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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-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-Abu-(5-amino-2-nitrobenzamide) + 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-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
?
-
-
-
?
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
-
-
?
APG(VGVAPG)2V + H2O
?
pH 8.6, room temperature
-
-
?
azocasein + H2O
fragments of azocasein
-
-
-
-
?
BID + H2O
?
37°C, Bid = BH3 interacting domain death agonist
-
-
?
biotinyl-Val-Tyr-Asp-Nva-4-nitroanilide + H2O
?
-
-
-
?
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 18.5102 nanomol)
-
-
?
Fibronectin + H2O
Hydrolyzed fibronectin
-
-
-
-
?
For-Ala-Ala-Pro-Abu-SBzl + H2O
?
the reaction is partly inhibited by antibody MCPR3-7 binding
-
-
?
GDVAVYEEN + H2O
?
-
-
-
-
?
GLLASLGL + H2O
GLLA + Ser + LGL
-
-
-
?
GLLFSLGL + H2O
GLLF + Ser + LGL
-
-
-
?
GLLISLGL + H2O
GLLI + Ser + LGL
-
-
-
?
GLLVALGL + H2O
GLLV + Ala + LGL
GLLVDLGL + H2O
GLLV + Asp + LGL
GLLVMLGL + H2O
GLLV + Met + LGL
GLLVRLGL + H2O
GLLV + Arg + LGL
GLLVSLGL + H2O
GLLV + Ser + LGL
GLLVWLGL + H2O
GLLV + Trp + LGL
GLLWSLGL + H2O
GLLW + Ser + LGL
-
-
-
?
GRGVAGGRG + H2O
GRGV + Ala + GGRG
-
-
-
-
?
GRGVSGGRG + H2O
GRGV + Ser + GGRG
-
-
-
-
?
GRGVVVGRG + H2O
GRGV + Val + Val + GRG
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
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 4,4-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
-
-
?
N-Boc-Ala-o-nitrophenol + H2O
?
37°C, pH 7.4
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-pNA + H2O
?
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
?
-
-
-
?
N-t-Boc-L-alanine-p-nitrophenyl-ester + H2O
?
-
-
-
?
NF-kappaB + H2O
?
-
-
-
?
NFkappaB + H2O
?
-
-
-
-
?
nuclear factor-kappaB + H2O
?
-
-
-
?
O-methyl-succinyl-Ala-Ala-Pro-Ala-S-benzyl ester + H2O
?
-
-
-
?
O-methyl-succinyl-Ala-Ala-Pro-Val-4-nitroanilide + 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
?
-
-
-
-
?
succinyl-Ala-Ala-Nva-S-benzyl ester + H2O
?
-
-
-
?
surfactant protein D + H2O
?
t-butyloxycarbonyl-Ala-Ala-Nva-thiobenzyl ester + 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-Nva-S-benzyl ester + H2O
?
-
-
-
?
Tert-Butyloxycarbonyl-Ala-Ala-Val thiobenzyl ester + H2O
?
-
-
-
-
?
tert-butyloxycarbonyl-Ala-Ala-Val-S-benzyl ester + H2O
?
-
-
-
?
tert-butyloxycarbonyl-Ala-O-4-nitrophenyl 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
-
-
-
-
?
VLLASEVL + H2O
VLLA + SEVL
-
-
-
-
?
VLLFSEVL + H2O
VLLF + SEVL
-
-
-
-
?
VLLISEVL + H2O
VLLI + SEVL
-
-
-
-
?
VLLVSEVL + 3 H2O
VLLV + Ser + Glu + VL
-
-
-
?
VLLVSEVL + H2O
VLLV + SEVL
-
-
-
-
?
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
-
-
-
?
GLLVALGL + H2O
GLLV + Ala + LGL
-
-
-
?
GLLVALGL + H2O
GLLV + Ala + LGL
-
-
-
-
?
GLLVDLGL + H2O
GLLV + Asp + LGL
-
-
-
?
GLLVDLGL + H2O
GLLV + Asp + LGL
-
-
-
-
?
GLLVMLGL + H2O
GLLV + Met + LGL
-
-
-
?
GLLVMLGL + H2O
GLLV + Met + LGL
-
-
-
-
?
GLLVRLGL + H2O
GLLV + Arg + LGL
-
-
-
?
GLLVRLGL + H2O
GLLV + Arg + LGL
-
-
-
-
?
GLLVSLGL + H2O
GLLV + Ser + LGL
-
-
-
?
GLLVSLGL + H2O
GLLV + Ser + LGL
-
-
-
-
?
GLLVWLGL + H2O
GLLV + Trp + LGL
-
-
-
?
GLLVWLGL + H2O
GLLV + Trp + LGL
-
-
-
-
?
IL-32 + H2O
?
-
-
-
-
?
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
-
?
protease-activated receptor-2 + H2O
?
-
-
-
-
?
protease-activated receptor-2 + H2O
?
-
-
-
?
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 cleavage of IFN-alpha2
-
-
?
additional information
?
-
no reaction with VGVAPGV and VAPGVGVAPGV
-
-
?
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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(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
(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
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%
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
-
-
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
-
-
7-amino-3-(2-bromoethoxy)-4-chloroisocoumarin
-
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
Ac-Pro-Tyr-Asp-AlaP(O-4-ClPh)2
-
Ac-Pro-Tyr-Phe-AlaP(O-4-ClPh)2
-
alpha-1 antitrypsin
AAT
-
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
-
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
biotin-Pro-Tyr-Asp-AbuP(O-4-ClPh)2
-
biotin-Pro-Tyr-Asp-AlaP(O-4-ClPh)2
-
biotin-Pro-Tyr-Asp-NvaP(O-4-ClPh)2
-
biotin-Val-Pro-LeuP(O-C6H4-4-COOCH3)2
-
biotin-Val-Pro-LeuP(OPh)2
-
biotin-Val-Tyr-Asp-AlaP(O-4-ClPh)2
-
biotin-Val-Tyr-Asp-NvaP(O-4-ClPh)2
-
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
biotin-[PEG]66-Pro-Tyr-Asp-AlaP(O-4-ClPh)2
-
-
BODIPY-FL-LN-Glu(OBzl)-Lys(Ac)-Pro(4-OBzl)-NvaP(OPh)2
-
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
MeO-Suc-Ala-Ala-Pro-ValP(OPh)2
-
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%
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
-
NH2+-Pro-Tyr-Asp-AlaP(O-4-ClPh)2
-
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%
(E)-4-(N-(2-(1-(hydroxyimino)butyl)phenyl)sulfamoyl)phenyl pivalate
-
(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)methyl)phenyl)sulfamoyl)phenyl pivalate
-
-
(E)-4-(N-(2-(1-(hydroxyimino)propyl)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
-
(E)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
-
-
(Z)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
-
(Z)-4-(N-(2-(1-(methoxyimino)ethyl)phenyl)sulfamoyl)phenyl pivalate
-
-
2-hydroxyethyl 2-(4-(pivaloyloxy)phenylsulfonamido)benzoate
-
2-hydroxyethyl 2-(4-(pivaloyloxy)phenylsulfonamido)benzoate
-
-
4-(N-(2-(2-hydroxyethylcarbamoyl)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-acetylphenyl)sulfamoyl)phenyl 2-methylpropane-2-sulfinate
-
-
4-(N-(2-acetylphenyl)sulfamoyl)phenyl pivalate
-
4-(N-(2-acetylphenyl)sulfamoyl)phenyl pivalate
-
-
4-(N-(2-butyrylphenyl)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 2-methylpropane-2-sulfinate
-
-
4-(N-(2-formylphenyl)sulfamoyl)phenyl pivalate
-
4-(N-(2-formylphenyl)sulfamoyl)phenyl pivalate
-
-
4-(N-(2-pentanoyl phenyl)sulfamoyl)phenyl pivalate
-
4-(N-(2-pentanoyl phenyl)sulfamoyl)phenyl pivalate
-
-
4-(N-(2-propionylphenyl)sulfamoyl)phenyl pivalate
-
4-(N-(2-propionylphenyl)sulfamoyl)phenyl pivalate
-
-
alpha1-antitrypsin
-
-
-
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
-
alpha2-Macroglobulin
-
-
-
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
-
-
-
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
-
ethyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
-
-
ethyl 2-(4-(pivaloyloxy)benzamido)benzoate
-
ethyl 2-(4-(pivaloyloxy)benzamido)benzoate
-
-
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
methyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
-
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
-
-
methyl 2-(4-(pivaloyloxy)benzamido)benzoate
-
methyl 2-(4-(pivaloyloxy)benzamido)benzoate
-
-
methyl 2-(4-pivalamidophenylsulfonamido)benzoate
-
methyl 2-(4-pivalamidophenylsulfonamido)benzoate
-
-
PMSF
-
-
PMSF
inhibits activity, binding of IL-32 to PR3 is not inhibited
propyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
-
propyl 2-(4-(3,3,3-trifluoro-2,2-dimethylpropanoyloxy)benzamido)benzoate
-
-
propyl 2-(4-(pivaloyloxy)benzamido)benzoate
-
propyl 2-(4-(pivaloyloxy)benzamido)benzoate
-
-
sivelestat
-
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, structureactivity relationship analysis, overview
-
additional information
-
synthesis and pharmacological characterization of 2-aminobenzaldehyde oxime analogues as dual inhibitors of neutrophil elastase and proteinase 3, structureactivity 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
-
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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
6.5
2-aminobenzoyl-VADCADQ-EDDnp
-
-
12.3
2-aminobenzoyl-VADCAQ-EDDnp
-
-
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
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
0.05
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
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
-
-
0.192
succinyl-Ala-Ala-Nva-S-benzyl ester
pH and temperature not specified in the publication
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
-
-
0.063
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
0.028
tert-butyloxycarbonyl-Ala-Ala-Val-thiobenzyl ester
-
-
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
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evolution
neutrophil serine proteases, proteinase 3 and human neutrophil elastase, share high sequence similarity, but have different substrate specificities and functions
evolution
-
presence of an elastase in Xenopus closely related to hPR-3 indicates a relatively early appearance of these enzymes during vertebrate evolution, sequence comparisons and phylogenetic analysis of the hematopoietic serine proteases, overview
evolution
presence of an elastase in Xenopus closely related to hPR-3 indicates a relatively early appearance of these enzymes during vertebrate evolution, sequence comparisons and phylogenetic analysis of the hematopoietic serine proteases, overview
malfunction
-
in mice lacking neutrophil serine PR3 (DPPI-/- mice), inhibition of caspase 1 activity results in decreased bioactive IL-1beta concentrations in the synovial tissue and less suppression of chondrocyte anabolic function. Dual blockade of both PR3 and caspase 1 leads to protection against cartilage and bone destruction. Deficiency of PR3 in combination with inhibition of caspase 1 does not reduce the joint swelling in streptococcal cell wall-induced acute arthritis
malfunction
excessive release of proteases mediates tissue damage
malfunction
overexpression of proteinase 3 in chronic myeloid leukemia induces apoptosis of high-affinity PR1-specific T cells, leading to deletional tolerance and leukemia outgrowth
malfunction
phospholipid scramblase 1 (PLSCR1) knockdown using siRNA not only prevents PR3 membrane expression but also increases the rate of apoptotic cell clearance by macrophages
malfunction
ratios between neutrophil serine proteases and their natural inhibitor are altered in non-alcoholic fatty liver disease (NAFLD) and type 2 diabetes when compared to healthy controls
metabolism
-
pro-PR3 interacts with CD63 upon heterologous co-expression in COS cells but endogenous interaction is not detected although cell surface proPR3 and CD63 are co-endocytosed in myelomonocytic cells. Cell surface pro-PR3 turns over more rapidly than cell surface CD63 consistent with processing/degradation of the pro-protease but recycling of CD63. Colocalization of proPR3 and CD63 with clathrin and Rab 7 suggests trafficking through coated vesicles and late endosomes. Blocking the C-terminus of pro-PR3 by creating a fusion with FK506 binding protein does not inhibit endosomal re-uptake of proPR3
metabolism
the enzyme is a target for chronic inflammatory diseases
metabolism
histone demethylase JMJD3 (EC 1.14.11.68) regulates the expression of neutrophil membrane proteinase 3 (mPR3) in lipopolysaccharide-stimulated neutrophils during the early inflammatory response in sepsis. JMJD3 regulates the expression of mPR3 by changing the level of trimethylated histone H3 on Lys27 (H3K27me3) in LPS-stimulated neutrophils
metabolism
increased proteinase 3 and neutrophil elastase (EC 3.4.21.37) plasma concentrations are associated with non-alcoholic fatty liver disease (NAFLD) and type 2 diabetes, potential role for the neutrophil serine proteases (NSPs), proteinase-3 (PR3) and neutrophil elastase (NE), in NAFLD as well as an imbalance between NSPs and their natural inhibitor alpha-1 antitrypsin (AAT). Circulating levels of NSPs associate with obesity-related metabolic disorders
metabolism
PR3 concentration in azurophilic granules is approximately 3 times higher than that of human neutrophil elastase and cathepsin G, and the enzyme is less susceptible to inhibition by endogenous serine protease inhibitors correlates with PR3 implication in various pathological processes
physiological function
-
69-year-old Caucasian female presenting initially with an isolated parotid abscess and only subsequently developing nasal, paranasal sinus and respiratory symptoms, shows anti-neutrophil cytoplasmic antibodies against proteinase 3 titres
physiological function
-
activation of IL-1beta in a manner independent of caspase 1 is especially apparent in the acute phase of inflammation, characterized by a predominantly neutrophilic infiltrate that serves as a source for PR3
physiological function
-
all c-ANCA-positive samples (diagnosed Wegener granulomatosis) show a significant increase of PR3 activity
physiological function
-
almost complete absence of anti-neutrophil cytoplasmic antibody (cANCA) binding to rhesus monkey PR3
physiological function
-
anti-neutrophil cytoplasmic antibodies (cANCAs) from Wegeners granulomatosis patients at least in part recognize similar surface structures as do mouse antibodies and compete with the binding of alpha1-protease inhibitor to PR3
physiological function
-
caspase 1-independent processing of IL-1beta occurs in arthritis by serine proteases such as PR3
physiological function
-
gibbon PR3 shows an intermediate anti-neutrophil cytoplasmic antibody (cANCA) binding pattern, whereas some anti-PR3 mouse antibodies and some patient sera recognize the antigen. The cANCAs from Wegeners granulomatosis patients at least in part recognize similar surface structures as do mouse antibodies and compete with the binding of alpha1-protease inhibitor to PR3
physiological function
-
involvement in the regulation of intracellular functions such as proliferation or apoptosis. Its membrane expression is a risk factor in chronic inflammatory diseases. PR3 is the preferred target antigen in Wegener's granulomatosis. Colocalization of PR3 with the integrin CD11b/CD18 (b2 integrin), the Fcgamma receptor FcgRIIIb and the p22phox subunit of cytochrome b558 in the membrane. Both PR3 and phospholipid scramblase 1 are associated within the same protein complex
physiological function
-
is a major anti-neutrophil cytoplasmic autoantibodies (ANCA)-antigen in Wegener's granulomatosis. Abnormally expressed membrane-bound PR3 is involved in the development and severity of Wegener's granulomatosis. Strong correlation of the percentages of membrane-bound PR3 high neutrophils between monozygotic twins but not in dizygotic twins. PR3 is externalized during neutrophil apoptosis independent of degranulation, which is mediated by phospholipid scramblase 1. CD177-deficient neutrophils also can be activated by PR3-anti-neutrophil cytoplasmic autoantibodies in vitro, thus CD177 is not necessary for this signaling
physiological function
-
macaque PR3 shows nearly no reactivity to anti-neutrophil cytoplasmic antibodies (cANCAs)
physiological function
-
neutrophil activation by PR3 antineutrophil cytoplasmic autoantibodies (ANCAs). CD177 may be a determinant of membrane expression of PR3 and, as such, influences the potential of neutrophils to be activated by PR3 ANCAs
physiological function
-
neutrophil-derived PR3 can induce kallikrein-independent activation of the kinin pathway
physiological function
-
occurrence of anti-neutrophil-cytoplasmic antibodies (ANCA) directed against proteinase-3 is a hallmark of Wegeners granulomatosis. Association of anti-PR3 titers and disease activity, which remains controversial. PR3 antigen elicits strong Th1-responses via dendritic cell maturation and subsequent antigen presentation to T-cells. Initial immune response in autoimmunity is directed against complementary PR3, resulting in the formation of antibodies against complementary PR3 (idiotypic response). Later on, an anti-idiotypic response against anti-complementary PR3 antibodies evolves. The antibodies formed during this anti-idiotypic response react to the sense autoantigen PR3. ANCA produced by granuloma-resident B cells bind to primed neutrophils that express PR3 on their surface. Genetic sequences complementary to human PR3 gene are detected in pathogens like Staphylococcus aureus, Ross River virus and Entamoeba histolytica. complementary PR3 transcripts are absent from healthy controls, PR3-ANCA-negative or lupus patients. Complementary PR3 mRNA is present in leukocytes of PR3-ANCA patients
physiological function
-
PRTN3-specific CD4+ T-cells precursors are part of normal human T-cell repertoires. T-cell precursors specific for various PRTN3 epitopes can be activated when properly stimulated. T-cell clones proliferate in response to peptides PRTN358 (GTLIHPSFVLTAAHALRDI), PRTN3216 (IDSFVIWGAATRLFPDFF), PRTN3235 (RVALYVDWIRSTLRR), and PRTN3241 (DWIRSTLRRVEAKGRP). T-cell clones specific for these four PRTN3 peptides strongly respond to autologous peripheral blood mononuclear cells in the presence of corresponding peptides. Only PRTN3235 is recognized by CD4+ T-cells as a naturally processed HLAclass-II-epitope. PRTN3235-specific CD4+ T-cells do not proliferate vigorously to stimulation with PRTN3-positive leukemia cell. PRTN3235 is able to induce T-cell responses in individuals with diverse DR genotypes
physiological function
-
significant Pr3 activity at the surface of activated neutrophils but not at the surface of quiescent neutrophils whatever the constitutive expression. Permanent presence of inactive Pr3 at the surface of quiescent neutrophils, which may explain why Pr3 is a major target of anti-neutrophil cytoplasmic antibodies, whose binding activates neutrophils and triggers inflammation, as in Wegener granulomatosis
physiological function
-
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
physiological function
proteinase 3 is a major autoimmune target in systemic vasculitis. Proteinase 3 is an abundant serine protease of neutrophil granules and a major target of PR3 antineutrophil cytoplasmic autoantibodies in granulomatosis with polyangiitis. Some of the enzyme synthesized by promyelocytes in the bone marrow escape the targeting to granules and occur on the plasma membrane of naive and primed neutrophils. This membrane-associated PR3 antigen may represent pro-PR3, mature PR3, or both forms
physiological function
the enzyme is involved in granulomatosis with polyangiitis, anti-neutrophil cytoplasmic antibodies with proteinase 3 specificity are not implicated in the pathogenesis
physiological function
effect of membrane proteinase 3-expressing polymorphonuclear neutrophils (PMN) and acute myeloid leukemia (AML) blasts on the proliferation of CD4 and CD8 T cells in vitro, overview. mP3-expressing PMN significantly inhibits autologous healthy donor T-cell proliferation but does not affect cytokine production in activated T-cells. This effect requires cell proximity and is abrogated by proteinase 3 blockade. This inhibition requires proteinase 3 enzyme activity. The suppression is not reversed by either the addition of catalase or the inhibition of arginase I. PMN inhibit T cell proliferation in a cell contact-dependent manner. In addition to proteinase 3 blockade, anti-low density lipoprotein receptor-related protein 1 (LRP1) Ab also restores T cells' capacity to proliferate. Dose-dependent inhibition of T-cell proliferation by mP3-expressing acute myeloid leukemia blasts
physiological function
membrane proteinase 3 (mPR3) expression on neutrophils plays a critical role in pro-inflammatory cytokine production. Plasma cytokine (interleukin-1beta and TNF-alpha) levels are increased in patients with sepsis exhibiting high mPR3 expression
physiological function
proteinase 3 (PR3), the autoantigen in granulomatosis with polyangiitis, is expressed at the plasma membrane of resting neutrophils, and this membrane expression increases during both activation and apoptosis. Proteinase 3 also is a phosphatidylserine-binding protein that affects the production and function of microvesicles. The interaction is dependent on the hydrophobic patch responsible for membrane anchorage. PR3 interacts with phosphatidylserine via a small number of amino acids, which engage in long lasting interactions with the lipid heads. The binding of PR3 to phosphatidylserine, a major component of microvesicles, leads to reduced production of microvesicles in PR3-expressing cells. PR3-expressing cells produce significantly fewer microvesicles during both activation and apoptosis, and this reduction is dependent on the ability of PR3 to associate with the membrane as mutating the hydrophobic patch restored microvesicle production. Activation-evoked microvesicles from PR3-expressing cells induce a significantly larger respiratory burst in human neutrophils compared with control microvesicles, while microvesicles generated during apoptosis inhibit the basal respiratory burst in human neutrophils, and those generated from PR3-expressing cells hamper this inhibition. Microvesicles generated from neutrophils expressing membrane PR3 may potentiate oxidative damage of endothelial cells and promote the systemic inflammation observed in this disease. PR3 hampers the ability of apoptosis-induced microvesicles to inhibit a respiratory burst in neutrophils. During apoptosis, membrane-bound PR3 serves as a 'don't eat me' signal. It is co-externalized with phosphatidylserine (PS) via its association with phospholipid scramblase 1 (PLSCR1), a protein facilitating membrane flip-flop
physiological function
the neutrophil serine protease proteinase-3 (PR3) is able to process interleukin-1beta to its bioactive form independently of caspase-1-NLRP3 inflammasome complex
physiological function
the neutrophilic serine protease proteinase 3 (PR3) is involved in inflammation and immune response and is a therapeutic target for a variety of infectious and inflammatory diseases
physiological function
the physiological role of PR3 is seen either inside the phagocytic vacuoles or externally where PR3 is engaged in processing of proinflammatory cytokines, receptors, heat shock proteins and other host proteins which after PR3-mediated hydrolysis lead to the generation of antibacterial peptides (e.g. cathelicidin hCAP-18). PR3 is capable of hydrolyzing several extracellular matrix proteins including collagen, elastin, fibronectin and laminin causing the inflammation and tissue injury. PR3 is also known as the antigen in granulomatosis with polyangiitis (GPA), a chronic inflammatory condition that triggers autoimmune response resulting in the production of antineutrophil cytoplasmic antibodies (ANCA). As the binding of ANCA activates neutrophils and therefore increases the level of cell surface PR3, the protein is directly involved in the pathogenesis of the disease
additional information
proteinase 3 is an abundant serine protease with high similarity to neutrophil elastase
additional information
enzyme-microvesicle interaction analysis by surface plasmon resonance spectroscopy. Molecular modeling
additional information
-
enzyme-microvesicle interaction analysis by surface plasmon resonance spectroscopy. Molecular modeling
additional information
similarly to azurocidin or CatG, PR3 can also act via the non-catalytic mechanism
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Homo sapiens (P24158), Homo sapiens, Mus musculus (Q61096), Mus musculus
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.
279
27688-27698
2004
Homo sapiens (P24158), Homo sapiens, Mus musculus (Q61096), Mus musculus
brenda
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.
280
30242-30253
2005
Homo sapiens (P24158)
brenda
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.
174
6381-6390
2005
Homo sapiens (P24158), Homo sapiens, 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
1248-1260
2006
Homo sapiens (P24158), Homo sapiens
brenda
Schreiber, A.; Luft, F.C.; Kettritz, R.
Membrane proteinase 3 expression and ANCA-induced neutrophil activation
Kidney Int.
65
2172-2183
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
75-84
2004
Homo sapiens (P24158), Homo sapiens
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
3316-3321
2006
Homo sapiens (P24158), Homo sapiens
brenda
Korkmaz, B.; Moreau, T.; Gauthier, F.
Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions
Biochimie
90
227-242
2008
Homo sapiens (P24158), Homo sapiens
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.
1109
84-92
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
4086-4095
2007
Homo sapiens
brenda
Jenne, D.E.; Kuhl, A.
Production and applications of recombinant proteinase 3, Wegeners autoantigen: problems and perspectives
Clin. Nephrol.
66
153-159
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
101-112
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
1989-1997
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
29998-30004
2007
Homo sapiens
brenda
Fridlich, R.; David, A.; Aviram, I.
Membrane proteinase 3 and its interactions within microdomains of neutrophil membranes
J. Cell. Biochem.
99
117-125
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
458-464
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 (P24158), Homo sapiens
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
336-343
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
1211-1214
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
196-201
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
1548-1557
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
19896-19902
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
7906-7915
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, Macaca mulatta, Hylobates pileatus, 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.
3
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
11783-11792
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
3182-3196
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 (Q61096), Mus musculus
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 (P24158), Homo sapiens
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 (P24158), Homo sapiens
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 (P24158), Homo sapiens
brenda
Grzywa, R.; Lesner, A.; Korkmaz, B.; Sienczyk, M.
Proteinase 3 phosphonic inhibitors
Biochimie
166
142-149
2019
Homo sapiens (P24158)
brenda
Popow-Stellmaszyk, J.; Bajorowicz, B.; Malankowska, A.; Wysocka, M.; Klimczuk, T.; Zaleska-Medynska, A.; Lesner, A.
Design, synthesis, and enzymatic evaluation of novel ZnO quantum Dot-based assay for detection of proteinase 3 activity
Bioconjug. Chem.
29
1576-1583
2018
Homo sapiens (P24158)
brenda
Hwang, T.; Wang, W.; Wang, T.; Yu, H.; Hsieh, P.
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 (P24158), Homo sapiens
brenda
Fu, Z.; Thorpe, M.; Akula, S.; Chahal, G.; Hellman, L.T.
Extended cleavage specificity of human neutrophil elastase, human proteinase 3, and their distant ortholog clawed frog PR3 - three elastases with similar primary but different extended specificities and stability
Front. Immunol.
9
2387
2018
Homo sapiens (P24158), Homo sapiens, Xenopus laevis
brenda
Chen, Y.; Liu, Z.; Pan, T.; Chen, E.; Mao, E.; Chen, Y.; Tan, R.; Wang, X.; Tian, R.; Liu, J.; Qu, H.
JMJD3 is involved in neutrophil membrane proteinase 3 overexpression during the hyperinflammatory response in early sepsis
Int. Immunopharmacol.
59
40-46
2018
Homo sapiens (P24158), Homo sapiens
brenda
Martin, K.R.; Kantari-Mimoun, C.; Yin, M.; Pederzoli-Ribeil, M.; Angelot-Delettre, F.; Ceroi, A.; Grauffel, C.; Benhamou, M.; Reuter, N.; Saas, P.; Frachet, P.; Boulanger, C.M.; Witko-Sarsat, V.
Proteinase 3 is a phosphatidylserine-binding protein that affects the production and function of microvesicles
J. Biol. Chem.
291
10476-10489
2016
Homo sapiens (P24158), Homo sapiens
brenda
Yang, T.H.; St John, L.S.; Garber, H.R.; Kerros, C.; Ruisaard, K.E.; Clise-Dwyer, K.; Alatrash, G.; Ma, Q.; Molldrem, J.J.
Membrane-associated proteinase 3 on granulocytes and acute myeloid leukemia inhibits T cell proliferation
J. Immunol.
201
1389-1399
2018
Homo sapiens (P24158)
brenda
Guarino, C.; Gruba, N.; Grzywa, R.; Dyguda-Kazimierowicz, E.; Hamon, Y.; Legowska, M.; Skorenski, M.; Dallet-Choisy, S.; Marchand-Adam, S.; Kellenberger, C.; Jenne, D.E.; Sienczyk, M.; Lesner, A.; Gauthier, F.; Korkmaz, B.
Exploiting the S4-S5 specificity of human neutrophil proteinase 3 to improve the potency of peptidyl di(chlorophenyl)-phosphonate ester inhibitors a kinetic and molecular modeling analysis
J. Med. Chem.
61
1858-1870
2018
Homo sapiens (P24158), Homo sapiens
brenda
Mirea, A.M.; Toonen, E.J.M.; van den Munckhof, I.; Munsterman, I.D.; Tjwa, E.T.T.L.; Jaeger, M.; Oosting, M.; Schraa, K.; Rutten, J.H.W.; van der Graaf, M.; Riksen, N.P.; de Graaf, J.; Netea, M.G.; Tack, C.J.; Chavakis, T.; Joosten, L.A.B.
Increased proteinase 3 and neutrophil elastase plasma concentrations are associated with non-alcoholic fatty liver disease (NAFLD) and type 2 diabetes
Mol. Med.
25
16
2019
Homo sapiens (P24158), Homo sapiens
brenda