Information on EC 3.4.24.26 - pseudolysin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.26
-
RECOMMENDED NAME
GeneOntology No.
pseudolysin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
171715-23-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene lasB
-
-
Manually annotated by BRENDA team
gene lasB
-
-
Manually annotated by BRENDA team
strain 1244
SwissProt
Manually annotated by BRENDA team
isolated from marine water in Sfax city, Tunisia, gene lasB
-
-
Manually annotated by BRENDA team
strain IFO 3455
SwissProt
Manually annotated by BRENDA team
IFO3455
SwissProt
Manually annotated by BRENDA team
strain ME-4
-
-
Manually annotated by BRENDA team
strain PA-28
SwissProt
Manually annotated by BRENDA team
strain PA01
-
-
Manually annotated by BRENDA team
strain PA103
SwissProt
Manually annotated by BRENDA team
strain PAO-E64, exhibits greatly reduced amounts of elastolytic activity
SwissProt
Manually annotated by BRENDA team
strain SES-938-1
SwissProt
Manually annotated by BRENDA team
similar enzyme produced by Vibrio cholerae
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
show the reaction diagram
2-aminobenzoyl-Ala-Gly-Leu-Ala-4-nitrobenzylamide + H2O
?
show the reaction diagram
-
25C, pH 7.4
-
-
?
3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine + H2O
L-phenylalanyl-L-phenylalanine + 3-(2-furyl)acryloyl-glycine
show the reaction diagram
-
at 37C, pH 7.3
-
-
?
3-(2-furylacryloyl)glycyl-L-leucine amide + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4-yl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
?
show the reaction diagram
-
-
-
-
-
AAF-7-amido-4-methylcoumarin + H2O
AAF + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Abz-Ala-Gly-Leu-Ala-4-nitrobenzylamide + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
acetyl-L-alanyl-L-alanyl-L-alanine-methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala-Ala-Phe-Ala + H2O
?
show the reaction diagram
-
30C, pH 8.6
-
-
?
Ala-Ala-Phe-Ala-NH2 + H2O
?
show the reaction diagram
-
30C, pH 8.6
-
-
?
alpha1-proteinase inhibitor + H2O
?
show the reaction diagram
-
25C, 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)
-
-
?
azocasein + H2O
?
show the reaction diagram
Benzyloxycarbonyl-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-Leu-Gly + H2O
?
show the reaction diagram
-
-
-
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-
Benzyloxycarbonyl-Gly-Leu-Leu + H2O
?
show the reaction diagram
-
-
-
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Benzyloxycarbonyl-Gly-Leu-NH2 + H2O
?
show the reaction diagram
-
-
-
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-
Benzyloxycarbonyl-Gly-Leu-Phe + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-Phe-NH2 + H2O
?
show the reaction diagram
-
-
-
-
-
Boc-GKR-7-amido-4-methylcoumarin + H2O
Boc-GKR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Boc-QAR-7-amido-4-methylcoumarin + H2O
Boc-QAR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Boc-VLK-7-amido-4-methylcoumarin + H2O
Boc-VLK + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Boc-VPR-7-amido-4-methylcoumarin + H2O
Boc-VPR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
BODIPY-casein + H2O
?
show the reaction diagram
-
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
carbobenzooxydialanine-leucylalaninamide + H2O
?
show the reaction diagram
-
30C, pH 8.6
-
-
?
carbobenzooxydialanine-phenylalanylalaninamide + H2O
?
show the reaction diagram
-
30C, pH 8.6
-
-
?
carbobenzooxydialanine-tyrosylalaninamide + H2O
?
show the reaction diagram
-
30C, pH 8.6
-
-
?
carbobenzoxy-Gly-Leu-NH2 + H2O
?
show the reaction diagram
-
-
-
?
carbobenzoxy-Gly-Phe-NH2 + H2O
?
show the reaction diagram
-
-
-
?
carbobenzoxy-Gly-Tyr-NH2 + H2O
?
show the reaction diagram
cartilage + H2O
?
show the reaction diagram
major components proteoglycans and collagen
-
-
?
casein + H2O
?
show the reaction diagram
Collagen + H2O
?
show the reaction diagram
Collagen IV + H2O
?
show the reaction diagram
-
37C
-
-
?
colostral S-IgA + H2O
?
show the reaction diagram
dabsyl-Ala-Ala-Phe-Ala-EDANS + H2O
?
show the reaction diagram
Denatured casein + H2O
?
show the reaction diagram
-
-
-
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Denatured fibrin + H2O
?
show the reaction diagram
-
-
-
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-
Denatured hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
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Denatured ovalbumin + H2O
?
show the reaction diagram
-
-
-
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-
eggshell membrane + H2O
Val-Leu-Pro-Pro + (X)-Val-Pro-Pro + Trp + ?
show the reaction diagram
-
-
-
-
?
elastase propeptide + H2O
elastase + ?
show the reaction diagram
Elastin + H2O
?
show the reaction diagram
elastin Congo red + H2O
?
show the reaction diagram
elastin-agarose + H2O
?
show the reaction diagram
-
-
-
-
?
elastin-Congo red
?
show the reaction diagram
-
-
-
?
elastin-fluorescein
?
show the reaction diagram
-
37C
-
-
?
elastin-orcin + H2O
?
show the reaction diagram
-
-
-
-
?
Fe2-transferrin + H2O
?
show the reaction diagram
-
25C, pH 7.4
-
-
?
Fibrin + H2O
?
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Ala-Leu-Ala + H2O
?
show the reaction diagram
-
pH 8.0, 30C
-
-
?
furylacryloyl-Ala-Leu-Gly + H2O
?
show the reaction diagram
-
pH 8.0, 30C
-
-
?
furylacryloyl-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
pH 8.0, 30C
-
-
?
furylacryloyl-Gly-Leu-Gly + H2O
?
show the reaction diagram
-
pH 8.0, 30C
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
show the reaction diagram
furylacryloyl-glycyl-L-leucyl-L-alanine + H2O
furylacryloyl-glycine + L-leucyl-L-alanine
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gliadin + H2O
?
show the reaction diagram
gluten + H2O
?
show the reaction diagram
hide powder azure + H2O
?
show the reaction diagram
hog gastric mucin + H2O
?
show the reaction diagram
-
-
-
-
?
human alpha-1 proteinase inhibitor + H2O
?
show the reaction diagram
-
-
-
?
human collagen + H2O
?
show the reaction diagram
-
-
-
?
human fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
human gamma-interferon + H2O
fragments of human gamma-interferon
show the reaction diagram
-
-
-
-
human lactoferrin + H2O
?
show the reaction diagram
-
-
-
-
?
human plasma alpha1-proteinase inhibitor + H2O
?
show the reaction diagram
-
-
-
-
?
human type III collagen + H2O
?
show the reaction diagram
-
25C
-
-
?
human type IV collagen + H2O
?
show the reaction diagram
-
25C
-
-
?
immunoglobulin A + H2O
?
show the reaction diagram
immunoglobulin G + H2O
?
show the reaction diagram
-
-
-
?
interleukin-6 + H2O
?
show the reaction diagram
-
complete digestion
-
-
?
interleukin-8 + H2O
?
show the reaction diagram
-
rapid processing to a 72 amino acid form, further degradation is slow
-
-
?
Laminin + H2O
?
show the reaction diagram
methyl-O-Suc-AAPV-7-amido-4-methylcoumarin + H2O
methyl-O-Suc-AAPV + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
monocyte-derived alpha1-antitrypsin + H2O
?
show the reaction diagram
-
37C
51-kD polypeptide
-
?
myeloma IgA1-kappa + H2O
?
show the reaction diagram
myeloma IgA2-lamda of A2m(2) allotype + H2O
?
show the reaction diagram
predominantly polymeric, 37C
-
-
-
N-chlorosuccinimide-oxidized inhibitor + H2O
?
show the reaction diagram
-
25C, pH 7.4, cleavage occurs between Glu354 and Ala355
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-L-(Ala)3-p-nitroanilide + H2O
?
show the reaction diagram
orcein-elastin + H2O
?
show the reaction diagram
-
-
-
-
?
ovalbumin + H2O
?
show the reaction diagram
-
-
-
-
?
ovomucin + H2O
?
show the reaction diagram
-
-
-
-
?
PAR-1 peptide + H2O
?
show the reaction diagram
-
cleavage at the R41-S42 site
-
-
?
PAR-2 peptide + H2O
?
show the reaction diagram
-
cleavage at the R36-S37 site
-
-
-
PAR-4 peptide + H2O
?
show the reaction diagram
-
cleavage at the R47-G48 site
-
-
-
PAR2 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
30C, pH 8.6
-
-
?
pentaalanine + H2O
Ala-Ala + Ala-Ala-Ala
show the reaction diagram
-
-
-
-
?
PFR-7-amido-4-methylcoumarin + H2O
PFR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
proteinase-activated receptor 2 + H2O
?
show the reaction diagram
the enzyme cleaves proteinase-activated receptor 2 to remove the extracellular Flag epitope
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-
?
secretory immunoglobulin A + H2O
?
show the reaction diagram
-
-
-
?
skim milk
?
show the reaction diagram
-
-
-
-
?
Suc-AAF-7-amido-4-methylcoumarin + H2O
Suc-AAF + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Suc-AFK-7-amido-4-methylcoumarin + H2O
Suc-AFK + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Suc-GPLGP-7-amido-4-methylcoumarin + H2O
Suc-GPLGP + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Suc-IIW-7-amido-4-methylcoumarin + H2O
Suc-IIW + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Suc-LLVY-7-amido-4-methylcoumarin + H2O
Suc-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
surfactant protein A + H2O
?
show the reaction diagram
37C
-
-
?
surfactant protein D + H2O
?
show the reaction diagram
37C
-
-
?
tear fluid surfactant protein D + H2O
35000 Da fragment of tear fluid surfactant protein D + ?
show the reaction diagram
-
purified elastase degrades tear fluid surfactant protein D in vitro and in vivo
-
-
?
tetraalanine + H2O
?
show the reaction diagram
-
30C, pH 8.6
-
-
?
tetraalanine + H2O
Ala-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
?
transferrin
?
show the reaction diagram
-
25C, pH 7.4
-
-
?
unnicked heat-labile enterotoxin + H2O
?
show the reaction diagram
-
-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Z-AAN-7-amido-4-methylcoumarin + H2O
Z-AAN + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-GAH-7-amido-4-methylcoumarin + H2O
Z-GAH + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-GAM-7-amido-4-methylcoumarin + H2O
Z-GAM + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-GGL-7-amido-4-methylcoumarin + H2O
Z-GGL + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-GGR-7-amido-4-methylcoumarin + H2O
Z-GGR + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-LLE-7-amido-4-methylcoumarin + H2O
Z-LLE + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Z-RLRGG-7-amido-4-methylcoumarin + H2O
Z-RLRGG + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
Elastin + H2O
?
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Gliadin + H2O
?
show the reaction diagram
gluten + H2O
?
show the reaction diagram
PAR2 + H2O
?
show the reaction diagram
P14756
-
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
-
?
Vitronectin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
Mn2+
inhibits activity at 10 mM
Ni2+
inhibits activity at 10 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
1,4-dithiothreitol
-
5 mM, 0% residual activity
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
-
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
-
Cetyltrimethylammonium bromide
-
0.1%, 53% residual activity
ClCH2CO-HOLeu-Ala-Gly-NH2
-
non-competitive
ClCH2CO-N-hydroxyleucine-Ala-Gly-NH2
-
-
Co2+
-
50% inhibition at 0.625 mM
D-glucose
extracellular elastase activity decreases if cells are cultured in the presence of glucose
EGTA
inhibition to a lesser extent than with EDTA
elastase propeptide
-
-
-
Fe3+
-
75% inhibition at 0.625 mM
Hg2+
-
complete inhibition at 5 mM
HSCH2(DL)CH[CH2CH(CH3)2]CO-Phe-Ala-NH2
2 isomeric forms
L-cysteine
-
complete inhibition at 1.25 mM
L-phenylalanyl-L-phenylalanine
-
-
N-(1-carboxy-3-phenylpropyl)-phenylalanyl-alpha-asparagine
-
enzyme binding structure analysis, PDB ID 1U4G. The inhibitor is bound in the S1-S1 sub-sites of pseudolysin by hydrogen bonding and hydrophobic and weak van der Waal's interactions
-
N-[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]-N-[(4-phenoxyphenyl)sulfonyl]glycine
-
-
Na2 EDTA
-
complete inhibition at 10 mM
o-phenanthroline
peptides
-
containing the hydroxamic acid, N-hydroxypeptide and thiol functional groups
Phosphoramidate
-
-
phosphoramidon
phosphoryl-L-leucyl-L-phenylalanine
S-homoPhe [N-alpha-alpha]Phe-IsoAsn
-
L-155542, competitive
sodium dodecylsulfate
-
0.1%, 61% residual 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
-
Zincov
-
zinc chelator
[(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
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
erythromycin
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide
1.4
3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine
-
-
1.8
Benzyloxycarbonyl-Gly-Leu-Ala
-
benzyloxycarbonyl-Gly-Leu-Leu, benzyloxycarbonyl-Phe-Leu-Ala
2.8
Benzyloxycarbonyl-Gly-Leu-Gly
-
-
6.4
Benzyloxycarbonyl-Gly-Leu-NH2
-
-
1
benzyloxycarbonyl-Gly-Leu-Phe
-
-
2.1
Benzyloxycarbonyl-Gly-Phe-NH2
-
-
2
Benzyloxycarbonyl-Gly-Tyr-NH2
-
-
0.09
carbobenzooxydialanine-leucylalaninamide
-
-
0.12
carbobenzooxydialanine-phenylalanylalaninamide
-
-
0.38
carbobenzooxydialanine-tyrosylalaninamide
-
-
0.065
dabsyl-Ala-Ala-Phe-Ala-EDANS
-
-
1.08
dialanine-phenylalanylalaninamide
-
-
0.16
furylacryloyl-Ala-Leu-Ala
-
-
0.18
furylacryloyl-Ala-Leu-Gly
-
-
0.21
furylacryloyl-Gly-Leu-Ala
-
-
0.23
furylacryloyl-Gly-Leu-Gly
-
-
0.94 - 4.4
pentaalanine
4.4 - 10.6
tetraalanine
0.37
trialanine-phenylalanylalanine
-
-
additional information
casein
-
Km-value is 2.7 mg/ml
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
100
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide
Pseudomonas aeruginosa
-
-
240
3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine
Pseudomonas aeruginosa
-
-
1100
benzyloxycarbonyl-Ala-Leu-Ala
Pseudomonas aeruginosa
-
-
945
Benzyloxycarbonyl-Gly-Leu-Ala
Pseudomonas aeruginosa
-
-
46.2
Benzyloxycarbonyl-Gly-Leu-Gly
Pseudomonas aeruginosa
-
-
890
Benzyloxycarbonyl-Gly-Leu-Leu
Pseudomonas aeruginosa
-
-
23
Benzyloxycarbonyl-Gly-Leu-NH2
Pseudomonas aeruginosa
-
-
640
benzyloxycarbonyl-Gly-Leu-Phe
Pseudomonas aeruginosa
-
-
47.6
Benzyloxycarbonyl-Gly-Phe-NH2
Pseudomonas aeruginosa
-
-
17.4
Benzyloxycarbonyl-Gly-Tyr-NH2
Pseudomonas aeruginosa
-
-
247
Benzyloxycarbonyl-Phe-Leu-Ala
Pseudomonas aeruginosa
-
-
190 - 406.8
carbobenzooxydialanine-leucylalaninamide
1032
carbobenzooxydialanine-phenylalanylalaninamide
Pseudomonas aeruginosa
-
-
338.2
carbobenzooxydialanine-tyrosylalaninamide
Pseudomonas aeruginosa
-
-
618
dabsyl-Ala-Ala-Phe-Ala-EDANS
Pseudomonas aeruginosa
-
-
540
dialanine-phenylalanylalaninamide
Pseudomonas aeruginosa
-
-
144
furylacryloyl-Ala-Leu-Ala
Pseudomonas aeruginosa
-
-
34
furylacryloyl-Ala-Leu-Gly
Pseudomonas aeruginosa
-
-
95
furylacryloyl-Gly-Leu-Ala
Pseudomonas aeruginosa
-
-
7
furylacryloyl-Gly-Leu-Gly
Pseudomonas aeruginosa
-
-
224.4 - 420
pentaalanine
106 - 250
tetraalanine
769.6
trialanine-phenylalanylalanine
Pseudomonas aeruginosa
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034
2-mercaptoacetyl-Leu-Dphe
at pH 7.5 and 25C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0015
2-mercaptoacetyl-Leu-Phe
at pH 7.5 and 25C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0002
2-mercaptoacetyl-Phe-Leu
at pH 7.5 and 25C, 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 25C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
6.2
benzyloxycarbonyl-L-leucine
at pH 7.5 and 25C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
5
benzyloxycarbonyl-L-phenylalanine
at pH 7.5 and 25C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.011
benzyloxycarbonyl-Leu-NHOH
at pH 7.5 and 25C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.021
benzyloxycarbonyl-Phe-NHOH
at pH 7.5 and 25C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
1.5
L-phenylalanyl-L-phenylalanine
-
-
1.1
Leu-Phe
at pH 7.5 and 25C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.4
Phe-Leu
at pH 7.5 and 25C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0002
phosphoryl-L-leucyl-L-phenylalanine
at pH 7.5 and 25C, 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
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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, 37C, 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, 37C, 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, 37C, 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, 37C, 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, 37C, 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, 37C, 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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2
-
purified recombinant enzyme from Escherichia coli expression, pH 8.0, 25C, substrate N-succinyl-Ala-Ala-Ala-4-nitroanilide
6.4
-
pH 8.0, 30C
2389
-
recombinant glycosylated enzyme, pH 7.5, 60C, substrate casein
2401
-
recombinant nonglycosylated enzyme, pH 7.5, 60C, substrate casein
81100
-
purified enzyme, pH 8.0, 37C
99610
-
60C, pH 8.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
with 2-aminobenzoyl-Ala-Gly-Leu-Ala-4-nitrobenzylamide as substrate
6
-
with the native alpha1-proteinase inhibitor as substrate
6.5
-
with the recombinant mutant M358L inhibitor as substrate
7 - 8
-
casein, elastin
7
-
with N-chlorosuccinimide-oxidized inhibitor as substrate
additional information
-
an endopeptidase active at neutral pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
5 - 10
-
activity range, profile overview
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 80
-
activity range, profile overview
32
the enzyme is less active at temperatures above 32C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.88
-
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
mutants E141D, E141Q, E141G, H223G, H223E, and H223L
Manually annotated by BRENDA team
additional information
-
in the sputum of patients infected with Pseudomonas aeruginosa
-
Manually annotated by BRENDA team
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18530
mass spectrometry
25000
subunit, SDS-PAGE
30000
-
SDS-PAGE
32926
x * 32926, calculated from amino acid sequence
33030
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
33500
proelastase II, SDS-PAGE
34000
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
34160
-
x * 34160, sequence calculation
50000
proelastase I, SDS-PAGE
52000
-
x * 52000, SDS-PAGE, pro-elastase, enzymatically inactive
53000
-
SDS-PAGE, preproenzyme
53610
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
60780
-
Legionella pneumophila, deduced from nucleotide sequence
80000
zymography; zymography
100000
-
x * 100000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in the presence of inhibitors S-homoPhe [N-alpha-alpha]Phe-IsoAsn, phosphoramidon, and ClCH2CO-HOLeu-Ala-Gly-NH2
-
resolved to 1.5 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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 - 10
-
4C, 16 h, in presence of Ca2+ stable
31116
6 - 9
-
-
669613
6 - 9.5
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
65
-
10 min, 33% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the first and second disulfide bonds are essential for the stability and activity of the enzyme, respectively
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-propanol
Acetone
benzene
-
25% v/v, 30C, stable for at least 72 h
chloroform
-
pH 7.0, 30C, 4 days, 95.6% activity remaining for the nonglycosylated recombinant enzyme, 91.5% for the glycosylated recombinant enzyme
cyclohexane
-
25% v/v, 30C, stable for at least 72 h
dimethyl sulfoxide
DMSO
-
pH 7.0, 30C, 4 days, 95.1% activity remaining for the nonglycosylated recombinant enzyme, 83.2% for the glycosylated recombinant enzyme
Ethanol
hexane
-
25% v/v, 30C, stable for at least 72 h
isopropanol
-
pH 7.0, 30C, 4 days, 39.2% activity remaining for the nonglycosylated recombinant enzyme, 17.5% for the glycosylated recombinant enzyme
Methanol
-
pH 7.0, 30C, 4 days, 102% activity remaining for the nonglycosylated recombinant enzyme, 96.5% for the glycosylated recombinant enzyme
n-Butanol
-
pH 7.0, 30C, 4 days, 89.5% activity remaining for the nonglycosylated recombinant enzyme, 78.5% for the glycosylated recombinant enzyme
toluene
-
25% v/v, 30C, stable for at least 72 h
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.02 M Tris-hydrochloride, 0.5 mM CaCl2 (pH 7.5), 1 year, less than 10% loss of activity
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
-
the propeptide-elastase complex
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli; expression in Escherichia coli
expression in Pseudomonas putida, no activity
-
expression of mutants E141D, E141Q, E141G, H223G, H223E, and H223L in Escherichia coli JM109
gene lasB, DNA and amino acid sequence determination and analysis
-
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)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D168A
-
site-directed mutagenesis, inactive mutant
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
H223D
-
no proteolytic or elastolytic activity
H223Y
-
no proteolytic or elastolytic activity
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
R198A
-
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
R245A
-
site-directed mutagenesis
R253A
-
site-directed mutagenesis, inactive mutant
R279A
-
site-directed mutagenesis, inactive mutant
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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