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Information on EC 3.4.21.76 - Myeloblastin
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3.4.21.76 MyeloblastinSpecify your search results
Word Map
- 3.4.21.76
-
ancas
- myeloperoxidase
-
antineutrophil
- elastase
- autoantibody
-
anca-associated
- cathepsin
-
pr3-anca
- polyangiitis
- proteases
- granule
- glomerulonephritis
- autoimmune
- vasculitides
-
mpo-anca
- autoantigens
- anti-pr3
-
remission
-
crescent
- cyclophosphamide
-
perinuclear
-
polymorphonuclear
-
azurophilic
- gpa
-
vasculitic
-
anti-mpo
-
anca-positive
-
churg-strauss
-
pauci-immune
-
granulomatous
- lactoferrin
-
anti-proteinase
-
small-vessel
-
antinuclear
-
anti-myeloperoxidase
-
azurocidin
- elafin
-
neutrophil-derived
- polyarteritis
-
antibody-associated
- rituximab
-
goodpasture
- anti-gbm
-
chapel
- drug development
-
mpo-anca-associated
- diagnostics
- analysis
-
anti-glomerular
- medicine
-
aspartate-specific
-
ethanol-fixed
-
necrotising
- nodosa
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-/- > -Val-/-
Synonyms
AGP7, C-ANCA antigen, hPR-3, human leukocyte proteinase 3, human PR3, human proteinase 3, Leukocyte proteinase 3, Leukocyte proteinase 4, membrane proteinase 3, membrane-associated proteinase 3, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AGP7
-
-
-
-
C-ANCA antigen
-
-
-
-
Leukocyte proteinase 3
-
-
-
-
Leukocyte proteinase 4
-
-
-
-
myeloblastin
neutrophil proteinase 3
P29
-
-
-
-
p29b
PMNL proteinase
-
-
-
-
PR3
proteinase 3
Proteinase PR-3
-
-
-
-
Proteinase-3
Wegener's autoantigen
-
-
-
-
Wegener's granulomatosis autoantigen
-
-
-
-
PR3
-
-
-
-
PR3
-
-
PR3
-
proteinase 3
-
-
proteinase 3
-
Proteinase-3
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-/- > -Val-/-
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
128028-50-2
-
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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
(7-methoxycoumarin-4-yl)acetyl-Ala-Ala-Ala-Ala-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Ala-Pro-Leu-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Ala-Pro-Val-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Lys(2-picolinoyl)-Tyr-Asp-Ala-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Lys(2-picolinoyl)-Tyr-Asp-Ile-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Lys(2-picolinoyl)-Val-Glu-Ala-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
2-aminobenzoyl-APEEIM(o)DRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-APEEIMDRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-APEEIMMDRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-EAIPMSIPPEVKFNKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-EAIPMSIPQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-GIATFCM(o)LM(o)PEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-GIATFCMLMPEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Gln-Asp-Met-Ala-Val-Val-Gln-Ser-Val-Pro-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Gln-Pro-Met-Ala-Val-Val-Gln-Ser-Val-Pro-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-IVSARMAPEEIIMDRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-MMRCAQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-TFCM(o)LEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-TFCMLEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Tyr-Tyr-aminobutyl-(5-amino-2-nitrobenzoyl)-Gln-NH2 + H2O
?
-
-
-
?
2-aminobenzoyl-Tyr-Tyr-aminobutyl-(5-amino-2-nitrobenzoyl)-NH2 + H2O
?
-
-
-
?
2-aminobenzoyl-Tyr-Tyr-aminobutyl-Asn-Glu-Pro-Tyr(3-NO2)-NH2 + H2O
?
-
-
-
?
2-aminobenzoyl-VADCAQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-VAECCQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Val-Ala-Asp-Cys-Ala-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Val-Ala-Asp-Cys-Arg-Asp-Arg-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Val-Ala-Asp-Nva-Ala-Asp-Tyr-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-VSARQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
5-TAMRA-VADnVADYQ-DAP(CF) + H2O
?
a fluorescence resonance energy transfer, FRET, substrate. The reaction is inhibited by antibody MCPR3-7 binding
-
-
?
5-TAMRA-VADnVRDYQ-diaminopropionyl-fluorescein + H2O
?
fluorogenic substrate
-
-
?
Abz-APEEIMDDQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 2.5/mM/s
-
-
?
Abz-APEEIMDQQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 2/mM/s
-
-
?
Abz-APEEIMDRQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 14.6/mM/s
-
-
?
Abz-APEEIMDRY-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = lower than 1/mM/s
-
-
?
Abz-APEEIMDRYQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 3.2/mM/s
-
-
?
Abz-APEEIMDYQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 2.6/mM/s
-
-
?
Abz-APEEIMPRQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = lower than 1/mM/s
-
-
?
Abz-APEEIMRRQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = lower than 1/mM/s
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
Abz-Tyr-Tyr-Abu + 5-amino-2-nitrobenzamide
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ala-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Ala-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Arg-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Arg-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asn-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Asn-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asp-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Asp-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gln-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Gln-NH2
-
is hydrolyzed by PR3 within 20 min, yielding (5-amino-2-nitrobenzoyl)-Gln-NH2 and Abz-Tyr-Tyr-Abu fragments with retention times of 10.4 and 12.3 min, respectively
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Glu-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Glu-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gly-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Gly-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-His-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-His-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ile-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Ile-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Leu-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Leu-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Lys-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Lys-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Phe-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Phe-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Pro-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Pro-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ser-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Ser-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Thr-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Thr-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Trp-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Trp-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Tyr-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Tyr-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Val-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Val-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-ANB-NH2 + H2O
?
a fluorescence resonance energy transfer, FRET, substrate. The reaction is inhibited by antibody MCPR3-7 binding
-
-
?
Abz-VADCADRY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 651/mM/s
-
-
?
Abz-VADCADY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 630/mM/s
-
-
?
Abz-VADCAPY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = lower than 1/mM/s
-
-
?
Abz-VADCAQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 292/mM/s
-
-
?
Abz-VADCARY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 3.8/mM/s
-
-
?
Abz-VADCAY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 10.9/mM/s
-
-
?
Abz-Val-Ala-Asp-Nvl-Ala-Asp-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
acetyl-Glu(O-benzyl)-Lys(Ac)-Pro(4-O-benzyl)-Nva-7-amido-4-carbamoylmethylcoumarin + H2O
?
-
-
-
?
Ahx-PYFA-4-nitroanilide + H2O
?
the reaction is inhibited by antibody MCPR3-7 binding
-
-
?
annexin 1 + H2O
?
-
proteinase 3 is the main enzyme responsible for cleavage in the N terminus region of the protein
-
-
?
Boc-Ala-ONp + H2O
?
the reaction is not inhibited by antibody MCPR3-7 binding
-
-
?
Boc-Ala-Pro-nVal-SBzl + H2O
?
the reaction is not inhibited by antibody MCPR3-7 binding
-
-
?
Collagen type IV + H2O
Hydrolyzed collagen type IV
-
no or minimal activity against interstitial collagens type I and III
-
-
?
endothelial cell protein C receptor + H2O
?
-
PR3 produces multiple cleavages, with early products including 20 kDa N-terminal and C-terminal (after Lys176) fragments. High affinity interaction between PR3 and the endothelial cell protein C receptor (KD of 18.5–102 nanomol)
-
-
?
For-Ala-Ala-Pro-Abu-SBzl + H2O
?
the reaction is partly inhibited by antibody MCPR3-7 binding
-
-
?
kininogen + H2O
?
-
PR3 incubated with kininogen, or a synthetic peptide derived from kininogen, induces breakdown and release of a novel tridecapeptide termed PR3-kinin, NH2-MKRPPGFSPFRSS-COOH, consisting of bradykinin with two additional amino acids on each terminus. The reaction is specific. PR3-kinin binds to and activates human kinin B1 receptors, but does not bind to B2 receptors, expressed by transfected HEK293 cells in vitro. PR3-kinin is processed to bradykinin and des-Arg-bradykinin by plasma kallikrein. PR3 proteolyzes kininogen in a dose-dependent and specific manner. PR3 in neutrophil extracts induces kininogen proteolysis and induces release of bradykinin-like peptides from kininogen
-
-
?
MeO-Suc-Ala-Ala-Pro-Val-4-nitroanilide + H2O
MeO-Suc-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
?
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-p-nitroanilide + H2O
?
pH 7.4, 150 mM NaCl
-
-
?
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-thiobenzylester + H2O
?
pH 7.4, 150 mM NaCl, 3 mM 4,4’-dithiodipyridine
-
-
?
N-Boc-3-[2-(2'-imidazolyl)benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
-
-
-
?
N-Boc-3-[2-(2'-methoxy-4'-dimethylaminophenyl)benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
-
-
-
?
N-Boc-3-[2-(2-quinolinyl)benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
-
-
-
?
N-Boc-3-[2-[2-(1'-methyl)pyrrolo]benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
is the most efficient PR3 substrate
-
-
?
Peptidyl thiobenzyl ester + H2O
?
-
the preferred P1 residue is a small hydrophobic amino acid such as aminobutyric acid, norvaline, valine or alanine, in decreasing order of preference
-
-
?
procaspase 3 + H2O
?
-
PR3 can cleave membrane-associated procaspase 3 into a 22 kDa fragment
-
-
?
protease-activated receptor-2
?
-
PR3 may possess the capacity to interact and activate protease-activated receptor-2 expressing antigen-presenting cells and thereby potentially link this proinflammatory activity to the initiation of an adaptive immune response (induction of PR3-specific T cells)
-
-
?
Tert-Butyloxycarbonyl-Ala-Ala-norvaline thiobenzyl ester + H2O
?
-
best substrate
-
-
?
tumour necrosis factor-alpha + H2O
?
-
PR-3-mediated cleavage of tumour necrosis factor-alpha in usual interstitial pneumonia, which may have implications for future therapeutic targeting of tumour necrosis factor-alpha converting enzyme (TACE)
-
-
?
Val-Ala-Asp-Val-Lys-Asp-Arg + H2O
?
-
simulations with a neutral Asp213 bound to the peptide reproduce the expected conformation of the catalytic triad: there are strong hydrogen bonds between histidine 57 and serine 195 and between histidine 57 and the aspartic acid 102. When Asp213 is ionized and in the presence of a peptide bound in the enzyme, its side chain moves away from Gly197 and toward Ser195. The resulting interaction between Asp213 and Ser195 is strong with the formation of a hydrogen bond that persists for over 90% of the simulation time. Interaction competes with the crucial Ser-His hydrogen of the catalytic triad altering the proteolytic function of the enzyme. The pKa for Asp213 is of 8.4 (with a fast empirical method or based on molecular dynamics simulations). In simulations with negatively charged form of Asp213 the interaction between the carbonyl of the P1 residue (oxyanion hole) of the substrate and Ser195 (NH) of PR3 has vanished and the favorable interactions between the enzyme and the substrate are disrupted. A strong hydrogen bond is formed between the imidazole ring of His57 and the P1 and P1' residues of the substrate (NH groups) lasting 83 and 55% of the simulation time, respectively. These hydrogen bonds compete with, or replace, the crucial ones between amino acids of the catalytic triad and in particular the Ser-His interaction
-
-
?
Abz-VADCADQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 614/mM/s
-
-
?
Abz-VADCRDRQ-EDDnp + H2O
Abz-VADCR + DRQ-EDDnp
best synthetic substrate
-
-
?
Boc-Ala-Pro-Nva-thiobenzylester + H2O
?
pH 7.5, serine-protease activity of PR3
-
-
?
Boc-Ala-Pro-Nva-thiobenzylester + H2O
?
pH 7.5, serine-protease activity of PR3
-
-
?
MeOSuc-AAPV-4-nitroanilide + H2O
MeOSuc-AAPV + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
MeOSuc-AAPV-4-nitroanilide + H2O
MeOSuc-AAPV + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
MeOSuc-AIPM-4-nitroanilide + H2O
MeOSuc-AIPM + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
MeOSuc-AIPM-4-nitroanilide + H2O
MeOSuc-AIPM + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
oxidized insulin B chain + H2O
?
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
oxidized insulin B chain + H2O
?
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
procaspase-3 + H2O
?
37°C
in vitro, purified PR3 cleaves procaspase-3 into an active 22 kDa fragment
-
?
procaspase-3 + H2O
?
-
in vitro, purified PR3 cleaves procaspase-3 into an active 22 kDa fragment
-
?
Suc-AAA-4-nitroanilide + H2O
Suc-AAA + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0, very low activity
-
-
?
Suc-AAA-4-nitroanilide + H2O
Suc-AAA + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
Suc-AAPL-4-nitroanilide + H2O
Suc-AAPL + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0, very low activity
-
-
?
Suc-AAPL-4-nitroanilide + H2O
Suc-AAPL + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
Suc-AAPV-4-nitroanilide + H2O
Suc-AAPV + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
Suc-AAPV-4-nitroanilide + H2O
Suc-AAPV + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
surfactant protein D + H2O
?
37°C, pH 7.4
a fragment of about 35000 Da
-
?
additional information
?
-
-
no significant hydrolysis of 2-aminobenzoyl-EAIPM(o)SIPPEVKFNKQN-(2,4dinitrophenyl)ethylenediamine and 2-aminobenzoyl-EAIPM(o)SIPQN-(2,4dinitrophenyl)ethylenediamine
-
?
additional information
?
-
-
PR3 induced cell proliferation is dependent on its serine proteinase activity
-
?
additional information
?
-
-
Suc-Ala-Ala-Ala-Ala-p-nitroanilide, Suc-Ala-Ala-Pro-Met-p-nitroanilide, Suc-Ala-Ala-Pro-Leu, and Suc-Ala-Ala-Pro-Nle-p-nitroanilide -p-nitroanilide are no substrates
-
?
additional information
?
-
-
involved in control of growth and differentiation of human leukemia cells, potent microbicidal activity, is the target antigen of cytoplasmic-staining antineutrophil cytoplasmic autoantibodies circulating in Wegener's granulomatosis
-
-
?
additional information
?
-
-
potent proinflammatory potential, expressed by phagocytic cells of the immune system
-
?
additional information
?
-
-
potent proinflammatory potential, expressed by phagocytic cells of the immune system
-
?
additional information
?
-
no reaction with VGVAPGV and VAPGVGVAPGV
-
-
?
additional information
?
-
-
Asp-61, Lys-99, and Arg-143 in Pr3 are in the vicinity of the substrate binding site that extends from at least subsites S4 to S3'. Subsites S1' to S3' are all in the vicinity of charged residues. Ionic interactions involving residue P3' and Asp-61 are not essential for substrate binding but elongation of the peptide chain helps to stabilize the substrate, improving catalytic efficiency
-
-
?
additional information
?
-
-
PR3 induces phenotypic and functional maturation of blood monocyte-derived iDCs
-
-
?
additional information
?
-
substrate specificity for small hydrophobic residues at P1 position (Val, Cys, Ala, Met, Ser and Leu)
-
-
?
additional information
?
-
-
substrate specificity for small hydrophobic residues at P1 position (Val, Cys, Ala, Met, Ser and Leu)
-
-
?
additional information
?
-
-
CD11b/CD18 (Mac-1, beta2-integrin) is a binding-partner of membrane-bound PR3. Active PR3, but not proPR3 can bind to the surface of CD177-transfected HEK293 cells, suggesting that N-terminal processing is important for binding of PR3 to CD177. FcgammaRIIIb also colocalizes with PR3 on the neutrophil membrane. PR3-CD177 binding may activate beta2-integrins and promote neutrophil firm adhesion
-
-
?
additional information
?
-
-
most intense proteolysis of peptides with polar noncharged acid residues: Gln and Asn followed by Ser. Less active are peptides with negatively charged Glu and Asp. The presence of Lys and Arg gives substrates with susceptibility rates one order of magnitude lower
-
-
?
additional information
?
-
-
the peptide sequence VADVKDR is highly specific for PR3
-
-
?
additional information
?
-
PR3 is capable of hydrolyzing several extracellular matrix proteins including collagen, elastin, fibronectin and laminin
-
-
?
additional information
?
-
analysis of S4-S5 specificity of human neutrophil proteinase 3
-
-
?
additional information
?
-
-
analysis of S4-S5 specificity of human neutrophil proteinase 3
-
-
?
additional information
?
-
analysis of substrate and cleavage specificity of hPR-3 using elastase substrates, having Val, Ala, and Ile in the P1 position, determination of the extended cleavage specificity, overview. hPR-3 shows good activity against the Val substrate, lower activity on the Ala substrate, and no activity on the other substrates, including one with an Ile in the P1 position
-
-
?
additional information
?
-
-
analysis of substrate and cleavage specificity of hPR-3 using elastase substrates, having Val, Ala, and Ile in the P1 position, determination of the extended cleavage specificity, overview. hPR-3 shows good activity against the Val substrate, lower activity on the Ala substrate, and no activity on the other substrates, including one with an Ile in the P1 position
-
-
?
additional information
?
-
binding of purified recombinant PR3 to phosphatidylserine externalized on apoptotic rat basophilic leukemia (RBL) cells or murine neutrophils (from 12-week-old male C57Bl6 mice). PR3 is a phosphatidylserine (PS)-binding protein and this interaction is dependent on the hydrophobic patch responsible for membrane anchorage. Molecular simulations suggest that PR3 interacts with phosphatidylserine via a small number of amino acids, which engage in long lasting interactions with the lipid heads, molecular modeling of the PR3-PS interaction, detailed overview
-
-
?
additional information
?
-
-
binding of purified recombinant PR3 to phosphatidylserine externalized on apoptotic rat basophilic leukemia (RBL) cells or murine neutrophils (from 12-week-old male C57Bl6 mice). PR3 is a phosphatidylserine (PS)-binding protein and this interaction is dependent on the hydrophobic patch responsible for membrane anchorage. Molecular simulations suggest that PR3 interacts with phosphatidylserine via a small number of amino acids, which engage in long lasting interactions with the lipid heads, molecular modeling of the PR3-PS interaction, detailed overview
-
-
?
additional information
?
-
design, synthesis, and enzymatic evaluation of novel ZnO quantum dot (QD)-based assay for detection of proteinase 3 (PR3) activity, composition and mechanism of action of QD PR3 sensor, overview. The peptide sequence Tyr-Tyr-Abu-Gln-Asp-Pro is exclusively cleaved by PR3, it is connected to QD via functionalized linker oxyethylene linker
-
-
?
additional information
?
-
proteinase 3 can also act via the non-catalytic mechanism. The structure of substrates most susceptible to PR3-mediated hydrolysis provide guidelines for developing ketomethylene compounds, azapeptides, and peptidyl phophonates
-
-
?
additional information
?
-
-
in mouse PR3 binding sites S6, S5, S1' and S3' are clearly polar, S2' is pretty polar, while S4, S3, S1, S4' are rather hydrophobic. VADVKDR does not interact properly with mouse PR3
-
-
?
additional information
?
-
-
unlike human PR3, mouse PR3 is unlikely to bind substrates with acidic groups (Asp, Glu) on the S side. Efficient substrates of human PR3 may be poor substrates of mouse PR3
-
-
?
additional information
?
-
-
analysis of substrate and cleavage specificity of xPR-3 using elastase substrates, having Val, Ala, and Ile in the P1 position, determination of the extended cleavage specificity, overview. Xenopus PR-3 shows the best activity against the Ala substrate, lower activity on the Val, and similarly to human PR-3 no activity against the Ile substrate. MLDAMGSL and MLDTMGSL are poor substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
involved in control of growth and differentiation of human leukemia cells, potent microbicidal activity, is the target antigen of cytoplasmic-staining antineutrophil cytoplasmic autoantibodies circulating in Wegener's granulomatosis
-
-
?
additional information
?
-
-
potent proinflammatory potential, expressed by phagocytic cells of the immune system
-
?
additional information
?
-
-
potent proinflammatory potential, expressed by phagocytic cells of the immune system
-
?
additional information
?
-
PR3 is capable of hydrolyzing several extracellular matrix proteins including collagen, elastin, fibronectin and laminin
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-4-isobutyl-2-[(p-chlorobenzylthio)methyl]-5-benzyl-1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
-
(S)-4-isobutyl-2-[(phenylthio)methyl]-1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
-
(S)-4-isobutyl-5-benzyl-2-chloromethyl-1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
-
(S)-4-isobutyl-5-benzyl-2-[(phenylthio)methyl]-1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
-
(S)-4-isobutyl-5-[(m-carboxyl)benzyl]-2-[(phenylsulfonyl)methyl]-1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
-
(S)-4-isobutyl-5-[(m-carboxymethyl)benzyl]-2-[(phenylsulfonyl)methyl]-1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
-
(S)-4-isobutyl-5-[(m-carboxymethyl)benzyl]-2-[(phenylthio)methyl]-1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
-
(S)-4-isobutyl-N-[(4-chlorobenzylsulfonyl)methyl]-5-benzyl-1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
-
1-acetyl-L-prolyl-L-tyrosyl-N-[1-[bis(4-chlorophenoxy)phosphoryl]ethyl]-L-alpha-asparagine
-
1-[11,21-dioxo-25-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-4,7,14,17-tetraoxa-10,20-diazapentacosanan-1-oyl]-L-prolyl-L-tyrosyl-N-[1-[bis(4-chlorophenoxy)phosphoryl]ethyl]-L-alpha-asparagine
-
1-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-prolyl-L-tyrosyl-N-[1-[bis(4-chlorophenoxy)phosphoryl]butyl]-L-alpha-asparagine
-
1-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-prolyl-L-tyrosyl-N-[1-[bis(4-chlorophenoxy)phosphoryl]ethyl]-L-alpha-asparagine
-
2,3-diethyl-5-([1-[(phenylsulfanyl)methyl]-1H-1,2,3-triazol-4-yl]methyl)-1,2,3,5-thiatriazolidin-4-one 1,1-dioxide
-
0.00862 mM inhibits by ca. 14%
2,3-diethyl-5-[[1-(2-oxo-2-phenylethyl)-1H-1,2,3-triazol-4-yl]methyl]-1,2,3,5-thiatriazolidin-4-one 1,1-dioxide
-
0.00862 mM inhibits by ca. 10%, fits into the Pr 3 active site well and engages in multiple interactions with the enzyme
2,3-diethyl-5-[[1-(4-methoxybenzyl)-1H-1,2,3-triazol-4-yl]methyl]-1,2,3,5-thiatriazolidin-4-one 1,1-dioxide
-
0.00862 mM inhibits by ca. 8%
2-(2,3-diethyl-1,1-dioxido-4-oxo-1,2,3,5-thiatriazolidin-5-yl)-N-phenylacetamide
-
0.00862 mM inhibits by ca. 13%
2-(2,3-diethyl-1,1-dioxido-4-oxo-1,2,3,5-thiatriazolidin-5-yl)-N-[2-(2-methoxyphenyl)ethyl]-3-phenylpropanamide
-
0.00862 mM inhibits by ca. 11%
2-(2,3-diethyl-1,1-dioxido-4-oxo-1,2,3,5-thiatriazolidin-5-yl)-N-[4-(morpholin-4-yl)phenyl]-3-phenylpropanamide
-
0.00862 mM inhibits by ca. 13%
4,5-bisbenzyl-2-[[(2-benzoxazolyl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4,5-bisbenzyl-2-[[(5-phenyl-1,3,4-oxadiazol-2-yl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4,5-bisbenzyl-2-[[(6-amino-2-benzoxazolyl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4-benzyl-5-methyl-2-[[(2-benzoxazolyl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4-isobutyl-5-methyl-2-[[(2-benzoxazolyl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4-isobutyl-5-methyl-2-[[(3-phenyl-1,2,4-oxadiazol-5-yl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4-isobutyl-5-methyl-2-[[(4,5-diphenyl-2-oxazolyl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4-isobutyl-5-methyl-2-[[(5-phenyl-1,3,4-oxadiazol-2-yl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4-isobutyl-5-methyl-2-[[(5-phenyl-2-benzoxazoyl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4-isobutyl-5-methyl-2-[[2-benzothiazolthio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
4-methyl-N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-norleucyl-L-tyrosyl-N-[1-[bis(4-chlorophenoxy)phosphoryl]ethyl]-L-alpha-asparagine
-
5-benzyl-4-isobutyl-2-[[(2-benzoxazolyl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
5-benzyl-4-isobutyl-2-[[(3-phenyl-1,2,4-oxadiazol-5-yl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
5-benzyl-4-isobutyl-2-[[(4,5-diphenyl-2-oxazolyl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
5-benzyl-4-isobutyl-2-[[(5-phenyl-1,3,4-oxadiazol-2-yl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
5-benzyl-4-isobutyl-2-[[(5-phenyl-2-benzoxazoyl)thio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
5-benzyl-4-isobutyl-2-[[2-benzothiazolthio]methyl]-1,2,5-thiadiazolidin-3-one-1,1-dioxide
-
-
Abz-VADnV[PSI](COCH2)ADYQ-EDDnp
best inhibitor, selective for proteinase 3, displays a competitive and reversible inhibition mechanism
alpha-1-Proteinase inhibitor
inhibits the enzyme, inhibition is implicated by anti-neutrophil cytoplasmic antibodies with proteinase 3 specificity
-
alpha1-proteinase
-
does not inhibit when PR3 is bound to the outer cell surface of neutrophils
-
anti-neutrophil cytoplasmic antibodies with proteinase 3 specificity
screening: a great majority of PR3-ANCA has inhibitory capacity towards the enzyme, overview. PR3-ANCA with inhibitory properties bind to the active site surface of proteinase 3. Epitopes of inhibitory PR3-ANCA are not masked by elafin
-
biotin-Val-Tyr-Asp-NvaP(O-C6H4-4-Cl)2
occupancy of the S1 subsite of PR3 by a NVA residue and of the S4-S5 subsites by a biotinylated Val residue enhances the second-order inhibition constant toward PR3 by more than 10 times as compared to the best phosphonate PR3 inhibitor reported. The inhibitor shows no significant inhibitory activity toward human neutrophil elastase and resists proteolytic degradation in sputa from cystic fibrosis patients. It also inhibits macaque PR3 but not the PR3 from rodents
N-(1,3-benzodioxol-5-yl)-2-(2,3-diethyl-1,1-dioxido-4-oxo-1,2,3,5-thiatriazolidin-5-yl)-3-phenylpropanamide
-
0.00862 mM inhibits by ca. 23%
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-leucyl-L-tyrosyl-N-[1-[bis(4-chlorophenoxy)phosphoryl]ethyl]-L-alpha-asparagine
-
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-norleucyl-L-tyrosyl-N-[1-[bis(4-chlorophenoxy)phosphoryl]ethyl]-L-alpha-asparagine
-
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-valyl-L-tyrosyl-N-[1-[bis(4-chlorophenoxy)phosphoryl]butyl]-L-alpha-asparagine
-
N-[5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]-L-valyl-L-tyrosyl-N-[1-[bis(4-chlorophenoxy)phosphoryl]ethyl]-L-alpha-asparagine
-
protein 3-specific MCPR3-7 antibody
the monoclonal antibody interfers with the activity of proteinase 3 by an allosteric mechanism. It can change its conformation and impair interactions with alpha1-proteinase inhibitor. The conformation of the S1 pocket of the enzyme is not changed significantly after binding of MCPR3-7, but rather the S1' subsite of the enzyme is changed
-
trappin
80% inhibition, oxidized with N-chlorosuccinimide: 19% inhibition
-
[4-[(2,3-diethyl-1,1-dioxido-4-oxo-1,2,3,5-thiatriazolidin-5-yl)methyl]-1H-1,2,3-triazol-1-yl]acetic acid
-
0.00862 mM inhibits by ca. 11%
(E)-4-(N-(2-(1-(hydroxyimino)butyl)phenyl)sulfamoyl)phenyl pivalate
-
(E)-4-(N-(2-(1-(hydroxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
the compound has several beneficial effects in inflammatory disease and lipopolysacchride-induced edema, overview
(E)-4-(N-(2-(1-(hydroxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
shows dual inhibitory effects on neutrophil elastase and proteinase 3. The compound significantly attenuates histological changes in lung tissue from mice with LPS-induced acute lung injury (ALI)
(E)-4-(N-(2-(1-(hydroxyimino)methyl)phenyl)sulfamoyl)phenyl pivalate
-
(E)-4-(N-(2-(1-(hydroxyimino)propyl)phenyl)sulfamoyl)phenyl pivalate
-
(E)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
-
(Z)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
-
4-(N-(2-(2-hydroxyethylcarbamoyl)phenyl)sulfamoyl)phenyl pivalate
-
4-(N-(2-acetylphenyl)sulfamoyl)phenyl 2-methylpropane-2-sulfinate
-
4-(N-(2-formylphenyl)sulfamoyl)phenyl 2-methylpropane-2-sulfinate
-
alpha1-antitrypsin
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.98 M
-
alpha1-antitrypsin
-
inhibition of bilayer-bound PR3 is more important than that observed for the soluble form of the enzyme
-
alpha1-antitrypsin
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.74 M
-
alpha1-protease inhibitor
-
membrane-bound Pr3 is inhibited almost as rapidly as the soluble Pr3, but inhibition is not complete after 1 h. No interaction between constitutive membrane-bound Pr3 and the inhibitor
-
alpha1-protease inhibitor
-
purified human alpha1-protease inhibitor inhibits gibbon PR3 and forms a covalently linked complex with it
-
Alpha1-proteinase inhibitor
the inhibition is highly dependent on the proper conformation of an exposed reactive center loop, which serves as a pseudosubstrate. Inhibitor mutant E342K is less effective due to an altered conformation of the reactive center loop
-
Eglin c
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 117 M
Eglin c
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 3.3 M
elafin
55% inhibition, oxidized with N-chlorosuccinimide: 10% inhibition
-
elafin
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 1.9 M
-
elafin
-
does not inhibit when PR3 is bound to the outer cell surface of neutrophils
-
elafin
-
membrane-bound Pr3 is inhibited almost as rapidly as the soluble Pr3, but inhibition is not complete after 1 h. No interaction between constitutive membrane-bound Pr3 and the inhibitor
-
elafin
-
is inhibited by purified human elafin, a canonical low molecular weight inhibitor of human PR3
-
elafin
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.99 M
-
ethyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
-
MeO-Suc-AAPA-chloromethyl ketone
-
irreversible inhibitor, inhibits about 90% of the activity after 2 h. Membrane-bound Pr3 remains bound to the membrane when inhibited by the chloromethyl ketone inhibitor
methyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
-
methyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)phenylsulfonamide)benzoate
-
methyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)phenylsulfonamide)benzoate
-
-
propyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
-
sivelestat
acetylating, nonpeptidic inhibitor, sivelestat, developed for the treatment of acute lung injury (ALI )in Japan
SLPI
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, limited inhibition, more than 75% of activity remained in the presence of the highest concentration of inhibitor
SLPI
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, limited inhibition, more than 75% of activity remained in the presence of the highest concentration of inhibitor
Val15-aprotinin
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, limited inhibition, more than 75% of activity remained in the presence of the highest concentration of inhibitor
-
Val15-aprotinin
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 447 M
-
additional information
-
substituted isocoumarins, peptide-phosphonates and chloromethyl ketones inhibit proteinase 3 less potently than human neutrophil elastase, by 1-2 orders of magnitude
-
additional information
-
not: alpha1-anti-chymotrypsin; secretory leukocyte proteinase inhibitor
-
additional information
-
aprotinin; cysteine, aspartic, or metalloproteinase inhibitors; secretory leukocyte proteinase inhibitor
-
additional information
-
membrane-bound enzyme is resistant to inhibition by physiologic proteinase inhibitors
-
additional information
low molecular weight serine protease inhibitors, but only partially by inhibitors of larger molecular weight such as alpha1-protease inhibitor
-
additional information
-
low molecular weight serine protease inhibitors, but only partially by inhibitors of larger molecular weight such as alpha1-protease inhibitor
-
additional information
transcription of PR3 is downregulated upon granulocyte and monocyte maturation
-
additional information
-
transcription of PR3 is downregulated upon granulocyte and monocyte maturation
-
additional information
-
hydrolysis of N-methoxysuccinyl-Ala-Ala-Pro-Val-pNA by neutrophil PR3 is reduced by 40% as a result of deglycosylation
-
additional information
-
peptide-specific T-cell responses, exemplary for PRTN358 and PRTN3235, can be inhibited by anti-HLA-DR antibodies, but not by an anti-HLAABC antibody
-
additional information
synthesis and pharmacological characterization of 2-aminobenzaldehyde oxime analogues as dual inhibitors of neutrophil elastase and proteinase 3, structure–activity relationship analysis, overview
-
additional information
-
synthesis and pharmacological characterization of 2-aminobenzaldehyde oxime analogues as dual inhibitors of neutrophil elastase and proteinase 3, structure–activity relationship analysis, overview
-
additional information
design of ketomethylene-based enzyme inhibitors that show low micromolar IC50 values. Molecular dynamics simulations show that the interactions between enzyme and ketomethylene-containing inhibitors are similar to those with the corresponding substrates. N- and C-terminal FRET groups are important for securing high inhibitory potency toward the enzyme
-
additional information
-
design of ketomethylene-based enzyme inhibitors that show low micromolar IC50 values. Molecular dynamics simulations show that the interactions between enzyme and ketomethylene-containing inhibitors are similar to those with the corresponding substrates. N- and C-terminal FRET groups are important for securing high inhibitory potency toward the enzyme
-
additional information
PR3 inhibitors belong either to the group of peptide analogues (whose structure is directed by the sequence of the substrates) or to non-peptidyl inhibitors, including oxazolidine-2,4-diones, 3,1-benzoxazin-4-ones, isocoumarins, N-hydroxysuccinimides, thiatriazolidines, oximes, Kojic acid derivatives. Analysis of aminophosphonates as potent and selective PR3 inhibitors, overview. Synthesis of alpha-aminoalkylphosphonate diaryl esters. No inhibition by Pro-Tyr-Asp-AlaP(O-C6H4-4-Cl)2
-
additional information
synthesis of a series 2-aminobenzaldehyde oxime and 2-aminobenzoate analogues, their inhibitory effects on neutrophilic serine proteases (NsPs), i.e. cathepsin G, proteinase 3 (Pr3), and human neutrophil elastase (HNE), are determined. A hydroxyl oxime moiety plays an important role in ligand-enzyme affinity through hydrogen bonding, structure-activity relationships, overview. Most of the compounds have a potent and dual inhibitory effect on human neutrophil elastase and Pr3
-
additional information
-
synthesis of a series 2-aminobenzaldehyde oxime and 2-aminobenzoate analogues, their inhibitory effects on neutrophilic serine proteases (NsPs), i.e. cathepsin G, proteinase 3 (Pr3), and human neutrophil elastase (HNE), are determined. A hydroxyl oxime moiety plays an important role in ligand-enzyme affinity through hydrogen bonding, structure-activity relationships, overview. Most of the compounds have a potent and dual inhibitory effect on human neutrophil elastase and Pr3
-
additional information
potencies of peptidyl di(chlorophenyl)-phosphonate ester inhibitors, kinetics and molecular docking and modeling, overview
-
additional information
-
potencies of peptidyl di(chlorophenyl)-phosphonate ester inhibitors, kinetics and molecular docking and modeling, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochalasin B
-
PR3 and CD177 are increased in parallel. Stimulating cells with cytochalasin B in combination with fML, PmPR3- and CD177-negative cells become positive
fMLP
-
PR3 and CD177 are increased in parallel. Causes a moderate increase. stimulating cells with cytochalasin B in combination with fML, PmPR3- and CD177-negative cells become positive
PMA
-
PR3 and CD177 are increased in parallel. Increases 4.9fold. mPR3- and CD177-negative cells become positive
TNF-alpha
-
leads to caspase-3-dependent apoptosis within 3 h accompanied by increased surface expression of PR3 and MPO
-
TNF-alpha
-
PR3 and CD177 are increased in parallel. Causes a moderate increase
-
additional information
-
glycosylation at Asn-147, but not at Asn-102, is critical for optimal hydrolytic activity of PR3. Efficient amino-terminal proteolytic processing of recombinant PR3 is dependent on glycosylation at Asn-102
-
additional information
-
PR3 externalization depends on PLSCR1, but is independently of its serine-proteinase activity. Higher membrane PR3 expression on neutrophils after apoptosis without degranulation. Phospholipid scramblase 1 is involved in membrane PR3 expression during apoptosis-induced phospholipid redistribution between the two plasma membrane leaflets
-
additional information
-
PRTN3235-specific T-cells can be stimulated from the blood of healthy individuals with multiple HLA-DR-genotypes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0174
2-aminobenzoyl-Tyr-Tyr-aminobutyl-(5-amino-2-nitrobenzoyl)-Gln-NH2
pH and temperature not specified in the publication
0.0314
2-aminobenzoyl-Tyr-Tyr-aminobutyl-(5-amino-2-nitrobenzoyl)-NH2
pH and temperature not specified in the publication
0.0032
2-aminobenzoyl-Tyr-Tyr-aminobutyl-Asn-Glu-Pro-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
0.0123
2-aminobenzoyl-Val-Ala-Asp-Cys-Ala-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
pH and temperature not specified in the publication
0.0033
2-aminobenzoyl-Val-Ala-Asp-Cys-Arg-Asp-Arg-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
pH and temperature not specified in the publication
0.0011
2-aminobenzoyl-Val-Ala-Asp-Nva-Ala-Asp-Tyr-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
pH and temperature not specified in the publication
0.0314
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide)
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.1731
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ala-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.0642
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Arg-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.0251
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asn-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.0281
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asp-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.0174
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gln-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.0253
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Glu-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.1242
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gly-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.0357
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-His-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.2763
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ile-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.2436
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Leu-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.0729
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Lys-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
1.126
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Phe-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.1823
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Pro-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.0278
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ser-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.0321
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Thr-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
1.274
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Trp-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.9823
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Tyr-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.3124
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Val-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.05
O-methyl-succinyl-Ala-Ala-Pro-Ala-S-benzyl ester
pH and temperature not specified in the publication
0.27
O-methyl-succinyl-Ala-Ala-Pro-Val-4-nitroanilide
pH and temperature not specified in the publication
0.61
Suc-AAA-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
3.5
Suc-AAPL-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
0.192
succinyl-Ala-Ala-Nva-S-benzyl ester
pH and temperature not specified in the publication
0.063
tert-butyloxycarbonyl-Ala-Ala-Nva-S-benzyl ester
pH and temperature not specified in the publication
0.028
tert-butyloxycarbonyl-Ala-Ala-Val-S-benzyl ester
pH and temperature not specified in the publication
0.66
tert-butyloxycarbonyl-Ala-O-4-nitrophenyl ester
pH and temperature not specified in the publication
additional information
additional information
-
Km values of peptidyl thiobenzyl esters
-
1.1
MeOSuc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
1.2
MeOSuc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
0.61
MeOSuc-AIPM-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
1.5
MeOSuc-AIPM-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
2.5
Suc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
3.7
Suc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.9
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide)
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
2.1
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ala-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
2.6
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Arg-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
5.3
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asn-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
4.8
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asp-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
6.4
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gln-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
3.3
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Glu-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
3.2
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gly-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
3.1
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-His-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
1.8
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ile-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
2
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Leu-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
2.5
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Lys-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
1.3
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Phe-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
1.1
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Pro-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
5.1
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ser-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
2.8
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Thr-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
1.3
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Trp-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
1.6
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Tyr-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
4.7
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Val-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.031
Suc-AAA-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
0.16
Suc-AAPL-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
additional information
additional information
-
turnover numbers of peptidyl thiobenzyl esters
-
0.59
MeOSuc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
6.2
MeOSuc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
0.26
MeOSuc-AIPM-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
7.2
MeOSuc-AIPM-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
0.37
Suc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
11.2
Suc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
2-aminobenzoyl-Gln-Asp-Met-Ala-Val-Val-Gln-Ser-Val-Pro-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
pH and temperature not specified in the publication
95.7
2-aminobenzoyl-Gln-Pro-Met-Ala-Val-Val-Gln-Ser-Val-Pro-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
pH and temperature not specified in the publication
274.9
2-aminobenzoyl-Tyr-Tyr-aminobutyl-(5-amino-2-nitrobenzoyl)-Gln-NH2
pH and temperature not specified in the publication
188.9
2-aminobenzoyl-Tyr-Tyr-aminobutyl-(5-amino-2-nitrobenzoyl)-NH2
pH and temperature not specified in the publication
1596
2-aminobenzoyl-Tyr-Tyr-aminobutyl-Asn-Glu-Pro-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
292
2-aminobenzoyl-Val-Ala-Asp-Cys-Ala-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
pH and temperature not specified in the publication
6500
2-aminobenzoyl-Val-Ala-Asp-Cys-Arg-Asp-Arg-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
pH and temperature not specified in the publication
7200
2-aminobenzoyl-Val-Ala-Asp-Nva-Ala-Asp-Tyr-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
pH and temperature not specified in the publication
188.9
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide)
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
12.2
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ala-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
41.1
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Arg-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
201.2
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asn-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
170.8
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asp-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
274.9
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gln-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
138.2
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Glu-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
25.8
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gly-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
86.7
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-His-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
6.5
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ile-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
7.2
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Leu-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
34.3
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Lys-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
1.1
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Phe-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.5
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Pro-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
183.8
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ser-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
87.3
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Thr-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
0.9
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Trp-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
1.6
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Tyr-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
15.1
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Val-NH2
-
in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C
360
acetyl-Glu(O-benzyl)-Lys(Ac)-Pro(4-O-benzyl)-Nva-7-amido-4-carbamoylmethylcoumarin
pH and temperature not specified in the publication
80.51
biotinyl-Val-Tyr-Asp-Nva-4-nitroanilide
pH and temperature not specified in the publication
1500
N-Boc-3-[2-[2-(1'-methyl)pyrrolo]benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide)
-
-
220
O-methyl-succinyl-Ala-Ala-Pro-Ala-S-benzyl ester
pH and temperature not specified in the publication
3.05
O-methyl-succinyl-Ala-Ala-Pro-Val-4-nitroanilide
pH and temperature not specified in the publication
470
succinyl-Ala-Ala-Nva-S-benzyl ester
pH and temperature not specified in the publication
1000
tert-butyloxycarbonyl-Ala-Ala-Nva-S-benzyl ester
pH and temperature not specified in the publication
380
tert-butyloxycarbonyl-Ala-Ala-Val-S-benzyl ester
pH and temperature not specified in the publication
15.15
tert-butyloxycarbonyl-Ala-O-4-nitrophenyl ester
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000025
elafin, oxidized with myeloperoxidase
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-thiobenzylester as substrate, pH 7.4, 150 mM NaCl, 3 mM 4,4’-dithiodipyridine
-
0.000029
elafin, oxidized with N-chlorosuccinimide
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-thiobenzylester as substrate, pH 7.4, 150 mM NaCl, 3 mM 4,4’-dithiodipyridine
-
0.00000018
trappin
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-thiobenzylester as substrate, pH 7.4, 150 mM NaCl, 3 mM 4,4’-dithiodipyridine
-
0.000035
trappin, oxidized with myeloperoxidase
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-thiobenzylester as substrate, pH 7.4, 150 mM NaCl, 3 mM 4,4’-dithiodipyridine
-
0.00005
trappin, oxidized with N-chlorosuccinimide
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-thiobenzylester as substrate, pH 7.4, 150 mM NaCl, 3 mM 4,4’-dithiodipyridine
-
0.00000018
trappin-2
25°C, recombinant trappin-2 expressed in Pichia pastoris
-
0.00000012
elafin
25°C, recombinant elafin expressed in Pichia pastoris
-
0.00000012
elafin
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-thiobenzylester as substrate, pH 7.4, 150 mM NaCl, 3 mM 4,4’-dithiodipyridine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
447000
Val15-aprotinin
Mus musculus
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 447 M
-
0.00173
(E)-4-(N-(2-(1-(hydroxyimino)butyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.4, 30°C
0.00173
(E)-4-(N-(2-(1-(hydroxyimino)butyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.5, 30°C
0.00022
(E)-4-(N-(2-(1-(hydroxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.4, 30°C
0.00022
(E)-4-(N-(2-(1-(hydroxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.5, 30°C
0.00053
(E)-4-(N-(2-(1-(hydroxyimino)methyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.4, 30°C
0.00053
(E)-4-(N-(2-(1-(hydroxyimino)methyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.5, 30°C
0.0025
(E)-4-(N-(2-(1-(hydroxyimino)propyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.4, 30°C
0.0025
(E)-4-(N-(2-(1-(hydroxyimino)propyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.5, 30°C
0.00061
(E)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.4, 30°C
0.00061
(E)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.5, 30°C
0.00237
(Z)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.4, 30°C
0.00237
(Z)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.5, 30°C
0.00061
2-hydroxyethyl 2-(4-(pivaloyloxy)phenylsulfonamido)benzoate
Homo sapiens
pH 7.4, 30°C
0.00061
2-hydroxyethyl 2-(4-(pivaloyloxy)phenylsulfonamido)benzoate
Homo sapiens
pH 7.5, 30°C
0.00031
4-(N-(2-(2-hydroxyethylcarbamoyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.4, 30°C
0.00031
4-(N-(2-(2-hydroxyethylcarbamoyl)phenyl)sulfamoyl)phenyl pivalate
Homo sapiens
pH 7.5, 30°C
0.01
4-(N-(2-acetylphenyl)sulfamoyl)phenyl 2-methylpropane-2-sulfinate
Homo sapiens
pH 7.4, 30°C
0.01
4-(N-(2-acetylphenyl)sulfamoyl)phenyl 2-methylpropane-2-sulfinate
Homo sapiens
above, pH 7.5, 30°C
0.01
4-(N-(2-formylphenyl)sulfamoyl)phenyl 2-methylpropane-2-sulfinate
Homo sapiens
pH 7.4, 30°C
0.01
4-(N-(2-formylphenyl)sulfamoyl)phenyl 2-methylpropane-2-sulfinate
Homo sapiens
above, pH 7.5, 30°C
740
alpha1-antitrypsin
Mus musculus
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.74 M
-
980
alpha1-antitrypsin
Homo sapiens
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.98 M
-
3300
Eglin c
Mus musculus
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 3.3 M
117000
Eglin c
Homo sapiens
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 117 M
990
elafin
Mus musculus
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.99 M
-
1900
elafin
Homo sapiens
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 1.9 M
-
0.01
ethyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
Homo sapiens
pH 7.4, 30°C
0.01
ethyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
Homo sapiens
above, pH 7.5, 30°C
0.01
methyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
Homo sapiens
pH 7.4, 30°C
0.01
methyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
Homo sapiens
above, pH 7.5, 30°C
0.00494
methyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)phenylsulfonamide)benzoate
Homo sapiens
pH 7.4, 30°C
0.00494
methyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)phenylsulfonamide)benzoate
Homo sapiens
pH 7.5, 30°C
0.01
methyl 2-(4-pivalamidophenylsulfonamido)benzoate
Homo sapiens
above, pH 7.5, 30°C
0.01
propyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
Homo sapiens
pH 7.4, 30°C
0.01
propyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
Homo sapiens
above, pH 7.5, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the mature PR3 has an inactive conformation in the acidic environment of the azurophilic granules, and becomes active upon translocation to a neutral pH environment
additional information
-
the mature PR3 has an inactive conformation in the acidic environment of the azurophilic granules, and becomes active upon translocation to a neutral pH environment
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
663599, 663606, 664451, 664822, 664898, 664960, 665530, 665647, 665920, 665985, 666198, 666199, 666751, 683193
SwissProt
brenda
-
-
-
brenda
-
697411, 698376, 707117, 707129, 707316, 707322, 707338, 707736, 708497, 709030, 709349, 709372, 709431, 709688, 709758, 710661, 717507, 717575, 717959, 718119
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
increased PR-3 on the alveolar macrophage surface in usual interstitial pneumonia relative to healthy controls and sarcoidosis subjects
brenda
PR3 plasma concentrations are increased in patients with liver steatosis
brenda
proteinase 3 is considerably more expressed in bone marrow than in the peripheral blood
brenda
additional information
-
cell associated PR3 levels are lower than in neutrophils, thus sensitivity of the indirect immunofluorescence test is lower
brenda
-
-
brenda
blood neutrophils from patients with active Wegener’s granulomatosis bear greater amounts of PR3 on their cell membranes than do neutrophils from healthy individuals
brenda
-
endogenous annexin 1 and PR3 localization in resting and stimulated blood neutrophils
brenda
-
high molecular weight complexes of unstimulated neutrophils comprise PR3, FcgammaRIIIb, the beta2 integrin CD11b/CD18, the membrane and cytosolic subunits of the NADPH oxidase, p22phox and p47phox/p67phox
brenda
-
targeting to granules is not dependent on glycosylation, but unglycosylated recombinant PR3 gets secreted preferentially into media supernatants
brenda
-
neutrophil extracts from vasculitis patients and healthy controls contain comparable amounts of PR3
brenda
neutrophil membrane expression of PR3 increases during both activation and apoptosis
brenda
-
presence of anti-complementary PR3 and anti-PR3 antibodies in human Wegener’s granulomatosis sera
brenda
-
cell associated PR3 levels are lower than in neutrophils, thus sensitivity of the indirect immunofluorescence test is lower
brenda
additional information
neutrophil-dereived PR3 is more potent than urinary PR3
brenda
additional information
-
neutrophil-dereived PR3 is more potent than urinary PR3
brenda
additional information
mRNA for PR3 is transcribed in the promyelocyte and promonocyte stages of myeloid differentiation. Present in mastocytes and no-hematopoietic cell
brenda
additional information
-
mRNA for PR3 is transcribed in the promyelocyte and promonocyte stages of myeloid differentiation. Present in mastocytes and no-hematopoietic cell
brenda
additional information
-
PR3 antigen is usually present in granulomas and antigen-presenting cells are found in these lesions as well
brenda
additional information
proteinase 3 is expressed by myeloid cells and localized within azurophil granules, it is also expressed on the cellular membrane of polymorphonuclear neutrophils (PMN)
brenda
additional information
the neutrophil membrane mPR3 is highly induced in patients with sepsis
brenda
additional information
-
the neutrophil membrane mPR3 is highly induced in patients with sepsis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
from human polymorphonuclear leukocytes (PMNL)
brenda
-
major pool of intracellular PR3 is within the azurophilic granules
brenda
a major neutrophilic serine protease expressed in neutrophil azurophil granules
brenda
-
strong correlation between PR3 and CD177 surface expression
brenda
-
low levels, CD177 is a receptor for PR3 on the neutrophil membrane, but in CD177 negative neutrophils PR3 is also present and is susceptible to PR3-anti-neutrophil cytoplasmic autoantibodies (ANCA) induced neutrophil activation
brenda
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hydrophobic patch F180-F181-L228-F229 is essential for PR3 membrane anchorage. PR3 membrane insertion appears to be pivotal for its proinflammatory activities, such as extracellular proteolysis and impairment of apoptotic cell clearance, but also for myeloid cell proliferation
brenda
-
behaves as a peripheral membrane protein. The mouse form is globally more electronegative than the human form. As a consequence of differences in sequence and structural properties, mouse PR3 is likely to be able to bind to the plasma membrane using the same region as human PR3, although less strongly and specifically
brenda
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PR3 and CD177 exhibit a dynamic plasma membrane expression with rapid internalization and re-expression
brenda
neutrophil membrane expression of PR3 increases during both activation and apoptosis. Membrane expression of PR3 is increased in patients with granulomatosis with polyangiitis. Membrane anchorage of PR3 is dependent on the hydrophobic patch containing four hydrophobic amino acids, Phe180, Phe181, Leu228, and Phe229, molecular simulations. Phospholipid scramblase 1 (PLSCR1) knockdown using siRNA prevents PR3 membrane expression
brenda
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the extragranular pool of PR3, which is externalized during apoptosis, may be functionally very important in the pathophysiology of vasculitis
-
brenda