3.4.21.76: Myeloblastin
This is an abbreviated version!
For detailed information about Myeloblastin, go to the full flat file.
Word Map on EC 3.4.21.76
-
3.4.21.76
-
ancas
-
myeloperoxidase
-
elastase
-
antineutrophil
-
autoantibody
-
anca-associated
-
cathepsin
-
pr3-anca
-
polyangiitis
-
autoimmune
-
granule
-
glomerulonephritis
-
mpo-anca
-
vasculitides
-
remission
-
autoantigens
-
anti-pr3
-
perinuclear
-
polymorphonuclear
-
cyclophosphamide
-
azurophilic
-
gpa
-
crescent
-
anti-mpo
-
anca-positive
-
lactoferrin
-
pauci-immune
-
churg-strauss
-
granulomatous
-
elafin
-
vasculitic
-
anti-myeloperoxidase
-
rituximab
-
small-vessel
-
antibody-associated
-
azurocidin
-
anti-proteinase
-
neutrophil-derived
-
polyarteritis
-
antinuclear
-
mpo-anca-associated
-
ethanol-fixed
-
goodpasture
-
drug development
-
diagnostics
-
chapel
-
medicine
-
analysis
-
nsp4
-
aspartate-specific
-
necrotising
-
nodosa
-
anti-gbm
-
anti-glomerular
- 3.4.21.76
-
ancas
- myeloperoxidase
- elastase
-
antineutrophil
- autoantibody
-
anca-associated
- cathepsin
-
pr3-anca
- polyangiitis
- autoimmune
- granule
- glomerulonephritis
-
mpo-anca
- vasculitides
-
remission
- autoantigens
- anti-pr3
-
perinuclear
-
polymorphonuclear
- cyclophosphamide
-
azurophilic
- gpa
-
crescent
-
anti-mpo
-
anca-positive
- lactoferrin
-
pauci-immune
-
churg-strauss
-
granulomatous
- elafin
-
vasculitic
-
anti-myeloperoxidase
- rituximab
-
small-vessel
-
antibody-associated
-
azurocidin
-
anti-proteinase
-
neutrophil-derived
- polyarteritis
-
antinuclear
-
mpo-anca-associated
-
ethanol-fixed
-
goodpasture
- drug development
- diagnostics
-
chapel
- medicine
- analysis
- nsp4
-
aspartate-specific
-
necrotising
- nodosa
- anti-gbm
-
anti-glomerular
Reaction
Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-/- > -Val-/- =
Synonyms
AGP7, C-ANCA antigen, hPR-3, human leukocyte proteinase 3, human PR3, human proteinase 3, Leukocyte proteinase 3, Leukocyte proteinase 4, membrane proteinase 3, membrane-associated proteinase 3, mP3, mPR3, myeloblastin, neutrophil protease PR3, neutrophil proteinase 3, neutrophil serine protease, neutrophilic serine protease proteinase 3, P29, p29b, PMNL proteinase, Pr 3, PR-3, PR3, protease 3, proteinase 3, Proteinase PR-3, Proteinase-3, proteinase3, PRTN3, SAP3, secreted aspartic proteinase 3, surface proteinase 3, Wegener autoantigen, Wegener's autoantigen, Wegener's granulomatosis autoantigen, Xenopus PR3, xPR-3
ECTree
3.4.21.76 MyeloblastinAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.76 - Myeloblastin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)acetyl-Ala-Ala-Ala-Ala-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Ala-Pro-Leu-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Ala-Ala-Pro-Val-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Lys(2-picolinoyl)-Tyr-Asp-Ala-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Lys(2-picolinoyl)-Tyr-Asp-Ile-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Lys(2-picolinoyl)-Val-Glu-Ala-Lys-Gly-Asp-Dpa-NH2 + H2O
?
-
-
-
?
2-aminobenzoyl-APEEIM(o)DRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-APEEIMDRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-APEEIMMDRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-EAIPMSIPPEVKFNKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-EAIPMSIPQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-GIATFCM(o)LM(o)PEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-GIATFCMLMPEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Gln-Asp-Met-Ala-Val-Val-Gln-Ser-Val-Pro-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Gln-Pro-Met-Ala-Val-Val-Gln-Ser-Val-Pro-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-IVSARMAPEEIIMDRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-MMRCAQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-TFCM(o)LEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-TFCMLEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Tyr-Tyr-aminobutyl-(5-amino-2-nitrobenzoyl)-Gln-NH2 + H2O
?
-
-
-
?
2-aminobenzoyl-Tyr-Tyr-aminobutyl-(5-amino-2-nitrobenzoyl)-NH2 + H2O
?
-
-
-
?
2-aminobenzoyl-Tyr-Tyr-aminobutyl-Asn-Glu-Pro-Tyr(3-NO2)-NH2 + H2O
?
-
-
-
?
2-aminobenzoyl-VADCAQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-VAECCQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Val-Ala-Asp-Cys-Ala-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Val-Ala-Asp-Cys-Arg-Asp-Arg-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-Val-Ala-Asp-Nva-Ala-Asp-Tyr-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
?
2-aminobenzoyl-VSARQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
?
5-TAMRA-VADnVADYQ-DAP(CF) + H2O
?
a fluorescence resonance energy transfer, FRET, substrate. The reaction is inhibited by antibody MCPR3-7 binding
-
-
?
5-TAMRA-VADnVRDYQ-diaminopropionyl-fluorescein + H2O
?
fluorogenic substrate
-
-
?
Abz-APEEIMDDQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 2.5/mM/s
-
-
?
Abz-APEEIMDQQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 2/mM/s
-
-
?
Abz-APEEIMDRQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 14.6/mM/s
-
-
?
Abz-APEEIMDRY-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = lower than 1/mM/s
-
-
?
Abz-APEEIMDRYQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 3.2/mM/s
-
-
?
Abz-APEEIMDYQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 2.6/mM/s
-
-
?
Abz-APEEIMPRQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = lower than 1/mM/s
-
-
?
Abz-APEEIMRRQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = lower than 1/mM/s
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
Abz-Tyr-Tyr-Abu + 5-amino-2-nitrobenzamide
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ala-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Ala-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Arg-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Arg-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asn-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Asn-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Asp-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Asp-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gln-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Gln-NH2
-
is hydrolyzed by PR3 within 20 min, yielding (5-amino-2-nitrobenzoyl)-Gln-NH2 and Abz-Tyr-Tyr-Abu fragments with retention times of 10.4 and 12.3 min, respectively
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Glu-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Glu-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Gly-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Gly-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-His-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-His-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ile-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Ile-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Leu-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Leu-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Lys-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Lys-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Phe-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Phe-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Pro-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Pro-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Ser-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Ser-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Thr-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Thr-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Trp-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Trp-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Tyr-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Tyr-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-(5-amino-2-nitrobenzoyl)-Val-NH2 + H2O
Abz-Tyr-Tyr-Abu + (5-amino-2-nitrobenzoyl)-Val-NH2
-
-
-
-
?
Abz-Tyr-Tyr-Abu-ANB-NH2 + H2O
?
a fluorescence resonance energy transfer, FRET, substrate. The reaction is inhibited by antibody MCPR3-7 binding
-
-
?
Abz-VADCADRY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 651/mM/s
-
-
?
Abz-VADCADY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 630/mM/s
-
-
?
Abz-VADCAPY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = lower than 1/mM/s
-
-
?
Abz-VADCAQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 292/mM/s
-
-
?
Abz-VADCARY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 3.8/mM/s
-
-
?
Abz-VADCAY(NO2) + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 10.9/mM/s
-
-
?
Abz-Val-Ala-Asp-Nvl-Ala-Asp-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
acetyl-Glu(O-benzyl)-Lys(Ac)-Pro(4-O-benzyl)-Nva-7-amido-4-carbamoylmethylcoumarin + H2O
?
-
-
-
?
Ahx-PYFA-4-nitroanilide + H2O
?
the reaction is inhibited by antibody MCPR3-7 binding
-
-
?
annexin 1 + H2O
?
-
proteinase 3 is the main enzyme responsible for cleavage in the N terminus region of the protein
-
-
?
Boc-Ala-ONp + H2O
?
the reaction is not inhibited by antibody MCPR3-7 binding
-
-
?
Boc-Ala-Pro-nVal-SBzl + H2O
?
the reaction is not inhibited by antibody MCPR3-7 binding
-
-
?
Collagen type IV + H2O
Hydrolyzed collagen type IV
-
no or minimal activity against interstitial collagens type I and III
-
-
?
endothelial cell protein C receptor + H2O
?
-
PR3 produces multiple cleavages, with early products including 20 kDa N-terminal and C-terminal (after Lys176) fragments. High affinity interaction between PR3 and the endothelial cell protein C receptor (KD of 18.5102 nanomol)
-
-
?
For-Ala-Ala-Pro-Abu-SBzl + H2O
?
the reaction is partly inhibited by antibody MCPR3-7 binding
-
-
?
kininogen + H2O
?
-
PR3 incubated with kininogen, or a synthetic peptide derived from kininogen, induces breakdown and release of a novel tridecapeptide termed PR3-kinin, NH2-MKRPPGFSPFRSS-COOH, consisting of bradykinin with two additional amino acids on each terminus. The reaction is specific. PR3-kinin binds to and activates human kinin B1 receptors, but does not bind to B2 receptors, expressed by transfected HEK293 cells in vitro. PR3-kinin is processed to bradykinin and des-Arg-bradykinin by plasma kallikrein. PR3 proteolyzes kininogen in a dose-dependent and specific manner. PR3 in neutrophil extracts induces kininogen proteolysis and induces release of bradykinin-like peptides from kininogen
-
-
?
MeO-Suc-Ala-Ala-Pro-Val-4-nitroanilide + H2O
MeO-Suc-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
?
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-p-nitroanilide + H2O
?
pH 7.4, 150 mM NaCl
-
-
?
methoxysuccinyl-lysyl-(2-picolinoyl)-Ala-Pro-Val-thiobenzylester + H2O
?
pH 7.4, 150 mM NaCl, 3 mM 4,4-dithiodipyridine
-
-
?
N-Boc-3-[2-(2'-imidazolyl)benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
-
-
-
?
N-Boc-3-[2-(2'-methoxy-4'-dimethylaminophenyl)benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
-
-
-
?
N-Boc-3-[2-(2-quinolinyl)benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
-
-
-
?
N-Boc-3-[2-[2-(1'-methyl)pyrrolo]benzoxazol-5-yl]-Ala-Tyr-Tyr-Abu-(5-amino-2-nitrobenzamide) + H2O
?
-
is the most efficient PR3 substrate
-
-
?
Peptidyl thiobenzyl ester + H2O
?
-
the preferred P1 residue is a small hydrophobic amino acid such as aminobutyric acid, norvaline, valine or alanine, in decreasing order of preference
-
-
?
procaspase 3 + H2O
?
-
PR3 can cleave membrane-associated procaspase 3 into a 22 kDa fragment
-
-
?
protease-activated receptor-2
?
-
PR3 may possess the capacity to interact and activate protease-activated receptor-2 expressing antigen-presenting cells and thereby potentially link this proinflammatory activity to the initiation of an adaptive immune response (induction of PR3-specific T cells)
-
-
?
Tert-Butyloxycarbonyl-Ala-Ala-norvaline thiobenzyl ester + H2O
?
-
best substrate
-
-
?
tumour necrosis factor-alpha + H2O
?
-
PR-3-mediated cleavage of tumour necrosis factor-alpha in usual interstitial pneumonia, which may have implications for future therapeutic targeting of tumour necrosis factor-alpha converting enzyme (TACE)
-
-
?
Val-Ala-Asp-Val-Lys-Asp-Arg + H2O
?
-
simulations with a neutral Asp213 bound to the peptide reproduce the expected conformation of the catalytic triad: there are strong hydrogen bonds between histidine 57 and serine 195 and between histidine 57 and the aspartic acid 102. When Asp213 is ionized and in the presence of a peptide bound in the enzyme, its side chain moves away from Gly197 and toward Ser195. The resulting interaction between Asp213 and Ser195 is strong with the formation of a hydrogen bond that persists for over 90% of the simulation time. Interaction competes with the crucial Ser-His hydrogen of the catalytic triad altering the proteolytic function of the enzyme. The pKa for Asp213 is of 8.4 (with a fast empirical method or based on molecular dynamics simulations). In simulations with negatively charged form of Asp213 the interaction between the carbonyl of the P1 residue (oxyanion hole) of the substrate and Ser195 (NH) of PR3 has vanished and the favorable interactions between the enzyme and the substrate are disrupted. A strong hydrogen bond is formed between the imidazole ring of His57 and the P1 and P1' residues of the substrate (NH groups) lasting 83 and 55% of the simulation time, respectively. These hydrogen bonds compete with, or replace, the crucial ones between amino acids of the catalytic triad and in particular the Ser-His interaction
-
-
?
Abz-VADCADQ-ethylene diamine 2,4 dinitrophenyl + H2O
?
37°C, pH 7.4, 150 mM NaCl, kcat/KM = 614/mM/s
-
-
?
Abz-VADCRDRQ-EDDnp + H2O
Abz-VADCR + DRQ-EDDnp
best synthetic substrate
-
-
?
Boc-Ala-Pro-Nva-thiobenzylester + H2O
?
pH 7.5, serine-protease activity of PR3
-
-
?
Boc-Ala-Pro-Nva-thiobenzylester + H2O
?
pH 7.5, serine-protease activity of PR3
-
-
?
MeOSuc-AAPV-4-nitroanilide + H2O
MeOSuc-AAPV + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
MeOSuc-AAPV-4-nitroanilide + H2O
MeOSuc-AAPV + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
MeOSuc-AIPM-4-nitroanilide + H2O
MeOSuc-AIPM + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
MeOSuc-AIPM-4-nitroanilide + H2O
MeOSuc-AIPM + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
oxidized insulin B chain + H2O
?
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
oxidized insulin B chain + H2O
?
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
procaspase-3 + H2O
?
37°C
in vitro, purified PR3 cleaves procaspase-3 into an active 22 kDa fragment
-
?
procaspase-3 + H2O
?
-
in vitro, purified PR3 cleaves procaspase-3 into an active 22 kDa fragment
-
?
Suc-AAA-4-nitroanilide + H2O
Suc-AAA + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0, very low activity
-
-
?
Suc-AAA-4-nitroanilide + H2O
Suc-AAA + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
Suc-AAPL-4-nitroanilide + H2O
Suc-AAPL + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0, very low activity
-
-
?
Suc-AAPL-4-nitroanilide + H2O
Suc-AAPL + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
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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
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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
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surfactant protein D + H2O
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37°C, pH 7.4
a fragment of about 35000 Da
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additional information
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no significant hydrolysis of 2-aminobenzoyl-EAIPM(o)SIPPEVKFNKQN-(2,4dinitrophenyl)ethylenediamine and 2-aminobenzoyl-EAIPM(o)SIPQN-(2,4dinitrophenyl)ethylenediamine
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additional information
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PR3 induced cell proliferation is dependent on its serine proteinase activity
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additional information
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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
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additional information
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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
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potent proinflammatory potential, expressed by phagocytic cells of the immune system
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potent proinflammatory potential, expressed by phagocytic cells of the immune system
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no reaction with VGVAPGV and VAPGVGVAPGV
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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
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PR3 induces phenotypic and functional maturation of blood monocyte-derived iDCs
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substrate specificity for small hydrophobic residues at P1 position (Val, Cys, Ala, Met, Ser and Leu)
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substrate specificity for small hydrophobic residues at P1 position (Val, Cys, Ala, Met, Ser and Leu)
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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
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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
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the peptide sequence VADVKDR is highly specific for PR3
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PR3 is capable of hydrolyzing several extracellular matrix proteins including collagen, elastin, fibronectin and laminin
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analysis of S4-S5 specificity of human neutrophil proteinase 3
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analysis of S4-S5 specificity of human neutrophil proteinase 3
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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
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additional information
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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
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additional information
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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
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additional information
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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
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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
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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
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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
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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
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additional information
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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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