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Ac-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
chromogenic substrate
-
-
?
Ac-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
chromogenic substrate
-
-
?
Ac-PANKAAC + H2O
Ac-PANK + Ala-Ala-Cys
-
betaI and betaII tryptase
-
?
Ac-PRNKAAC + H2O
Ac-PRNK + Ala-Ala-Cys
-
betaI and betaII tryptase
-
?
Ac-PRNRAAC + H2O
Ac-PRNR + Ala-Ala-Cys
-
betaI and betaII tryptase
-
?
Ac-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
chromogenic substrate, best peptide substrate
-
-
?
Ac-PRTKAAC + H2O
Ac-PRTK + Ala-Ala-Cys
-
betaI and betaII tryptase
-
?
Ac-Ser-Ile-Gln-Ser-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 51.2%
-
?
Ala-Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
chromogenic substrate, high activity
-
-
?
Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
chromogenic substrate
-
-
?
alpha2-antiplasmin + H2O
?
-
substrate binding and interaction with the enzyme, overview
-
-
?
Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
chromogenic substrate
-
-
?
benzoyl-Arg 4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
-
-
-
?
Benzoyl-L-Lys-Gly-L-Arg 4-nitroanilide + H2O
Benzoyl-L-Lys-Gly-L-Arg + 4-nitroaniline
benzoyl-L-Phe-L-Val-L-Arg-4-nitroanilide + H2O
benzoyl-L-Phe-L-Val-L-Arg + 4-nitroaniline
-
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys 4-methoxy-2-naphthylamide + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Arg-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Ala-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Benzyloxycarbonyl-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarine
-
-
-
-
?
Benzyloxycarbonyl-Arg 4-nitroanilide + H2O
Benzyloxycarbonyl-Arg + 4-nitroaniline
-
-
-
?
Benzyloxycarbonyl-Glu-Phe-Arg 4-nitroanilide + H2O
Benzyloxycarbonyl-Glu-Phe-Arg + 4-nitroaniline
-
best substrate for lung enzyme
-
-
?
Benzyloxycarbonyl-Gly-Arg 4-trifluoromethylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Gly-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Benzyloxycarbonyl-Gly-Pro-Arg 4-nitroanilide + H2O
Benzyloxycarbonyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
-
?
Benzyloxycarbonyl-L-Ala-L-Arg-L-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-L-Ala-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Ala-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Ala-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Benzyloxycarbonyl-L-Ala-L-Lys-L-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-L-Ala-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Benzyloxycarbonyl-L-Ala-L-Lys-L-Lys 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-L-Ala-L-Lys-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Benzyloxycarbonyl-Lys-Arg 4-trifluoromethylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Lys-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Benzyloxycarbonyl-Lys-Arg-S-CH2(CH3)2 + H2O
Benzyloxycarbonyl-Lys-Arg + S-CH2(CH3)2
-
best substrate for skin enzyme
-
-
?
Boc-Phe-Ser-Arg-methyl-coumarin + H2O
?
-
synthetic substrate
-
?
bovine prothrombin + H2O
?
-
-
-
-
?
Bz-Arg-p-nitroanilide + H2O
?
-
-
-
?
complement component 3 + H2O
?
-
digestion
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
-
-
-
?
D-Ile-Pro-Arg-p-nitroanilide + H2O
?
-
-
-
?
D-Phe-Pip-Arg-p-nitroanilide + H2O
?
-
-
-
?
D-Phe-piperocolyl-L-Arg 4-nitroanilide + H2O
D-Phe-piperocolyl-L-Arg + 4-nitroaniline
-
-
-
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
D-Pro-Phe-Arg-p-nitroanilide + H2O
?
-
-
-
?
D-Val-Leu-Arg 4-methoxy-2-naphthylamide + H2O
?
-
-
-
-
?
D-Val-Leu-Arg-p-nitroanilide + H2O
?
-
-
-
?
fibrinogen + H2O
fibrin + ?
fibrinogen + H2O
fibrinogen fragments
Gelatinase + H2O
?
-
digestion of the 72000 MW form to a 62000 MW form
-
-
?
Glu-Gly-Arg-p-nitroanilide + H2O
?
-
-
-
?
Glu-Pro-Arg-p-nitroanilide + H2O
?
-
-
-
?
High-molecular mass kininogen + H2O
?
-
-
-
-
?
high-molecular-weight kininogen + H2O
?
-
-
-
-
?
histone 2B + H2O
?
-
-
-
-
?
histone 3 + H2O
?
-
-
-
-
?
human influenza virus HA + H2O
HA1 + HA2
-
-
-
?
Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
chromogenic substrate
-
-
?
kininogen + H2O
?
-
-
-
-
?
L-pyroGlu-Gly-Arg 4-nitroanilide + H2O
L-pyroGlu-Gly-Arg + 4-nitroaniline
-
-
-
-
?
LL-37 + H2O
LL-37 fragments
-
the platelet-derived chemokine CXCL4 protects LL-37 from cleavage by beta-tryptase
-
-
?
MeOCO-Nle-Gly-Arg-p-nitroanilide + H2O
?
-
-
-
?
N-(p-tosyl)-Gly-Pro-Arg-4-nitroanilide + H2O
N-(p-tosyl)-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
N-(p-tosyl)-Gly-Pro-Lys-4-nitroanilide + H2O
N-(p-tosyl)-Gly-Pro-Lys + 4-nitroaniline
-
-
-
?
N-Benzoyl-Arg ethyl ester + H2O
?
-
-
-
-
?
N-benzoyl-DL-Arg-4-nitroanilide + H2O
N-benzoyl-DL-Arg + 4-nitroaniline
-
-
-
?
N-benzoyl-DL-Arg-p-nitroanilide + H2O
N-benzoyl-DL-Arg + p-nitroaniline
-
measurements of tryptase activity in sputum of chronic obstructive pulmonary disease patiens
-
-
?
N-benzoyl-DL-arginine-4-nitroanilide + H2O
N-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
N-Carbobenzoxy-Arg-Arg 4-methylcoumarin 7-amide + H2O
N-Carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-carbobenzoxy-GPR-4-nitroanilide + H2O
?
-
-
-
?
N-Carbobenzoxy-Phe-Arg 4-methylcoumarin 7-amide + H2O
N-Carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
?
N-p-tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + p-nitroaniline
-
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
N-tert-Butyloxycarbonyl-Ile-Glu-Gly-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Ile-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
rapid hydrolysis by free enzyme, scarcely hydrolyzed by the enzyme associated with trypstatin
-
-
?
N-tert-Butyloxycarbonyl-Phe-Ser-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
N-tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
?
-
-
-
?
Nalpha-benzoyl-L-arginine-p-nitroanilide + H2O
?
-
-
-
?
neurotensin + H2O
?
-
-
-
-
?
Oxidized B-chain of insulin + H2O
?
-
cleavage at Arg8-Gly9-NH2, Arg8-Arg9- and Arg22-Gly23-bonds
-
-
?
plasminogen + H2O
plasmin + ?
Precursor of matrix metalloproteinase 1 + H2O
?
-
conversion of the 52000 MW precursor into a 41000 MW protein, generation of new N-termini, namely Gln80 and Val82
-
-
?
Precursor of matrix metalloproteinase 3 + H2O
?
-
conversion of the 57000 MW precursor to a 45000 MW polypeptide, N-terminal amino acid is Phe83
-
-
?
Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
chromogenic substrate, best peptide substrate
-
-
?
pro-interleukin-6 + H2O
interleukin-6 + ?
-
-
-
-
?
pro-matrix metalloprotease-3 + H2O
?
-
digestion
-
-
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
-
-
-
-
?
pro-matrix metalloproteinase-13 + H2O
matrix metalloproteinase-13 + ?
-
-
-
-
?
pro-matrix metalloproteinase-2 + H2O
matrix metalloproteinase-2 + ?
-
-
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
-
-
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
-
-
-
-
?
pro-nerve growth factor + H2O
mature nerve growth factor and smaller fragments
-
-
analyzed by MS/MS
-
?
pro-nuclear factor-kappa B + H2O
nuclear factor-kappa B + ?
-
-
-
-
?
Pro-Phe-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 3.9%
-
?
pro-proteinase-activated receptor 2 + H2O
proteinase-activated receptor 2 + ?
-
-
-
-
?
pro-tissue necrosis factor + H2O
tissue necrosis factor + ?
-
-
-
-
?
Pro-urokinase + H2O
?
-
digestion
-
-
?
protease activated receptor-2 + H2O
?
protease-activated receptor 2 + H2O
fibrin + ?
-
-
-
-
?
protease-activated receptor-2 + H2O
?
-
digestion
-
-
?
proteinase-activated receptor 2 + H2O
?
-
-
-
-
?
proteinase-activated receptor-2 + H2O
?
-
tryptase may contribute to cyclooxygenase-2 upregulation by epithelial proteinase-activated receptor-2 activation during early lip carcinogenesis
-
-
?
prothrombin + H2O
thrombin + ?
S-2288 + H2O
D-Ile-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 100%
-
?
t-butyloxycarbonyl-Gln-Arg-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 26.0%
-
?
t-butyloxycarbonyl-Gln-Gly-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 63.3%
-
?
t-butyloxycarbonyl-Glu(OBzl)-Ala-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 67.3%
-
?
t-butyloxycarbonyl-Glu(OBzl)-Gly-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 26.3%
-
?
t-butyloxycarbonyl-Glu-Lys-Lys-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 1.6%
-
?
t-butyloxycarbonyl-Gly-Lys-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 10.9%
-
?
t-butyloxycarbonyl-Ile-Glu-Gly-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 3.5%
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 5.9%
-
?
t-butyloxycarbonyl-Leu-Gly-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 30.0%
-
?
t-butyloxycarbonyl-Leu-Lys-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 14.4%
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-4-methyl-coumarin 7-amide + H2O
?
t-butyloxycarbonyl-Val-Pro-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 6.1%
-
?
tert-butyloxycarbonyl-Gly-Lys-Arg 4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
TGFbeta + H2O
activated TGFbeta + ?
Tos-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Tos-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Tosyl-Arg methyl ester + H2O
?
-
-
-
-
?
Tosyl-Gly-L-Pro-Arg 4-nitroanilide + H2O
Tosyl-Gly-L-Pro-Arg + 4-nitroaniline
-
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
tosyl-Gly-Pro-Arg + p-nitroaniline
-
-
-
?
Tosyl-Gly-Pro-Lys 4-nitroanilide + H2O
Tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
-
-
-
?
tosyl-glycine-L-proline-L-arginine-4-nitroanilide + H2O
tosyl-glycine-L-proline-L-arginine + 4-nitroaniline
-
-
-
-
?
tosyl-GPK-4-nitroanilide + H2O
?
-
-
-
?
tosyl-GPR-4-nitroanilide + H2O
?
-
-
-
?
Type IV collagen + H2O
?
-
-
-
-
?
urokinase plasminogen activator + H2O
?
-
-
-
-
?
Vasoactive intestinal peptide + H2O
?
-
-
-
-
?
Z-D-Arg-Gly-Arg-p-nitroanilide + H2O
?
-
-
-
?
[Arg8]vasopressin + H2O
?
-
-
-
-
?
additional information
?
-
Benzoyl-L-Lys-Gly-L-Arg 4-nitroanilide + H2O
Benzoyl-L-Lys-Gly-L-Arg + 4-nitroaniline
-
best of the substrates screened
-
-
?
Benzoyl-L-Lys-Gly-L-Arg 4-nitroanilide + H2O
Benzoyl-L-Lys-Gly-L-Arg + 4-nitroaniline
-
best of the substrates screened
-
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
-
-
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
digestion
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrinogen fragments
-
-
-
?
fibrinogen + H2O
fibrinogen fragments
-
-
-
?
fibrinogen + H2O
fibrinogen fragments
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
digestion
-
-
?
N-p-tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
?
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
?
-
synthetic peptide substrate, mutant enzyme, expressed in insect cells
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
-
synthetic peptide substrate
-
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
-
-
-
?
N-tert-Butyloxycarbonyl-Phe-Ser-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tert-Butyloxycarbonyl-Phe-Ser-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
protease activated receptor-2 + H2O
?
-
-
-
-
?
protease activated receptor-2 + H2O
?
-
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-4-methyl-coumarin 7-amide + H2O
?
-
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-4-methyl-coumarin 7-amide + H2O
?
-
synthetic substrate, relative activity 36.3%
-
?
TGFbeta + H2O
activated TGFbeta + ?
-
activation
-
-
?
TGFbeta + H2O
activated TGFbeta + ?
-
tryptase activates TGFbeta, a key remodelling factor in asthma, in human airway smooth muscle cells via direct proteolysis in a PAR2-independent manner, TGFbeta is produced as a latent complex and the main limiting step in TGFb bioavailability is its activation, overview
-
-
?
additional information
?
-
-
biological functions and true roles of tryptase has not yet been demonstrated
-
?
additional information
?
-
equine tryptase has alanine at residue 216, rather than glycine, which confers increased arginine substrate specificity in vitro and may restrict fibrinogenolysis in vivo
-
-
?
additional information
?
-
-
equine tryptase has alanine at residue 216, rather than glycine, which confers increased arginine substrate specificity in vitro and may restrict fibrinogenolysis in vivo
-
-
?
additional information
?
-
-
pituitary enzyme has a preference for cleaving COOH-terminal to arginine or lysine residues which are preceded by a proline residue 4 or 6 residues NH2-terminal to the site of cleavage
-
-
?
additional information
?
-
-
kininogenase activity
-
-
?
additional information
?
-
-
the enzyme inactivates fibrinogen and high-molecular weight kininogen and converts C3 to C3a
-
-
?
additional information
?
-
-
the enzyme inactivates fibrinogen and high-molecular weight kininogen and converts C3 to C3a
-
-
?
additional information
?
-
-
skin and lung enzymes have both extended substrate-binding sites and proline residues at P3 substantially decrease kcat/Km, both enzymes prefer the tripeptide 4-nitroanilides with a P2 Gly residue over Phe, both favour the substrate benzyloxycarbonyl-Lys-Gly-Arg 4-nitroanilide over similar substrates containing six other representive amino acid residues at P3
-
-
?
additional information
?
-
-
4 closely related isoenzymes, tryptase alpha, I tryptase, tryptase II/beta and III tryptase, preferentially cleaves peptide substrates carboxy-terminal to arginine and lysine residues, hydrolyses bronchodilatatory neuropeptides, vasoactive intestinal peptide and peptide histidine methionine in vitro, cleaves fibrinogen and fibronectin inactivating, and activating the zymogens of stromelysin-1 and urokinase-type plasminogen activator
-
?
additional information
?
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Ile-Phe-Lys-p-nitroanilide, N-acetyl-Ile-Glu-Ala-Arg-p-nitroanilide, N-benzoyl-Arg-p-nitroanilide, N-benzoyl-Ile-Glu-Gly-Arg-p-nitroanilide, N-benzoyl-Phe-Val-Arg-p-nitroanilide, or N-benzoyl-Pro-Phe-Arg-p-nitroanilide are no substrates
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little or no reaction with Suc-Ala-Ala-Pro-Phe-p-nitroanilide and MeO-Suc-Arg-Pro-Tyr-p-nitroanilide
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tryptases betaI and betaII have a strict preference for cleavage after the basic amino acids, lysine and arginine, with only a slight preference for lysine over arginine, prefernce for proline at P4, preference for arginine or lysine at P3 and P2, these enzymes are not controlled by blood plasma proteinase inhibitors and only cleave a few physiological substrates in vitro
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unlike beta-tryptases, alpha-tryptases apparently are proteolytically inactive
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tryptase may have kallikrein-like activity under physiological conditions, tryptase could be of importance in the generation of kinnins subsequent to mast cell activation
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potential biological activities of human enzyme: 1. fibrinogenolysis, prevents clotting at local sites of mast cell activation
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the preference of the skin tryptase for substrates with 2 terminal basic residues indicates that this enzyme could process prohormones and proproteins which contain this structural feature at the cleavage site
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2. augmentation of histamine-mediated contractility of airway smooth, increases airway hyperreactivity to histamine and allergens, 3. degradation of vasoactive intestinal peptide, decreases endogenous bronchodilatory activity in lung 4. activation of prostromelysin, facilitates activation of procollagenase and tissue remodeling, 5. degradation of fibronectin, tissue remodeling, 6. stimulation of fibroblast proliferation, enhances fibrogenesis or wound repair
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currently unknown whether tryptases perform redundant or unique functions in vivo
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tryptase activates PKB in inflammatory reaction in ECV304 cells, tryptase can activate phosphoinositol-3-kinase/protein kinase B pathway and enhance IL-8 expression
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beta-tryptase is involved in the pathogenesis of airway inflammation, the enzyme accounts for more than 25% or total protein in human mast cells, activated cells release the enzyme along with histamine and heparin proteoflycans, overview
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the enzyme is an inflammation mediator
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the enzyme is involved in allergic inflammation, mechanism, overview
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the lack of eosinophils in asthmatic airway smooth muscle bundles in contrast to the large number of mast cells is a key feature of asthma and is caused by beta-tryptase abrogating the eosinophil chemotactic activities of ASM cell-derived eosinophil chemoattractants such as eotaxin and RANTES, overview
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beta-tryptase is a tetramer that has enzymatic activity, but requires heparin binding to maintain functional and structural stability, alpha-tryptase has little, if any, enzymatic activity but is a stable tetramer in the absence of heparin, both forms are in a two-state equilibrium, which is influenced by the residues in the vicinity of the active site and by inhibitor/substrate binding, substrate binding structure, overview, Asp216 and Lys192 are the main determinants of tryptase activity
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the enzyme is a serine protease that is a major and selective component of the secretory granules of all human mast cells, active monomers of human beta-tryptase have expanded substrate specificities, overview
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the unique structure of the proteinase comprises four almost identical monomer subunits arranged in a square flat ring with its substrate pockets faced inside, forming a tetramer with a central pore that can be penetrated by a short peptide, the optimal length of the tryptase substrate is a pentasaccharide, substrate specificity and cleavage pattern, screening of a peptide library, overview
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beta-tryptase enhances release of vascular endothelial growth factor from human osteoarthritic chondrocytes
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the enzyme cleaves preferentially after Lys/Arg residues
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the enzyme is an inflammation mediator, mMCP-6 is a major storage component of connective tissue-type mast cells, and is not normally released into the environment
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the enzyme is involved in allergic inflammation, mechanism, overview
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mast cell secretion of the tryptase MCP-6 contributes to eosinophil recruitment to the site of Trichinella spiralis larval infection
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mast cell-derived tryptase-heparin complexes play important roles in mouse bovine serum albumin/interleukin-1beta-induced arthritis
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ferritin is not a substrate for tryptase
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the enzyme cleaves preferentially after Lys/Arg residues
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specificity overview: peptide 4-nitroanilides
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specificity overview: peptide 4-nitroanilides
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specificity overview: peptide 4-nitroanilides
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not: casein, hemoglobin, azocoll
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no activation of the precursor of matrix metalloproteinase 2
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enzyme plays a crucial role in the process of degranulation
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activity only toward substrates with Arg at the P1 position, only 0.3% and 0.1% activity with t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarin 7-amide and Arg-4-methylcoumarin 7-amide, Suc-Ala-Pro-Ala-4-methylcoumarin 7-amide and Suc-Leu-Leu-Val-Leu-4-methylcoumarin 7-amide are no substrates
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post-translational proteolytic cleavage of the precursors of the fusion glycoproteins of enveloped RNA viruses is indispensable for their fusion activity and infectivity, enzyme triggers infection by pneumotropic Sendai and influenza A viruses by processing
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