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(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
?
-
-
-
?
(VGVAPG)2V + H2O
?
-
pH 8.6, room temperature
-
-
?
(VGVAPG)3V + H2O
?
-
pH 8.6, room temperature
-
-
?
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-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-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
-
-
-
?
2-aminobenzoyl-VADCAQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-VAECCQ-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-GIATDCRDRPEQ-EDDnp + H2O
?
-
-
-
-
?
Abz-GIATFCDLMPEQ-EDDnp + H2O
?
-
-
-
-
?
Abz-GIATFCMKMPEQ-EDDnp + H2O
?
-
-
-
-
?
Abz-GIATFCMLMPEQ-EDDnp + H2O
?
-
-
-
-
?
Abz-GIATFCRLMPEQ-EDDnp + H2O
?
-
-
-
-
?
Abz-GRATFCMLMPEQ-EDDnp + H2O
?
-
-
-
-
?
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-VADCADQ-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
Abz-VADCADQ-EDDnp + H2O
?
-
-
-
-
?
Abz-VADCADQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
Abz-VADCADQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
Abz-VADCADRQ-EDDnp + H2O
Abz-VADCA + DRQ-EDDnp
-
-
-
-
?
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-EDDnp + H2O
?
-
-
-
-
?
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-VADCDDRQ-EDDnp + H2O
Abz-VADCD + DRQ-EDDnp
-
-
-
-
?
Abz-VADCRDRQ-EDDnp + H2O
Abz-VADCR + DRQ-EDDnp
Abz-VADnVADRQ-EDDnp + H2O
Abz-VADnVA + DRQ-EDDnp
-
-
-
-
?
Abz-VADnVADYQ-EDDnp + H2O
?
-
-
-
-
?
Abz-VADnVRDRQ-EDDnp + H2O
Abz-VADnVR + DRQ-EDDnp
-
-
-
-
?
Abz-VADnVRDYQ-EDDnp + H2O
?
-
-
-
-
?
Abz-VADVKDRQ-EDDnp + H2O
Abz-VADVK + DRQ-EDDnp
-
-
-
-
?
Abz-VADVKDRQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
-
-
-
-
?
Abz-Val-Ala-Asp-Nvl-Ala-Asp-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
Abz-VARCRDRQ-EDDnp + H2O
Abz-VARCR + DRQ-EDDnp
-
-
-
-
?
Ac-Ala-Ala-Pro-Ala-p-nitroanilide + H2O
?
-
-
-
?
Ac-Ala-Ala-Pro-Val-p-nitroanilide + 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
-
-
?
APG(VGVAPG)2V + H2O
?
-
pH 8.6, room temperature
-
-
?
azocasein + H2O
fragments of azocasein
-
-
-
-
-
BID + H2O
?
-
37°C, Bid = BH3 interacting domain death agonist
-
-
?
Boc-Ala-Ala-Nva-SBzl + H2O
?
-
-
-
?
Boc-Ala-Ala-Nva-thiobenzyl ester + H2O
?
-
-
-
-
?
Boc-Ala-Ala-Nva-thiobenzylester + H2O
?
-
pH 8.6, room temperature
-
-
?
Boc-Ala-Ala-Pro-Ala-p-nitroanilide + H2O
?
-
-
-
?
Boc-Ala-ONp + H2O
?
-
the reaction is not inhibited by antibody MCPR3-7 binding
-
-
?
Boc-Ala-Pro-Nva-4-chloro-thiobenzyl ester + H2O
?
Boc-Ala-Pro-Nva-SBzl + H2O
?
-
-
-
?
Boc-Ala-Pro-Nva-thiobenzylester + H2O
?
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
-
-
-
DRDAVDRDID + H2O
?
-
-
-
-
?
DVARVKDRQEG + H2O
?
-
-
-
-
?
Elastin + H2O
Hydrolyzed elastin
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 18.5ā102 nanomol)
-
-
?
Fibronectin + H2O
Hydrolyzed fibronectin
-
-
-
-
-
For-Ala-Ala-Pro-Abu-SBzl + H2O
?
-
the reaction is partly inhibited by antibody MCPR3-7 binding
-
-
?
GDVAVYEEN + H2O
?
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
-
IL-1beta + H2O
?
-
-
-
-
?
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
-
-
?
laminin + H2O
fragments of laminin
-
-
-
-
-
Mca-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
-
-
-
?
MeO-Suc-Ala-Ala-Pro-Val-4-nitroanilide + H2O
MeO-Suc-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
MeO-Suc-Lys-(pico)-Ala-Pro-Val-thiobenzylester + H2O
?
-
25°C
-
-
?
MeOSuc-AAPV-4-nitroanilide + H2O
MeOSuc-AAPV + 4-nitroaniline
MeOSuc-AIPM-4-nitroanilide + H2O
MeOSuc-AIPM + 4-nitroaniline
MeOSuc-Ala-Ala-Pro-Val-p-nitroanilide + H2O
?
-
-
-
?
MeOSuc-Lys(2-picolinoyl)-Ala-Pro-Val-p-nitroanilide + H2O
?
-
-
-
?
MeOSuc-Lys(2-picolinoyl)-Tyr-Asp-Ala-p-nitroanilide + H2O
?
-
-
-
?
MeOSuc-Lys(2-picolinoyl)-Tyr-Asp-Val-p-nitroanilide + H2O
?
-
-
-
?
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 4,4ā-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
-
-
?
N-Boc-Ala-o-nitrophenol + H2O
?
-
37°C, pH 7.4
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-pNA + H2O
?
-
-
-
-
?
N-t-Boc-L-alanine-p-nitrophenyl-ester + H2O
?
-
-
-
?
NF-kappaB + H2O
?
-
-
-
-
?
NFkappaB + H2O
?
-
-
-
-
?
nuclear factor-kappaB + H2O
?
-
-
-
-
?
oxidized insulin B chain + H2O
?
PAR-2 + H2O
?
-
PAR-2 = protease-activated receptor 2
-
-
?
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
-
-
-
pro-TNFalpha + H2O
?
-
-
-
-
?
procaspase 3 + H2O
?
-
PR3 can cleave membrane-associated procaspase 3 into a 22 kDa fragment
-
-
?
proIL-1beta + H2O
active IL-1beta + ?
-
is processed by PR3 or caspase 1
-
-
?
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)
-
-
?
protease-activated receptor-2 + H2O
?
-
-
-
-
?
RDVARCRDRQEG + H2O
?
-
-
-
-
?
RDVARCRDRQQG + H2O
?
-
-
-
-
?
Suc-AAA-4-nitroanilide + H2O
Suc-AAA + 4-nitroaniline
Suc-AAPL-4-nitroanilide + H2O
Suc-AAPL + 4-nitroaniline
Suc-AAPV-4-nitroanilide + H2O
Suc-AAPV + 4-nitroaniline
Suc-Ala-Ala-Asp-Val-p-nitroanilide + H2O
?
-
-
-
?
Suc-Ala-Ala-Glu-Val-p-nitroanilide + H2O
?
-
-
-
?
Suc-Ala-Ala-Pro-2-aminobutyric acid-p-nitroanilide + H2O
?
-
-
-
?
Suc-Ala-Ala-Pro-Ala-p-nitroanilide + H2O
?
-
-
-
?
Suc-Ala-Ala-Pro-Ile-p-nitroanilide + H2O
?
-
-
-
?
Suc-Ala-Ala-Pro-Nva-p-nitroanilide + H2O
?
-
-
-
?
Suc-Ala-Ala-Pro-Val-p-nitroanilide + H2O
?
-
-
-
?
Suc-Ala-Tyr-Leu-Val-p-nitroanilide + H2O
?
-
-
-
?
Suc-Ala4-p-nitroanilide + H2O
?
-
-
-
?
Suc-Leu-Val-Glu-Ala-p-nitroanilide + H2O
?
-
-
-
?
Succinyl-Ala-Ala-norvaline thiobenzyl ester + H2O
?
-
-
-
-
-
surfactant protein D + H2O
?
Tert-Butyloxycarbonyl-Ala-Ala-Ala thiobenzyl ester + H2O
?
-
-
-
-
-
Tert-Butyloxycarbonyl-Ala-Ala-Ile thiobenzyl ester + H2O
?
-
-
-
-
-
Tert-Butyloxycarbonyl-Ala-Ala-Met thiobenzyl ester + H2O
?
-
-
-
-
-
Tert-Butyloxycarbonyl-Ala-Ala-norvaline thiobenzyl ester + H2O
?
-
best substrate
-
-
-
Tert-Butyloxycarbonyl-Ala-Ala-Val thiobenzyl ester + H2O
?
-
-
-
-
-
TNF-alpha + H2O
?
-
-
-
-
?
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
-
-
-
Vitronectin + H2O
Hydrolyzed vitronectin
-
-
-
-
-
additional information
?
-
Abz-VADCADQ-ethylene diamine 2,4 dinitrophenyl + H2O

?
-
-
-
-
-
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
-
-
-
-
?
Abz-VADCRDRQ-EDDnp + H2O
Abz-VADCR + DRQ-EDDnp
-
best synthetic substrate
-
-
?
Boc-Ala-Pro-Nva-4-chloro-thiobenzyl ester + H2O

?
-
-
-
-
?
Boc-Ala-Pro-Nva-4-chloro-thiobenzyl ester + H2O
?
-
-
-
-
?
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
-
-
?
Elastin + H2O

Hydrolyzed elastin
-
-
-
-
-
Elastin + H2O
Hydrolyzed elastin
-
-
-
-
?
IL-32 + H2O

?
-
-
-
-
?
IL-32 + H2O
?
-
37°C
-
-
?
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

?
-
-
-
-
?
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
-
-
?
p21 + H2O

?
-
-
-
-
?
p21 + H2O
?
-
37°C, cleavage occurs between Thr80 and Gly81
-
-
?
p21 + H2O
?
-
pH 7.4, 30°C
-
-
?
p21 protein + H2O

?
-
-
-
?
p21 protein + H2O
?
-
-
-
?
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
-
?
surfactant protein D + H2O
?
-
-
a fragment of about 35000 Da
-
?
VADVKDR + H2O

?
-
37°C, pH 7.4, 0.75 M NaCl
-
-
?
VADVKDR + H2O
?
-
highly specific of and efficiently cleaved by human PR3
-
-
?
VARVRDR + H2O

?
-
-
-
-
?
VARVRDR + H2O
?
-
-
-
-
?
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 cleavage of IFN-alpha2
-
-
-
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
?
-
-
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
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(DL)-5-benzyl-3-(phenylsulfonylmethyl)-1-benzylhydantoin
-
-
(DL)-5-benzyl-3-(phenylsulfonylmethyl)hydantoin
-
-
(DL)-5-benzyl-3-(phenylthiomethyl)-1-benzylhydantoin
-
-
(DL)-5-benzyl-3-(phenylthiomethyl)hydantoin
-
-
(DL)-5-benzylhydantoin
-
-
(DL)-5-isobutyl-3-(phenylsulfonylmethyl)-1-benzylhydantoin
-
-
(DL)-5-isobutyl-3-(phenylsulfonylmethyl)hydantoin
-
-
(DL)-5-isobutyl-3-(phenylthiomethyl)-1-benzylhydantoin
-
-
(DL)-5-isobutyl-3-(phenylthiomethyl)hydantoin
-
-
(DL)-5-isobutylhydantoin
-
-
(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)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
-
-
(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
-
-
(Z)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
-
-
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%
2-hydroxyethyl 2-(4-(pivaloyloxy)phenylsulfonamido)benzoate
-
-
3,4-dichloroisocoumarin
-
-
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-(2-aminoethyl)benzenesulfonyl fluoride
-
-
4-(N-(2-(2-hydroxyethylcarbamoyl)phenyl)sulfamoyl)phenyl pivalate
-
-
4-(N-(2-acetylphenyl)sulfamoyl)phenyl 2-methylpropane-2-sulfinate
-
-
4-(N-(2-acetylphenyl)sulfamoyl)phenyl pivalate
-
-
4-(N-(2-butyrylphenyl)sulfamoyl)phenyl pivalate
-
-
4-(N-(2-formylphenyl)sulfamoyl)phenyl 2-methylpropane-2-sulfinate
-
-
4-(N-(2-formylphenyl)sulfamoyl)phenyl pivalate
-
-
4-(N-(2-pentanoyl phenyl)sulfamoyl)phenyl pivalate
-
-
4-(N-(2-propionylphenyl)sulfamoyl)phenyl pivalate
-
-
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
-
-
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
-
-
7-Amino-4-chloro-3-(2-bromoethoxy)isocoumarin
-
-
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
-
alpha-1-proteinase inhibitor serpin
-
-
-
alpha1-protease inhibitor
-
alpha1-proteinase
-
does not inhibit when PR3 is bound to the outer cell surface of neutrophils
-
Alpha1-proteinase inhibitor
-
alpha2-Macroglobulin
-
-
-
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
-
anti-PR3
-
partially inhibits PR3-induced kininogen reaction
-
benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone
diisopropyl fluorophosphate
-
-
diisopropylfluorophosphate
-
irreversible inhibition
ethyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
-
-
ethyl 2-(4-(pivaloyloxy)benzamido)benzoate
-
-
MeO-Suc-AAPA-chloromethyl ketone
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-(pivaloyloxy)benzamido)benzoate
-
-
methyl 2-(4-pivalamidophenylsulfonamido)benzoate
-
-
monocyte-neutrophil elastase inhibitor
-
-
-
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%
phenylmethylsulfonyl fluoride
-
-
Phenylmethylsulphonylfluoride
-
-
phosphatidylinositol-specific phospholipase C
-
-
-
propyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
-
-
propyl 2-(4-(pivaloyloxy)benzamido)benzoate
-
-
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
-
serpin LEX032
-
reactive site variant of alpha-1-ACT
-
siRNA
-
less PR3 externalization in the presence of rPLSCR1 siRNA
-
Soybean trypsin inhibitor
-
-
-
Substituted isocoumarins
-
-
-
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%
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
-
physiologic inhibitor of PR3
-
alpha1-antitrypsin
-
endogenous inhibitor of PR3
-
alpha1-antitrypsin
-
inhibition of bilayer-bound PR3 is more important than that observed for the soluble form of the enzyme
-
alpha1-antitrypsin
-
inhibits PR3-induced kininogen reaction
-
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

-
50-70% inhibition
-
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
-
-
-
alpha1-protease inhibitor
-
purified human alpha1-protease inhibitor inhibits gibbon PR3 and forms a covalently linked complex with it
-
Alpha1-proteinase inhibitor

-
-
-
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
-
benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone

-
-
benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone
-
-
Eglin c

-
weak
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
-
lactacystin

-
-
MeO-Suc-AAPA-chloromethyl ketone

-
poor inhibition
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
PMSF

-
inhibits activity, binding of IL-32 to PR3 is not inhibited
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
-
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, structureāactivity 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
-
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6.5
2-aminobenzoyl-VADCADQ-EDDnp
-
-
12.3
2-aminobenzoyl-VADCAQ-EDDnp
-
-
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
3.1
Abz-VADCADRQ-EDDnp
-
-
0.0065
Abz-VADCADY(NO2)
-
37°C, pH 7.4, 150 mM NaCl
12
Abz-VADCDDRQ-EDDnp
-
-
3.3
Abz-VADCRDRQ-EDDnp
-
-
2.7
Ac-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.4, 25°C
2.8
Ac-Ala-Ala-Pro-Val-p-nitroanilide
-
pH 7.4, 25°C
2
Boc-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.4, 25°C
1.1 - 1.2
MeOSuc-AAPV-4-nitroanilide
0.61 - 1.5
MeOSuc-AIPM-4-nitroanilide
0.47
MeOSuc-Ala-Ala-Pro-Val-p-nitroanilide
-
pH 7.4, 25°C
0.14
MeOSuc-Lys(2-picolinoyl)-Ala-Pro-Val-p-nitroanilide
-
pH 7.4, 25°C
0.1
MeOSuc-Lys(2-picolinoyl)-Tyr-Asp-Ala-p-nitroanilide
-
pH 7.4, 25°C
0.013
MeOSuc-Lys(2-picolinoyl)-Tyr-Asp-Val-p-nitroanilide
-
pH 7.4, 25°C
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
2.5 - 3.7
Suc-AAPV-4-nitroanilide
0.62
Suc-Ala-Ala-Asp-Val-p-nitroanilide
-
pH 7.4, 25°C
0.97
Suc-Ala-Ala-Glu-Val-p-nitroanilide
-
pH 7.4, 25°C
0.38
Suc-Ala-Ala-Pro-2-aminobutyric acid-p-nitroanilide
-
pH 7.4, 25°C
1.9
Suc-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.4, 25°C
0.64
Suc-Ala-Ala-Pro-Ile-p-nitroanilide
-
pH 7.4, 25°C
0.5
Suc-Ala-Ala-Pro-Nva-p-nitroanilide
-
pH 7.4, 25°C
0.6
Suc-Ala-Ala-Pro-Val-p-nitroanilide
-
pH 7.4, 25°C
0.17
Suc-Ala-Tyr-Leu-Val-p-nitroanilide
-
pH 7.4, 25°C
0.9
Suc-Leu-Val-Glu-Ala-p-nitroanilide
-
pH 7.4, 25°C
0.148
succinyl-Ala-Ala-norvaline-thiobenzyl ester
-
-
0.106
tert-butyloxycarbonyl-Ala-Ala-Ala-thiobenzyl ester
-
-
0.031
tert-butyloxycarbonyl-Ala-Ala-Ile-thiobenzyl ester
-
-
0.061
tert-butyloxycarbonyl-Ala-Ala-Met-thiobenzyl ester
-
-
0.063
tert-butyloxycarbonyl-Ala-Ala-norvaline-thiobenzyl ester
-
-
0.028
tert-butyloxycarbonyl-Ala-Ala-Val-thiobenzyl ester
-
-
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
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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
13.2
Ac-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.4, 25°C
60
Ac-Ala-Ala-Pro-Val-p-nitroanilide
-
pH 7.4, 25°C
18
Boc-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.4, 25°C
0.59 - 6.2
MeOSuc-AAPV-4-nitroanilide
0.26 - 7.2
MeOSuc-AIPM-4-nitroanilide
30
MeOSuc-Ala-Ala-Pro-Val-p-nitroanilide
-
pH 7.4,25°C
138
MeOSuc-Lys(2-picolinoyl)-Ala-Pro-Val-p-nitroanilide
-
H 7.4, 25°C
192
MeOSuc-Lys(2-picolinoyl)-Tyr-Asp-Ala-p-nitroanilide
-
H 7.4, 25°C
660
MeOSuc-Lys(2-picolinoyl)-Tyr-Asp-Val-p-nitroanilide
-
H 7.4, 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
0.37 - 11.2
Suc-AAPV-4-nitroanilide
84
Suc-Ala-Ala-Asp-Val-p-nitroanilide
-
pH 7.4, 25°C
60
Suc-Ala-Ala-Glu-Val-p-nitroanilide
-
pH 7.4, 25°C
30
Suc-Ala-Ala-Pro-2-aminobutyric acid-p-nitroanilide
-
pH 7.4, 25°C
13.8
Suc-Ala-Ala-Pro-Ala-p-nitroanilide
-
pH 7.4, 25°C
16.2
Suc-Ala-Ala-Pro-Ile-p-nitroanilide
-
pH 7.4, 25°C
5.4
Suc-Ala-Ala-Pro-Nva-p-nitroanilide
-
pH 7.4, 25°C
12
Suc-Ala-Ala-Pro-Val-p-nitroanilide
-
pH 7.4, 25°C
3 - 6
Suc-Ala-Tyr-Leu-Val-p-nitroanilide
-
pH 7.4, 25°C
2 - 22.2
Suc-Leu-Val-Glu-Ala-p-nitroanilide
19
Succinyl-Ala-Ala-norvaline thiobenzyl ester
-
-
10.1
tert-butyloxycarbonyl-Ala-Ala-Ala thiobenzyl ester
-
-
1.9
tert-butyloxycarbonyl-Ala-Ala-Ile thiobenzyl ester
-
-
12.2
tert-butyloxycarbonyl-Ala-Ala-Met thiobenzyl ester
-
-
63.3
tert-butyloxycarbonyl-Ala-Ala-norvaline thiobenzyl ester
-
-
10.4
tert-butyloxycarbonyl-Ala-Ala-Val thiobenzyl ester
-
-
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
2 - 8
Suc-Leu-Val-Glu-Ala-p-nitroanilide

-
pH 7.4, 25°C
22.2
Suc-Leu-Val-Glu-Ala-p-nitroanilide
-
pH 7.4, 25°C
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Kam, C.M.; Kerrigan, J.E.; Dolman, K.M.; Goldschmeding, R.; von dem Borne, A.E.G.K.; Powers, J.C.
Substrate and inhibitor studies on proteinase 3
FEBS Lett.
297
119-123
1992
Homo sapiens
brenda
Labbaye, C.; Musette, P.; Cayre, Y.E.
Wegener autoantigen and myeloblastin are encoded by a single mRNA
Proc. Natl. Acad. Sci. USA
88
9253-9256
1991
Homo sapiens
brenda
Rao, N.V.; Wehner, N.G.; Marshall, B.C.; Gray, W.R.; Gray, B.H.; Hoidal, J.R.
Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties
J. Biol. Chem.
266
9540-9548
1991
Homo sapiens
brenda
Brubaker, M.J.; Groutas, W.C.; Hoidal, J.R.; Rao, N.V.
Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters
Biochem. Biophys. Res. Commun.
188
1318-1324
1992
Homo sapiens
brenda
Hoidal, J.R.; Rao, N.V.; Gray, B.
Myeloblastin: leukocyte proteinase 3
Methods Enzymol.
244
61-67
1994
Homo sapiens
brenda
Dolman, K.M.; van de Wiel, B.A.; Kam, C.M.; Abbink, J.J.; Hack, C.E.; Sonnenberg, A.; Powers, J.C.; van dem Borne, A.E.G.K.; Goldscheding, R.
Determination of proteinase 3-alpha 1-antitrypsin complexes in inflammatory fluids
FEBS Lett.
314
117-121
1992
Homo sapiens
brenda
Renesto, P.; Halbwachs-Mecarelli, L.; Nusbaum, P.; Lesavre, P.; Chignard, M.
Proteinase 3. A neutrophil proteinase with activity on platelets
J. Immunol.
152
4612-4617
1994
Homo sapiens
brenda
Rao, N.V.; Rao, G.V.; Marshall, B.C.; Hoidal, J.R.
Biosynthesis and processing of proteinase 3 in U937 cells. Processing pathways are distinct from those of cathepsin G
J. Biol. Chem.
271
2972-2978
1996
Homo sapiens
brenda
Dolman, K.M.; van de Wiel, B.A.; Kam, C.M.; Kerrigan, J.E.; Hack, C.E.; van dem Borne, A.E.G.K.; Powers, J.C.; Goldschmeding, R.
Proteinase 3: substrate specificity and possible pathogenetic effect of Wegeners granulomatosis autoantibodies (c-ANCA) by dysregulation of the enzyme
Adv. Exp. Med. Biol.
336
55-60
1993
Homo sapiens
brenda
Wiedow, O.; Luedemann, J.; Utecht, B.; Christophers, E.
Inhibition of proteinase 3 activity by peptides derived from human epidermis
Adv. Exp. Med. Biol.
336
61-66
1993
Homo sapiens
brenda
Korkmaz, B.; Attucci, S.; Hazouard, E.; Ferrandiere, M.; Jourdan, M.L.; Brillard-Bourdet, M.; Juliano, L.; Gauthier, F.
Discriminating between the activities of human neutrophil elastase and proteinase 3 using serpin-derived fluorogenic substrates
J. Biol. Chem.
277
39074-39081
2002
Homo sapiens
brenda
Groutas, W.C.; Ruan, S.; Kuang, R.; Hook, J.B.; Sands, H.
Inhibition of human leukocyte proteinase 3 by a novel recombinant serine proteinase inhibitor (LEX032)
Biochem. Biophys. Res. Commun.
233
697-699
1997
Homo sapiens
brenda
Groutas, W.C.; Kuang, R.; Ruan, S.; Epp, J.B.; Venkataraman, R.; Truong, T.M.
Potent and specific inhibition of human leukocyte elastase, cathepsin G and proteinase 3 by sulfone derivatives employing the 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold
Bioorg. Med. Chem.
6
661-671
1998
Homo sapiens
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He, S.; Kuang, R.; Venkataraman, R.; Tu, J.; Truong, T.M.; Chan, H.K.; Groutas, W.C.
Potent inhibition of serine proteases by heterocyclic sulfide derivatives of 1,2,5-thiadiazolidin-3-one 1,1 dioxide
Bioorg. Med. Chem.
8
1713-1717
2000
Homo sapiens
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Goldmann, W.H.; Niles, J.L.; Arnaout, M.A.
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Homo sapiens
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Witko-Sarsat, V.; Canteloup, S.; Durant, S.; Desdouets, C.; Chabernaud, R.; Lemarchand, P.; Descamps-Latscha, B.
Cleavage of p21waf1 by proteinase-3, a myeloid-specific serine protease, potentiates cell proliferation
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Homo sapiens, Rattus norvegicus
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Koehl, C.; Knight, C.G.; Bieth, J.G.
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Homo sapiens
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Campbell, E.J.; Campbell, M.A.; Owen, C.A.
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Homo sapiens
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Stummann, L.; Wiik, A.
A simple high yield procedure for purification of human proteinase 3, the main molecular target of cANCA
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Homo sapiens
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Korkmaz, B.; Attucci, S.; Moreau, T.; Godat, E.; Juliano, L.; Gauthier, F.
Design and use of highly specific substrates of neutrophil elastase and proteinase 3
Am. J. Respir. Cell Mol. Biol.
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Homo sapiens, Homo sapiens (P24158)
brenda
Lombard, C.; Bouchu, D.; Wallach, J.; Saulnier, J.
Proteinase 3 hydrolysis of peptides derived from human elastin exon 24
Amino Acids
28
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2005
Homo sapiens, Homo sapiens (P24158)
brenda
Csernok, E.; Ai, M.; Gross, W.L.; Wicklein, D.; Petersen, A.; Lindner, B.; Lamprecht, P.; Holle, J.U.; Hellmich, B.
Wegener autoantigen induces maturation of dendritic cells and licenses them for Th1 priming via the protease-activated receptor-2 pathway
Blood
107
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2006
Homo sapiens, Homo sapiens (P24158)
brenda
Zani, M.L.; Nobar, S.M.; Lacour, S.A.; Lemoine, S.; Boudier, C.; Bieth, J.G.; Moreau, T.
Kinetics of the inhibition of neutrophil proteinases by recombinant elafin and pre-elafin (trappin-2) expressed in Pichia pastoris
Eur. J. Biochem.
271
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2004
Homo sapiens, Homo sapiens (P24158)
brenda
Nobar, S.M.; Zani, M.L.; Boudier, C.; Moreau, T.; Bieth, J.G.
Oxidized elafin and trappin poorly inhibit the elastolytic activity of neutrophil elastase and proteinase 3
FEBS J.
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Homo sapiens (P24158)
brenda
Wiesner, O.; Litwiller, R.D.; Hummel, A.M.; Viss, M.A.; McDonald, C.J.; Jenne, D.E.; Fass, D.N.; Specks, U.
Differences between human proteinase 3 and neutrophil elastase and their murine homologues are relevant for murine model experiments
FEBS Lett.
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2005
Homo sapiens, Homo sapiens (P24158), Mus musculus, Mus musculus (Q61096)
brenda
Hirche, T.O.; Crouch, E.C.; Espinola, M.; Brokelman, T.J.; Mecham, R.P.; DeSilva, N.; Cooley, J.; Remold-O'Donnell, E.; Belaaouaj, A.
Neutrophil serine proteinases inactivate surfactant protein D by cleaving within a conserved subregion of the carbohydrate recognition domain
J. Biol. Chem.
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Homo sapiens, Homo sapiens (P24158), Mus musculus, Mus musculus (Q61096)
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Dublet, B.; Ruello, A.; Pederzoli, M.; Hajjar, E.; Courbebaisse, M.; Canteloup, S.; Reuter, N.; Witko-Sarsat, V.
Cleavage of p21/WAF1/CIP1 by proteinase 3 modulates differentiation of a monocytic cell line. Molecular analysis of the cleavage site
J. Biol. Chem.
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2005
Homo sapiens (P24158)
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Pederzoli, M.; Kantari, C.; Gausson, V.; Moriceau, S.; Witko-Sarsat, V.
Proteinase-3 induces procaspase-3 activation in the absence of apoptosis: potential role of this compartmentalized activation of membrane-associated procaspase-3 in neutrophils
J. Immunol.
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2005
Homo sapiens, Homo sapiens (P24158), Rattus norvegicus (Q8K597)
brenda
Hajjar, E.; Korkmaz, B.; Gauthier, F.; Brandsdal, B.O.; Witko-Sarsat, V.; Reuter, N.
Inspection of the binding sites of proteinase3 for the design of a highly specific substrate
J. Med. Chem.
49
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2006
Homo sapiens, Homo sapiens (P24158)
brenda
Schreiber, A.; Luft, F.C.; Kettritz, R.
Membrane proteinase 3 expression and ANCA-induced neutrophil activation
Kidney Int.
65
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2004
Homo sapiens (P24158)
brenda
Pendergraft, W.F.3rd.; Rudolph, E.H.; Falk, R.J.; Jahn, J.E.; Grimmler, M.; Hengst, L.; Jennette, J.C.; Preston, G.A.
Proteinase 3 sidesteps caspases and cleaves p21 Waf1/Cip1/Sdi1 to induce endothelial cell apoptosis
Kidney Int.
65
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2004
Homo sapiens, Homo sapiens (P24158)
brenda
Novick, D.; Rubinstein, M.; Azam, T.; Rabinkov, A.; Dinarello, C.A.; Kim, S.H.
Proteinase 3 is an IL-32 binding protein
Proc. Natl. Acad. Sci. USA
103
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2006
Homo sapiens, Homo sapiens (P24158)
brenda
Korkmaz, B.; Moreau, T.; Gauthier, F.
Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions
Biochimie
90
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2008
Homo sapiens, Homo sapiens (P24158)
brenda
Mueller, A.; Voswinkel, J.; Gottschlich, S.; Csernok, E.
Human proteinase 3 (PR3) and its binding molecules: implications for inflammatory and PR3-related autoimmune responses
Ann. N. Y. Acad. Sci.
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2007
Homo sapiens
brenda
Kantari, C.; Pederzoli-Ribeil, M.; Amir-Moazami, O.; Gausson-Dorey, V.; Moura, I.C.; Lecomte, M.C.; Benhamou, M.; Witko-Sarsat, V.
Proteinase 3, the Wegener autoantigen, is externalized during neutrophil apoptosis: evidence for a functional association with phospholipid scramblase 1 and interference with macrophage phagocytosis
Blood
110
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2007
Homo sapiens
brenda
Jenne, D.E.; Kuhl, A.
Production and applications of recombinant proteinase 3, Wegeners autoantigen: problems and perspectives
Clin. Nephrol.
66
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2006
Homo sapiens, Mus musculus
brenda
Csernok, E.; Moosig, F.; Gross, W.L.
Pathways to ANCA production: From differentiation of dendritic cells by proteinase 3 to B lymphocyte maturation in Wegeners granuloma
Clin. Rev. Allergy Immunol.
34
300-306
2008
Homo sapiens, Mus musculus
brenda
Hajjar, E.; Korkmaz, B.; Reuter, N.
Differences in the substrate binding sites of murine and human proteinase 3 and neutrophil elastase
FEBS Lett.
581
5685-5690
2007
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Specks, U.; Fass, D.N.; Finkielman, J.D.; Hummel, A.M.; Viss, M.A.; Litwiller, R.D.; McDonald, C.J.
Functional significance of Asn-linked glycosylation of proteinase 3 for enzymatic activity, processing, targeting, and recognition by anti-neutrophil cytoplasmic antibodies
J. Biochem.
141
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2007
Homo sapiens
brenda
Korkmaz, B.; Hajjar, E.; Kalupov, T.; Reuter, N.; Brillard-Bourdet, M.; Moreau, T.; Juliano, L.; Gauthier, F.
Influence of charge distribution at the active site surface on the substrate specificity of human neutrophil protease 3 and elastase. A kinetic and molecular modeling analysis
J. Biol. Chem.
282
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2007
Homo sapiens
brenda
Vong, L.; DAcquisto, F.; Pederzoli-Ribeil, M.; Lavagno, L.; Flower, R.J.; Witko-Sarsat, V.; Perretti, M.
Annexin 1 cleavage in activated neutrophils: a pivotal role for proteinase 3
J. Biol. Chem.
282
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Homo sapiens
brenda
Fridlich, R.; David, A.; Aviram, I.
Membrane proteinase 3 and its interactions within microdomains of neutrophil membranes
J. Cell. Biochem.
99
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2006
Homo sapiens
brenda
Bauer, S.; Abdgawad, M.; Gunnarsson, L.; Segelmark, M.; Tapper, H.; Hellmark, T.
Proteinase 3 and CD177 are expressed on the plasma membrane of the same subset of neutrophils
J. Leukoc. Biol.
81
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2007
Homo sapiens
brenda
Villegas-Mendez, A.; Montes, R.; Ambrose, L.R.; Warrens, A.N.; Laffan, M.; Lane, D.A.
Proteolysis of the endothelial cell protein C receptor by neutrophil proteinase 3
J. Thromb. Haemost.
5
980-988
2007
Homo sapiens
brenda
Borelli, C.; Ruge, E.; Schaller, M.; Monod, M.; Korting, H.C.; Huber, R.; Maskos, K.
The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A
Proteins
68
738-748
2007
Candida albicans
brenda
Damoiseaux, J.; Daehnrich, C.; Rosemann, A.; Probst, C.; Komorowski, L.; Stegeman, C.A.; Egerer, K.; Hiepe, F.; van Paassen, P.; Stoecker, W.; Schlumberger, W.; Tervaert, J.W.
A novel enzyme-linked immunosorbent assay using a mixture of human native and recombinant proteinase-3 significantly improves the diagnostic potential for antineutrophil cytoplasmic antibody-associated vasculitis
Ann. Rheum. Dis.
68
228-233
2009
Homo sapiens, Homo sapiens (P24158)
brenda
Armstrong, L.; Godinho, S.I.; Uppington, K.M.; Whittington, H.A.; Millar, A.B.
Tumour necrosis factor-alpha processing in interstitial lung disease: a potential role for exogenous proteinase-3
Clin. Exp. Immunol.
156
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2009
Homo sapiens
brenda
Kasuga, A.; Mandai, Y.; Katsuno, T.; Sato, T.; Yamaguchi, T.; Yokosuka, O.
Pulmonary complications resembling Wegeners granulomatosis in ulcerative colitis with elevated proteinase-3 anti-neutrophil cytoplasmic antibody
Intern. Med.
47
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2008
Homo sapiens
brenda
Wysocka, M.; Lesner, A.; Majkowska, G.; Legowska, A.; Guzow, K.; Rolka, K.; Wiczk, W.
The new fluorogenic substrates of neutrophil proteinase 3 optimized in prime site region
Anal. Biochem.
399
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2010
Homo sapiens
brenda
Wysocka, M.; Lesner, A.; Guzow, K.; Kulczycka, J.; Legowska, A.; Wiczk, W.; Rolka, K.
Highly specific substrates of proteinase 3 containing 3-(2-benzoxazol-5-yl)-l-alanine and their application for detection of this enzyme in human serum
Anal. Chem.
82
3883-3889
2010
Homo sapiens
brenda
Hu, N.; Westra, J.; Huitema, M.G.; Bijl, M.; Brouwer, E.; Stegeman, C.A.; Heeringa, P.; Limburg, P.C.; Kallenberg, C.G.
Coexpression of CD177 and membrane proteinase 3 on neutrophils in antineutrophil cytoplasmic autoantibody-associated systemic vasculitis: anti-proteinase 3-mediated neutrophil activation is independent of the role of CD177-expressing neutrophils
Arthritis Rheum.
60
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2009
Homo sapiens
brenda
Joosten, L.A.; Netea, M.G.; Fantuzzi, G.; Koenders, M.I.; Helsen, M.M.; Sparrer, H.; Pham, C.T.; van der Meer, J.W.; Dinarello, C.A.; van den Berg, W.B.
Inflammatory arthritis in caspase 1 gene-deficient mice: contribution of proteinase 3 to caspase 1-independent production of bioactive interleukin-1beta
Arthritis Rheum.
60
3651-3662
2009
Homo sapiens, Mus musculus
brenda
Hu, N.; Westra, J.; Kallenberg, C.G.
Membrane-bound proteinase 3 and its receptors: relevance for the pathogenesis of Wegeners Granulomatosis
Autoimmun. Rev.
8
510-514
2009
Homo sapiens
brenda
Dou, D.; He, G.; Li, Y.; Lai, Z.; Wei, L.; Alliston, K.R.; Lushington, G.H.; Eichhorn, D.M.; Groutas, W.C.
Utilization of the 1,2,3,5-thiatriazolidin-3-one 1,1-dioxide scaffold in the design of potential inhibitors of human neutrophil proteinase 3
Bioorg. Med. Chem.
18
1093-1102
2010
Homo sapiens
brenda
Hajjar, E.; Broemstrup, T.; Kantari, C.; Witko-Sarsat, V.; Reuter, N.
Structures of human proteinase 3 and neutrophil elastase - so similar yet so different
FEBS J.
277
2238-2254
2010
Homo sapiens, Mus musculus
brenda
Korkmaz, B.; Jaillet, J.; Jourdan, M.L.; Gauthier, A.; Gauthier, F.; Attucci, S.
Catalytic activity and inhibition of Wegener antigen proteinase 3 on the cell surface of human polymorphonuclear neutrophils
J. Biol. Chem.
284
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2009
Homo sapiens
brenda
Kahn, R.; Hellmark, T.; Leeb-Lundberg, L.M.; Akbari, N.; Todiras, M.; Olofsson, T.; Wieslander, J.; Christensson, A.; Westman, K.; Bader, M.; Mueller-Esterl, W.; Karpman, D.
Neutrophil-derived proteinase 3 induces kallikrein-independent release of a novel vasoactive kinin
J. Immunol.
182
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2009
Homo sapiens
brenda
Kuhl, A.; Korkmaz, B.; Utecht, B.; Kniepert, A.; Schoenermarck, U.; Specks, U.; Jenne, D.E.
Mapping of conformational epitopes on human proteinase 3, the autoantigen of Wegener's granulomatosis
J. Immunol.
185
387-399
2010
Homo sapiens, Hylobates pileatus, Macaca mulatta, Pan troglodytes verus
brenda
Geyer, M.; Kulamarva, G.; Davis, A.
Wegeners Granulomatosis presenting with an abscess in the parotid gland: a case report
J. Med. Case Rep.
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19
2009
Homo sapiens
brenda
Hajjar, E.; Dejaegere, A.; Reuter, N.
Challenges in pKa predictions for proteins: the case of Asp213 in human proteinase 3
J. Phys. Chem. A
113
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2009
Homo sapiens
brenda
Hua, F.; Wilde, B.; Dolff, S.; Witzke, O.
T-lymphocytes and disease mechanisms in Wegeners granulomatosis
Kidney Blood Press. Res.
32
389-398
2009
Homo sapiens
brenda
Piesche, M.; Hildebrandt, Y.; Chapuy, B.; Wulf, G.G.; Truemper, L.; Schroers, R.
Characterization of HLA-DR-restricted T-cell epitopes derived from human proteinase 3
Vaccine
27
4718-4723
2009
Homo sapiens
brenda
Abdgawad, M.; Gunnarsson, L.; Bengtsson, A.A.; Geborek, P.; Nilsson, L.; Segelmark, M.; Hellmark, T.
Elevated neutrophil membrane expression of proteinase 3 is dependent upon CD177 expression
Clin. Exp. Immunol.
161
89-97
2010
Homo sapiens
brenda
Kaellquist, L.; Rosen, H.; Nordenfelt, P.; Calafat, J.; Janssen, H.; Persson, A.M.; Hansson, M.; Olsson, I.
Neutrophil elastase and proteinase 3 trafficking routes in myelomonocytic cells
Exp. Cell Res.
316
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2010
Homo sapiens
brenda
Kantari, C.; Millet, A.; Gabillet, J.; Hajjar, E.; Broemstrup, T.; Pluta, P.; Reuter, N.; Witko-Sarsat, V.
Molecular analysis of the membrane insertion domain of proteinase 3, the Wegeners autoantigen, in RBL cells: implication for its pathogenic activity
J. Leukoc. Biol.
90
941-950
2011
Homo sapiens
brenda
Kim, Y.C.; Shin, J.E.; Lee, S.H.; Chung, W.J.; Lee, Y.S.; Choi, B.K.; Choi, Y.
Membrane-bound proteinase 3 and PAR2 mediate phagocytosis of non-opsonized bacteria in human neutrophils
Mol. Immunol.
48
1966-1974
2011
Homo sapiens
brenda
Broemstrup, T.; Reuter, N.
How does proteinase 3 interact with lipid bilayers?
Phys. Chem. Chem. Phys.
12
7487-7496
2010
Homo sapiens (P24158)
brenda
Relle, M.; Thomaidis, T.; Galle, P.R.; Schwarting, A.
Comparative aspects of murine proteinase 3
Rheumatol. Int.
31
1105-1111
2011
Mus musculus, Mus musculus (Q61096)
brenda
Hwang, T.L.; Wang, W.H.; Wang, T.Y.; Yu, H.P.; Hsieh, P.W.
Synthesis and pharmacological characterization of 2-aminobenzaldehyde oxime analogs as dual inhibitors of neutrophil elastase and proteinase 3
Bioorg. Med. Chem.
23
1123-1134
2015
Homo sapiens, Homo sapiens (P24158)
brenda
Hinkofer, L.C.; Hummel, A.M.; Stone, J.H.; Hoffman, G.S.; Merkel, P.A.; Spiera, E.R.; St Clair, W.; McCune, J.W.; Davis, J.C.; Specks, U.; Jenne, D.E.
Allosteric modulation of proteinase 3 activity by anti-neutrophil cytoplasmic antibodies in granulomatosis with polyangiitis
J. Autoimmun.
59
43-52
2015
Homo sapiens, Homo sapiens (P24158)
brenda
Hinkofer, L.C.; Seidel, S.A.; Korkmaz, B.; Silva, F.; Hummel, A.M.; Braun, D.; Jenne, D.E.; Specks, U.
A monoclonal antibody (MCPR3-7) interfering with the activity of proteinase 3 by an allosteric mechanism
J. Biol. Chem.
288
26635-26648
2013
Homo sapiens (P24158)
brenda
Budnjo, A.; Narawane, S.; Grauffel, C.; Schillinger, A.S.; Fossen, T.; Reuter, N.; Haug, B.E.
Reversible ketomethylene-based inhibitors of human neutrophil proteinase 3
J. Med. Chem.
57
9396-9408
2014
Homo sapiens, Homo sapiens (P24158)
brenda