2(DL)CH[CH2CH(CH3)2]CO-Phe-Ala-NH2
-
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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)
0.082 - 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
0.33
[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
0.0028
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.2
-
purified recombinant enzyme from Escherichia coli expression, pH 8.0, 25°C, substrate N-succinyl-Ala-Ala-Ala-4-nitroanilide
2389
-
recombinant glycosylated enzyme, pH 7.5, 60°C, substrate casein
2401
-
recombinant nonglycosylated enzyme, pH 7.5, 60°C, substrate casein
additional information
additional information
-
development and evaluation of a highly sensitive assay based on internally quenched fluorogenic peptide substrates comprising an edans (5-(2-aminoethylamino)-1-naphthalenesulfonic acid) group at the C-terminus and a dabsyl (4-(dimethylamino)azobenzene-4'-sulfonyl chloride) fluorophore at the N-terminus of the peptide chains, overview
additional information
-
chronic wound fluid samples from infected human subjects, pH 7.3
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
-
with 2-aminobenzoyl-Ala-Gly-Leu-Ala-4-nitrobenzylamide as substrate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7
-
no activity at pH 2.0, the enzyme can resist and be active at low pH values e.g. in the human stomach
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
mutants E141D, E141Q, E141G, H223G, H223E, and H223L
additional information
-
in the sputum of patients infected with Pseudomonas aeruginosa
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
33030
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
34000
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
35000
36000
51000
53600
53610
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
33000
-
x * 33000, SDS-PAGE, recombinant protein from Escherichia coli
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
?
x * 33000, SDS-PAGE, mature elastase; x * 51000, SDS-PAGE, precursor form of elastase
?
-
x * 32926, calculated from amino acid sequence; x * 33000, SDS-PAGE, recombinant protein from Escherichia coli
?
-
x * 36000, SDS-PAGE, mature 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 * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the recombinant elastase contains three potential N-glycosylation sites N43, N212, and N280 (Asn-Xaa-Ser/Thr consensus sequences), potential role of N-glycosylation in the activity and stability. 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. The N-linked oligosaccharides of Pichia pastoris-secreted glycoproteins are a high-mannose type (Man8GlcNAc2 or Man9GlcNAc2) with molecular weights close to 2 kDa
proteolytic modification
proteolytic modification
-
the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids
proteolytic modification
-
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
proteolytic modification
-
the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in the presence of inhibitors S-homoPhe [N-alpha-alpha]Phe-IsoAsn, phosphoramidon, and ClCH2CO-HOLeu-Ala-Gly-NH2
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
-
purified enzyme, 60 min, loss of 30% activity at pH 5.0 and of 50% at pH 11.0, completely stable at pH 6.0-10.0, profile overview
717673
6 - 9.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
60
70
30 - 60
-
purified enzyme, completely stable at 30°C and 40°C after 60 min, A2 protease retains about 80% and 60% of its initial activity after incubation for 60 min at 50°C and 60°C, respectively
70
-
half-lives of the glycosylated and non-glycosylated forms of recombinant enzyme are 32.2 and 23.1 min, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the first and second disulfide bonds are essential for the stability and activity of the enzyme, respectively
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-propanol
Acetone
chloroform
-
pH 7.0, 30°C, 4 days, 95.6% activity remaining for the nonglycosylated recombinant enzyme, 91.5% for the glycosylated recombinant enzyme
dimethyl sulfoxide
DMSO
-
pH 7.0, 30°C, 4 days, 95.1% activity remaining for the nonglycosylated recombinant enzyme, 83.2% for the glycosylated recombinant enzyme
Ethanol
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
additional information
Ethanol
-
pH 7.0, 30°C, 4 days, 71.5% activity remaining for the nonglycosylated recombinant enzyme, 62.1% for the glycosylated recombinant enzyme
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.02 M Tris-hydrochloride, 0.5 mM CaCl2 (pH 7.5), 1 year, less than 10% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
-
native enzyme 2.23fold to homogeneity by ultrafiltration, gel filtration, and anion exchange chromatography
-
native extracellular enzyme from cell culture medium by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and cation exchange chromatography
-
native extracellular enzyme from culture supernatant by anion exchange chromatography and ultrafiltration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by ammonium sulfate fractionation, anion exchange chromatography
-
solubilized recombinant His-tagged enzyme from Escherichia coli cells by metal affinity chromatography, or the enzyme is simultaneously further purified, refolded and buffer-exchanged on a preparative Superdex 200 column by a modified urea reverse-gradient gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; expression in Escherichia coli
expression of mutants E141D, E141Q, E141G, H223G, H223E, and H223L in Escherichia coli JM109
gene lasB, recombinant expression in Escherichia coli and in Pichia pastoris and secretion of the enzyme, large-scale expression of His-tagged enzyme under the control of the T7 promoter in Escherichia coli strain BL21(DE3) in inclusion bodies
-
recombinant enzyme expression in Pichia pastoris with heterogeneous N-glycosylation, expression of enzyme glycosylation site mutants
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D189A
-
site-directed mutagenesis, the mutant shows decreased thermal stabilities and increased activities compared to the wild-type enzyme
D201A
-
site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly decreased activity compared to the wild-type enzyme
E249A
-
site-directed mutagenesis, the mutant shows both decreased thermal stability and decreased activity 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
N212Q/N280Q
-
site-directed mutagenesis, 90.6% decreased activity 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
N43Q
-
site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
N43Q/N212Q
-
site-directed mutagenesis, 68.7% 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/N280Q
-
site-directed mutagenesis, 73.6% 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
R205A
-
site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly 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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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
solubilization of recombinant His-tagged enzyme from strain BL21(DE3) in inclusion bodies by 8 M urea
-
the recombinant protein is denatured with guanidine-HCl; the recombinant protein is denatured with guanidine-HCl
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
diagnostics
-
specific protease activity of the enzyme as indicator for the degree of Pseudomonas aeruginosa infection in chronic infected wounds
industry
medicine
nutrition
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
synthesis
-
the Pseudomonas aeruginosa elastase, produced by Pichia pastoris, is a promising biocatalyst for peptide synthesis in organic solvents
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
-
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
-
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
the inhibitor may have a therapeutic application by delaying the progression of corneal destruction in Pseudomonas keratitis
medicine
-
phosphoramidon, the inhibitor of the enzyme, may prove beneficial in the treatment of Pseudomonas aeruginosa corneal infections
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
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
the protective activity of elastase mutants against Pseudomonas infections may be useful in producing vaccines
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
-
application of the inhibitors may be helpful in the management of corneal infections with Pseudomonas aeruginosa
nutrition
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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
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.24.26)
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