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Information on EC 3.4.21.59 - Tryptase
for references in articles please use BRENDA:EC3.4.21.59
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.59 Tryptase
IUBMB Comments
Occurs as a tetrameric molecule with high affinity for heparin, in mast cell granules. In peptidase family S1 (trypsin family). Not inhibited by α1-proteinase inhibitor or α2-macroglobulin
The enzyme appears in viruses and cellular organisms
- 3.4.21.59
- histamine
-
allergic
- chymase
- anaphylaxis
-
degranulation
-
eosinophil
- mastocytosis
- ige
- granule
- airway
- asthma
- marrow
- mucosal
-
anaphylactic
- nasal
- c-kit
-
basophil
- lavage
- par-2
- rhinitis
- bronchial
-
asthmatic
- urticaria
-
atopic
-
leukotriene
- toluidine
- sting
- hymenoptera
-
trypsin-like
- receptor-2
-
provocation
-
ige-mediated
-
prick
-
anti-ige
-
metachromatic
-
proteinase-activated
- mast-cell
-
antihistamine
-
sneezing
-
nonallergic
-
ige-dependent
- angioedema
- bronchospasm
- pruritus
- drug development
-
wheal
-
nonatopic
- ketotifen
- nafamostat
- cladribine
-
enzyme-histochemical
- medicine
Reaction Schemes
showPreferential cleavage: Arg-/-, Lys-/-, but with more restricted specificity than trypsin
Synonyms
tryptase, serum tryptase, mast cell tryptase, beta-tryptase, mmcp-6, rat mast cell protease ii, human mast cell tryptase, basal serum tryptase, mc tryptase, tpsab1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-tryptase
beta-tryptase
betaII-tryptase
delta-tryptase
gamma-tryptase
group 2 tryptase
Lung tryptase
-
-
-
-
Mast cell neutral proteinase
-
-
-
-
mast cell protease 11
Mast cell protease II
-
-
-
-
Mast cell proteinase II
-
-
-
-
mast cell specific tryptase
Mast cell tryptase
MC tryptase
Pituitary tryptase
-
-
-
-
Proteinase, mast cell neutral
-
-
-
-
Proteinase, mast cell serine, II
-
-
-
-
Proteinase, mast cell serine, tryptase
-
-
-
-
Rat mast cell protease II
-
-
-
-
Skin tryptase
-
-
-
-
TPSAB1
TPSB2
transmembrane tryptase
tryptase
tryptase beta-2
Tryptase M
-
-
-
-
Tryptase, skin
-
-
-
-
tryptase-beta
beta-tryptase
-
-
Mast cell tryptase
-
-
-
-
Mast cell tryptase
-
-
Mast cell tryptase
-
-
tryptase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: Arg-/-, Lys-/-, but with more restricted specificity than trypsin
preferential cleavage: Arg-, Lys-, but with more restricted specificity than trypsin
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
97501-93-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
Substrates: chromogenic substrate
Products: -
Products: -
?
Ac-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
Substrates: chromogenic substrate
Products: -
Products: -
?
Ac-PANKAAC + H2O
Ac-PANK + Ala-Ala-Cys
-
Substrates: betaI and betaII tryptase
Products: -
Products: -
?
Ac-PRNKAAC + H2O
Ac-PRNK + Ala-Ala-Cys
-
Substrates: betaI and betaII tryptase
Products: -
Products: -
?
Ac-PRNRAAC + H2O
Ac-PRNR + Ala-Ala-Cys
-
Substrates: betaI and betaII tryptase
Products: -
Products: -
?
Ac-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
Substrates: chromogenic substrate, best peptide substrate
Products: -
Products: -
?
Ac-PRTKAAC + H2O
Ac-PRTK + Ala-Ala-Cys
-
Substrates: betaI and betaII tryptase
Products: -
Products: -
?
Ac-Ser-Ile-Gln-Ser-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 51.2%
Products: -
Products: -
?
Ala-Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
Substrates: chromogenic substrate, high activity
Products: -
Products: -
?
Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
Substrates: chromogenic substrate
Products: -
Products: -
?
alpha2-antiplasmin + H2O
?
-
Substrates: substrate binding and interaction with the enzyme, overview
Products: -
Products: -
?
Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
Substrates: chromogenic substrate
Products: -
Products: -
?
benzoyl-Arg 4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
benzoyl-L-Phe-L-Val-L-Arg-4-nitroanilide + H2O
benzoyl-L-Phe-L-Val-L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Ala-Ala-Lys 4-methoxy-2-naphthylamide + H2O
?
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Ala-Arg-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Ala-Arg-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarine
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Arg 4-nitroanilide + H2O
Benzyloxycarbonyl-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Glu-Phe-Arg 4-nitroanilide + H2O
Benzyloxycarbonyl-Glu-Phe-Arg + 4-nitroaniline
-
Substrates: best substrate for lung enzyme
Products: -
Products: -
?
Benzyloxycarbonyl-Gly-Arg 4-trifluoromethylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Gly-Arg + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Gly-Pro-Arg 4-nitroanilide + H2O
Benzyloxycarbonyl-Gly-Pro-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-L-Ala-L-Arg-L-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-L-Ala-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-L-Ala-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Ala-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-L-Ala-L-Lys-L-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-L-Ala-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-L-Ala-L-Lys-L-Lys 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-L-Ala-L-Lys-L-Lys + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Lys-Arg 4-trifluoromethylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Lys-Arg + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Lys-Arg-S-CH2(CH3)2 + H2O
Benzyloxycarbonyl-Lys-Arg + S-CH2(CH3)2
-
Substrates: best substrate for skin enzyme
Products: -
Products: -
?
Boc-Phe-Ser-Arg-methyl-coumarin + H2O
?
-
Substrates: synthetic substrate
Products: -
Products: -
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
H-D-Ile-Pro-Arg + 4-nitroaniline
Substrates: substrate S-2288
Products: -
Products: -
?
D-Phe-piperocolyl-L-Arg 4-nitroanilide + H2O
D-Phe-piperocolyl-L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
fibrinogen + H2O
fibrinogen fragments
-
Substrates: -
Products: -
Products: -
?
Gelatinase + H2O
?
-
Substrates: digestion of the 72000 MW form to a 62000 MW form
Products: -
Products: -
?
Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
Substrates: chromogenic substrate
Products: -
Products: -
?
L-pyroGlu-Gly-Arg 4-nitroanilide + H2O
L-pyroGlu-Gly-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
LL-37 + H2O
LL-37 fragments
-
Substrates: the platelet-derived chemokine CXCL4 protects LL-37 from cleavage by beta-tryptase
Products: -
Products: -
?
N-(p-tosyl)-Gly-Pro-Arg-4-nitroanilide + H2O
N-(p-tosyl)-Gly-Pro-Arg + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
N-(p-tosyl)-Gly-Pro-Lys-4-nitroanilide + H2O
N-(p-tosyl)-Gly-Pro-Lys + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
N-benzoyl-DL-Arg-4-nitroanilide + H2O
N-benzoyl-DL-Arg + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
N-benzoyl-DL-Arg-p-nitroanilide + H2O
N-benzoyl-DL-Arg + p-nitroaniline
-
Substrates: measurements of tryptase activity in sputum of chronic obstructive pulmonary disease patiens
Products: -
Products: -
?
N-benzoyl-DL-arginine-4-nitroanilide + H2O
N-benzoyl-DL-arginine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-Gly-Pro-Arg-p-nitroanilide + H2O
?
-
Substrates: -
Products: -
Products: -
?
N-Carbobenzoxy-Arg-Arg 4-methylcoumarin 7-amide + H2O
N-Carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-Carbobenzoxy-Phe-Arg 4-methylcoumarin 7-amide + H2O
N-Carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-p-tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-tert-Butyloxycarbonyl-Ile-Glu-Gly-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Ile-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
Substrates: rapid hydrolysis by free enzyme, scarcely hydrolyzed by the enzyme associated with trypstatin
Products: -
Products: -
?
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
Oxidized B-chain of insulin + H2O
?
-
Substrates: cleavage at Arg8-Gly9-NH2, Arg8-Arg9- and Arg22-Gly23-bonds
Products: -
Products: -
?
Precursor of matrix metalloproteinase 1 + H2O
?
-
Substrates: conversion of the 52000 MW precursor into a 41000 MW protein, generation of new N-termini, namely Gln80 and Val82
Products: -
Products: -
?
Precursor of matrix metalloproteinase 3 + H2O
?
-
Substrates: conversion of the 57000 MW precursor to a 45000 MW polypeptide, N-terminal amino acid is Phe83
Products: -
Products: -
?
Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
Substrates: chromogenic substrate, best peptide substrate
Products: -
Products: -
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
-
Substrates: -
Products: -
Products: -
?
pro-matrix metalloproteinase-13 + H2O
matrix metalloproteinase-13 + ?
-
Substrates: -
Products: -
Products: -
?
pro-matrix metalloproteinase-2 + H2O
matrix metalloproteinase-2 + ?
-
Substrates: -
Products: -
Products: -
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
-
Substrates: -
Products: -
Products: -
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
-
Substrates: -
Products: -
Products: -
?
pro-nerve growth factor + H2O
mature nerve growth factor and smaller fragments
-
Substrates: -
Products: analyzed by MS/MS
Products: analyzed by MS/MS
?
pro-nuclear factor-kappa B + H2O
nuclear factor-kappa B + ?
-
Substrates: -
Products: -
Products: -
?
Pro-Phe-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 3.9%
Products: -
Products: -
?
pro-proteinase-activated receptor 2 + H2O
proteinase-activated receptor 2 + ?
-
Substrates: -
Products: -
Products: -
?
pro-tissue necrosis factor + H2O
tissue necrosis factor + ?
-
Substrates: -
Products: -
Products: -
?
protease-activated receptor 2 + H2O
fibrin + ?
-
Substrates: -
Products: -
Products: -
?
proteinase-activated receptor-2 + H2O
?
-
Substrates: tryptase may contribute to cyclooxygenase-2 upregulation by epithelial proteinase-activated receptor-2 activation during early lip carcinogenesis
Products: -
Products: -
?
S-2288 + H2O
D-Ile-L-Pro-L-Arg + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
t-butyloxycarbonyl-Gln-Ala-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 100%
Products: -
Products: -
?
t-butyloxycarbonyl-Gln-Arg-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 26.0%
Products: -
Products: -
?
t-butyloxycarbonyl-Gln-Gly-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 63.3%
Products: -
Products: -
?
t-butyloxycarbonyl-Glu(OBzl)-Ala-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 67.3%
Products: -
Products: -
?
t-butyloxycarbonyl-Glu(OBzl)-Gly-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 26.3%
Products: -
Products: -
?
t-butyloxycarbonyl-Glu-Lys-Lys-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 1.6%
Products: -
Products: -
?
t-butyloxycarbonyl-Gly-Lys-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 10.9%
Products: -
Products: -
?
t-butyloxycarbonyl-Ile-Glu-Gly-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 3.5%
Products: -
Products: -
?
t-butyloxycarbonyl-Leu-Arg-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 5.9%
Products: -
Products: -
?
t-butyloxycarbonyl-Leu-Gly-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 30.0%
Products: -
Products: -
?
t-butyloxycarbonyl-Leu-Lys-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 14.4%
Products: -
Products: -
?
t-butyloxycarbonyl-Val-Pro-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 6.1%
Products: -
Products: -
?
tert-butyloxycarbonyl-Gly-Lys-Arg 4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Tos-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Tos-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Tosyl-Gly-L-Pro-Arg 4-nitroanilide + H2O
Tosyl-Gly-L-Pro-Arg + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
tosyl-Gly-Pro-Arg + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Tosyl-Gly-Pro-Lys 4-nitroanilide + H2O
Tosyl-Gly-Pro-Lys + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
tosyl-glycine-L-proline-L-arginine-4-nitroanilide + H2O
tosyl-glycine-L-proline-L-arginine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Benzoyl-L-Lys-Gly-L-Arg 4-nitroanilide + H2O
Benzoyl-L-Lys-Gly-L-Arg + 4-nitroaniline
-
Substrates: best of the substrates screened
Products: -
Products: -
?
Benzoyl-L-Lys-Gly-L-Arg 4-nitroanilide + H2O
Benzoyl-L-Lys-Gly-L-Arg + 4-nitroaniline
-
Substrates: best of the substrates screened
Products: -
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-p-tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
?
-
Substrates: synthetic peptide substrate, mutant enzyme, expressed in insect cells
Products: -
Products: -
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
-
Substrates: -
Products: -
Products: -
?
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
-
Substrates: synthetic peptide substrate
Products: -
Products: -
?
N-tert-Butyloxycarbonyl-Phe-Ser-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-tert-Butyloxycarbonyl-Phe-Ser-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
N-tert-Butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
t-butyloxycarbonyl-Phe-Ser-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
t-butyloxycarbonyl-Phe-Ser-Arg-4-methyl-coumarin 7-amide + H2O
?
-
Substrates: synthetic substrate, relative activity 36.3%
Products: -
Products: -
?
TGFbeta + H2O
activated TGFbeta + ?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: biological functions and true roles of tryptase has not yet been demonstrated
Products: -
Products: -
?
additional information
?
-
Substrates: equine tryptase has alanine at residue 216, rather than glycine, which confers increased arginine substrate specificity in vitro and may restrict fibrinogenolysis in vivo
Products: -
Products: -
?
additional information
?
-
-
Substrates: equine tryptase has alanine at residue 216, rather than glycine, which confers increased arginine substrate specificity in vitro and may restrict fibrinogenolysis in vivo
Products: -
Products: -
?
additional information
?
-
-
Substrates: chicken cathepsin G-like enzyme in Gallus gallus is analyzed by phage display and with recombinant substrates. The results show that this enzyme is a highly specific tryptase with preference for two arginines and a lysine residue preceded by the aromatic amino acid tryptophane (WRRK). The high selectivity of this enzyme makes it possible to screen the chicken proteome for potential targets. The most interesting potential targets are PDGF-A, coagulation factor V, and low-density lipoprotein receptor like-8. Poor or no activity with GRRWSAPVL, PGGRRGVVL, and PGGWRAKVE
Products: -
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: little or no reaction with Suc-Ala-Ala-Pro-Phe-p-nitroanilide and MeO-Suc-Arg-Pro-Tyr-p-nitroanilide
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: unlike beta-tryptases, alpha-tryptases apparently are proteolytically inactive
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Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme inactivates fibrinogen and high-molecular weight kininogen and converts C3 to C3a
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme inactivates fibrinogen and high-molecular weight kininogen and converts C3 to C3a
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: currently unknown whether tryptases perform redundant or unique functions in vivo
Products: -
Products: -
?
additional information
?
-
-
Substrates: tryptase may have kallikrein-like activity under physiological conditions, tryptase could be of importance in the generation of kinnins subsequent to mast cell activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: potential biological activities of human enzyme: 1. fibrinogenolysis, prevents clotting at local sites of mast cell activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: tryptase activates PKB in inflammatory reaction in ECV304 cells, tryptase can activate phosphoinositol-3-kinase/protein kinase B pathway and enhance IL-8 expression
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is an inflammation mediator
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in allergic inflammation, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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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?
additional information
?
-
-
Substrates: 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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?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: beta-tryptase enhances release of vascular endothelial growth factor from human osteoarthritic chondrocytes
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?
additional information
?
-
-
Substrates: the enzyme cleaves preferentially after Lys/Arg residues
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?
additional information
?
-
Substrates: due to its tetrameric organization, tryptase has a relatively restricted substrate cleavage profile
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-
additional information
?
-
-
Substrates: cleavage specificity of Zebra mbuna granzyme A1, substrate binding analysis and cleavage specificity by phage display, generation of a consensus sequence from sequenced phage inserts, overview. Granzyme A1 shows a high preference for aromatic amino acids, such as Phe and Trp, in the P2 position just N-terminally of the cleavage site. Granzyme A1 is a tryptase with preference for arginine in the P1 position of substrates
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-
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in allergic inflammation, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: mast cell secretion of the tryptase MCP-6 contributes to eosinophil recruitment to the site of Trichinella spiralis larval infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: mast cell-derived tryptase-heparin complexes play important roles in mouse bovine serum albumin/interleukin-1beta-induced arthritis
Products: -
Products: -
?
additional information
?
-
-
Substrates: ferritin is not a substrate for tryptase
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme cleaves preferentially after Lys/Arg residues
Products: -
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?
additional information
?
-
-
Substrates: specificity overview: peptide 4-nitroanilides
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?
additional information
?
-
-
Substrates: specificity overview: peptide 4-nitroanilides
Products: -
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?
additional information
?
-
-
Substrates: specificity overview: peptide 4-nitroanilides
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?
additional information
?
-
-
Substrates: not: casein, hemoglobin, azocoll
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?
additional information
?
-
-
Substrates: no activation of the precursor of matrix metalloproteinase 2
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?
additional information
?
-
-
Substrates: enzyme plays a crucial role in the process of degranulation
Products: -
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?
additional information
?
-
-
Substrates: 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
Products: -
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?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
-
Substrates: -
Products: -
Products: -
?
pro-matrix metalloproteinase-13 + H2O
matrix metalloproteinase-13 + ?
-
Substrates: -
Products: -
Products: -
?
pro-matrix metalloproteinase-2 + H2O
matrix metalloproteinase-2 + ?
-
Substrates: -
Products: -
Products: -
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
-
Substrates: -
Products: -
Products: -
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
-
Substrates: -
Products: -
Products: -
?
pro-nerve growth factor + H2O
mature nerve growth factor and smaller fragments
-
Substrates: -
Products: analyzed by MS/MS
Products: analyzed by MS/MS
?
pro-nuclear factor-kappa B + H2O
nuclear factor-kappa B + ?
-
Substrates: -
Products: -
Products: -
?
pro-proteinase-activated receptor 2 + H2O
proteinase-activated receptor 2 + ?
-
Substrates: -
Products: -
Products: -
?
pro-tissue necrosis factor + H2O
tissue necrosis factor + ?
-
Substrates: -
Products: -
Products: -
?
protease-activated receptor 2 + H2O
fibrin + ?
-
Substrates: -
Products: -
Products: -
?
proteinase-activated receptor-2 + H2O
?
-
Substrates: tryptase may contribute to cyclooxygenase-2 upregulation by epithelial proteinase-activated receptor-2 activation during early lip carcinogenesis
Products: -
Products: -
?
TGFbeta + H2O
activated TGFbeta + ?
-
Substrates: 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
Products: -
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?
additional information
?
-
-
Substrates: biological functions and true roles of tryptase has not yet been demonstrated
Products: -
Products: -
?
additional information
?
-
-
Substrates: currently unknown whether tryptases perform redundant or unique functions in vivo
Products: -
Products: -
?
additional information
?
-
-
Substrates: tryptase may have kallikrein-like activity under physiological conditions, tryptase could be of importance in the generation of kinnins subsequent to mast cell activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: potential biological activities of human enzyme: 1. fibrinogenolysis, prevents clotting at local sites of mast cell activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: tryptase activates PKB in inflammatory reaction in ECV304 cells, tryptase can activate phosphoinositol-3-kinase/protein kinase B pathway and enhance IL-8 expression
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is an inflammation mediator
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in allergic inflammation, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: beta-tryptase enhances release of vascular endothelial growth factor from human osteoarthritic chondrocytes
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in allergic inflammation, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: mast cell secretion of the tryptase MCP-6 contributes to eosinophil recruitment to the site of Trichinella spiralis larval infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: mast cell-derived tryptase-heparin complexes play important roles in mouse bovine serum albumin/interleukin-1beta-induced arthritis
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a crucial role in the process of degranulation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CaCl2
-
tryptase free from trypstatin is activated by 10 mM CaCl2, but tryptase associated with trypstatin is not
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-1-acetyl-N-[4-[(aminoiminomethyl)amino]-1-(2-benzothiazolylcarbonyl)butyl]-2,5-dihydro-1H-pyrrole-2-carboxamide
-
-
(2S)-1-acetyl-N-[4-[(aminoiminomethyl)amino]-1-(2-benzothiazolylcarbonyl)butyl]-2-azetidinearboxamide
-
-
(2S)-1-acetyl-N-[4-[(aminoiminomethyl)amino]-1-(2-benzothiazolylcarbonyl)butyl]-2-pyrrolidinecarboxamide
-
-
(2S)-2-acetylamino-N-[4-[(aminoiminomethyl)amino]-1-(2-benzothiazolylcarbonyl)butyl]-4-methylpentanamide
-
-
1,1-dioxido-3-oxo-1,2-benzisothiazol-2(3H)-yl-methyl 4-[[(phenylmethoxy)carbonyl]amino]-benzoate
-
-
1,1-dioxido-3-oxo-1,2-benzisothiazol-2(3H)-yl-methyl 5-[[(phenylmethoxy)carbonyl]amino]-pentanoate
-
-
1,1-dioxido-3-oxo-1,2-benzisothiazol-2(3H)-yl-methyl N-[(phenylmethoxy)carbonyl]-beta-alanate
-
-
1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
1,2,5-zhiadiazolidin-3-one 1,1-dioxide-based heterocyclic sulfides are potent inhibitors
1-acetyl-N-[(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-pyrrolidin-3-ylpropyl]prolinamide
-
-
1-methylethyl [5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
2-methoxyethyl [5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
3-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-1,1-diethylurea
-
-
3-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-1,1-dimethylurea
-
-
4'-[[5-(phenylethynyl)furan-2-yl]carbonyl]spiro[1-benzofuran-3,1'-cyclohexane]-5-carboxamide
-
-
4'-[[5-(phenylethynyl)furan-2-yl]carbonyl]spiro[1-benzofuran-3,1'-cyclohexane]-5-carboximidamide
-
-
4-amino-N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]butanamide
-
-
5-amino-N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]pentanamide
-
-
6-amidino-2-naphthyl p-guanidinobenzoate dimethane sulfonate
-
nafamostat mesilate
6-amino-N-[(9S,12R,16R)-12-[(2S)-butan-2-yl]-16-(3-carbamimidamidopropyl)-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]hexanamide
-
-
6-amino-N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]hexanamide
-
-
7-amino-N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]heptanamide
-
-
acetyl [(1S)-5-amino-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
benzyl 4-[(3-[N2-[(benzyloxy)carbonyl]-L-lysyl]-1,2,4-oxadiazol-5-yl)methyl]piperazine-1-carboxylate
-
-
benzyl [(1S)-2-(1,3-benzothiazol-2-yl)-1-(1H-indol-2-ylmethyl)-2-oxoethyl]carbamate
-
-
benzyl [(1S)-2-(1,3-benzothiazol-2-yl)-2-oxo-1-(1H-pyrrolo[2,3-c]pyridin-2-ylmethyl)ethyl]carbamate
-
-
benzyl [(1S)-5-amino-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-([5-[4-(benzylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-([5-[4-(benzyloxy)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-([5-[4-([2-[3-(trifluoromethyl)phenyl]ethyl]carbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-([5-[4-([2-[4-(trifluoromethyl)phenyl]ethyl]carbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[4-[(2-thiophen-2-ylethyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[4-[(3,4-dimethylbenzyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[4-[(3-methylbutyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[4-[(3-phenylpropyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[4-[(4-phenylbutyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[4-[(naphthalen-1-ylmethyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[4-[(naphthalen-2-ylmethyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[[4-(3-phenylpropanoyl)piperazin-1-yl]methyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[[4-(3-phenylpropyl)piperazin-1-yl]methyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[[4-(4-phenylbutanoyl)piperazin-1-yl]methyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[(5-[[4-(4-phenylbutyl)piperazin-1-yl]methyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[[5-(4-methoxybenzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[[5-(4-[[(2E)-3-phenylprop-2-en-1-yl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[[5-(4-[[2-(3,4-dichlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate10n
-
-
benzyl [(1S)-5-amino-1-[[5-(4-[[2-(3,5-difluorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[[5-(4-[[2-(4-fluorophenoxy)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
benzyl [(1S)-5-amino-1-[[5-(4-[[4-(2-fluorobenzyl)piperazin-1-yl]carbonyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
benzyl [(1S,3E)-5-amino-1-(1,3-benzothiazol-2-ylcarbonyl)pent-3-en-1-yl]carbamate
-
-
benzyl((1S)-5-amino-1-[(5-(4-[(2,4-dichlorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl((1S)-5-amino-1-[(5-(4-[(3,4-dichlorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl((1S)-5-amino-1-[(5-(4-[(3,4-dimethoxybenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl((1S)-5-amino-1-[(5-(4-[(3-chlorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl((1S)-5-amino-1-[(5-(4-[(3-methoxybenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl((1S)-5-amino-1-[(5-(4-[(4-chlorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl((1S)-5-amino-1-[(5-(4-[(4-fluorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl((1S)-5-amino-1-[(5-(4-[(4-methoxybenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl((1S)-5-amino-1-[(5-benzyl-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl((benzyl ((1S)-5-amino-1-[(5-(4-[(3,4-dimethoxybenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate1S)-5-amino-1-[(5-(4-[(3-methoxybenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
benzyl[(1S)-5-amino-1-((5-[3-(2-phenylethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
benzyl[(1S)-5-amino-1-((5-[3-(3-phenylpropoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
benzyl[(1S)-5-amino-1-((5-[4-(2-phenylethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
benzyl[(1S)-5-amino-1-((5-[4-(3-phenylpropoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
benzyl[(1S)-5-amino-1-((5-[4-(benzyloxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
benzyl[(1S)-5-amino-1-((5-[4-(cyclohexylmethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
benzyl[(1S)-5-amino-1-((5-[4-(naphthalen-1-ylmethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
benzyl[(1S)-5-amino-1-((5-[4-(naphthalen-2-ylmethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
Calcium
-
5 mM is needed to cause an irreversible 50% loss of activity after 60 min at room temperature
ethyl [(1S)-5-amino-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
ethyl [(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
ethyl [5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
ethyl[(1S)-5-amino-1-((5-[4-(2-phenylethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
ferritin
-
ferritin can retard the cleavage of both native oxidized high-molecular-weight kininogen by tryptase, initial rates of cleavage are reduced 45-75% in the presence of ferritin
-
M58539
-
i.e. N-[3-[4-(aminomethyl)phenyl]propyl]-N'-[(1-chloronaphthalen-2-yl)sulfanyl]ethane-1,2-diamine, a highly selective inhibitor
methyl 4'-[3-([(6-chloronaphthalen-2-yl)sulfonyl][2-[(2-hydroxyethyl)(methyl)amino]-2-oxoethyl]amino)-2-oxopiperidin-1-yl]-3'-fluorobiphenyl-2-sulfinate
-
-
methyl [(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-pyrrolidin-3-ylpropyl]carbamate
-
-
methyl [5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
MOL 6131
-
developed against mast cell beta-tryptase and studied in ovalbumin-induced allergic airway inflammation
N-[(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-piperidin-4-ylpropyl]-3,4-difluorobenzamide
-
-
N-[(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-pyrrolidin-3-ylpropyl]-3,4-difluorobenzamide
-
-
N-[(1S)-3-azetidin-3-yl-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)propyl]-3,4-difluorobenzamide
-
-
N-[(1S)-5-amino-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]-3,4-difluorobenzamide
-
-
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-1,3-benzodioxole-5-carboxamide
-
-
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-3,4-difluorobenzamide
-
-
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-3,5-difluorobenzamide
-
-
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-3-fluorobenzamide
-
-
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-4-chlorobenzamide
-
-
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-4-fluorobenzamide
-
-
N-[(9S,12R,16R)-12-[(2S)-butan-2-yl]-16-(3-carbamimidamidopropyl)-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]acetamide
-
-
N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]acetamide
-
-
N-[2-(3-chlorophenyl)ethyl]-4-([3-[N2-(2,2-dimethylpropanoyl)-L-lysyl]-1,2,4-oxadiazol-5-yl]methyl)benzamide
-
-
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(1,2,3,4-tetrahydroisoquinolin-7-ylsulfanyl)ethane-1,2-diamine
-
-
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(1-benzothiophen-2-ylsulfanyl)ethane-1,2-diamine
-
-
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(1-benzothiophen-5-ylsulfanyl)ethane-1,2-diamine
-
-
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(2,3-dihydro-1H-inden-5-ylsulfanyl)ethane-1,2-diamine
-
-
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(naphthalen-2-ylsulfanyl)ethane-1,2-diamine
-
-
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-[(2-methyl-1,3-benzothiazol-6-yl)sulfanyl]ethane-1,2-diamine
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2,2,2-trifluoroacetamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2,2-dimethylpropanamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2,4-difluorobenzamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2,5-dimethylfuran-3-carboxamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2-fluorobenzamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2-methoxyacetamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2-methylpropanamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-3,4-difluorobenzamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-3-fluorobenzamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-4-chlorobenzamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-4-fluorobenzamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]cyclopentanecarboxamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]cyclopropanecarboxamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]furan-2-carboxamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]hexanamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]morpholine-4-carboxamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]piperidine-1-carboxamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]pyrrolidine-1-carboxamide
-
-
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]tetrahydrofuran-3-carboxamide
-
-
neutrophil myeloperoxidase
-
important component of the neutrophil response to microbial infection, high concentrations of heparin can prevent the inhibition of tryptase by MPO
-
p-Aminophenylmethanesulfonyl fluoride
-
lung enzyme is inhibited over 3times faster than the skin enzyme
prop-2-en-1-yl [(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-pyrrolidin-3-ylpropyl]carbamate
-
-
trans-4-(Guanidinomethyl)cyclohexanecarboxylic acid esters
-
most effective: trans-4-(guanidinomethyl)cyclohexanecarboxylic acid butylphenyl ester
[1'-(acetyloxy)-5'-(aminomethyl)-1',2'-dihydrospiro[cyclohexane-1,3'-indol]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
-
-
[5'-(aminomethyl)-1',2'-dihydrospiro[cyclohexane-1,3'-indol]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
-
-
[5'-(aminomethyl)-1'-[(methylsulfinyl)oxy]-1',2'-dihydrospiro[cyclohexane-1,3'-indol]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
-
-
[5'-(aminomethyl)-1'-[(phenylsulfinyl)oxy]-1',2'-dihydrospiro[cyclohexane-1,3'-indol]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl](5-benzylfuran-2-yl)methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-(2-phenylethyl)furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-(phenylethynyl)furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-(phenylsulfanyl)furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(2-chlorophenyl)ethynyl]furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(2-fluorophenyl)ethynyl]furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(2-methoxyphenyl)ethynyl]furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(2-methylphenyl)ethynyl]furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(4-hydroxyphenyl)ethynyl]furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(4-methylphenyl)ethynyl]furan-2-yl]methanone
-
-
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(4-tert-butylphenyl)ethynyl]furan-2-yl]methanone
-
-
[5-[(1E)-1-aminoprop-1-en-1-yl]spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-(phenylethynyl)furan-2-yl]methanone
-
-
[6'-(aminomethyl)-2',3'-dihydrospiro[cyclohexane-1,1'-inden]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
-
-
alpha1-antitrypsin
-
rat peritoneal mast cell enzyme, no inhibition of skin enzyme
-
APC-366
-
low molecular weight active site-directed competitive tryptase inhibitor
APC366
-
N-(1-hydroxy-2-naphthoyl)-L-arginyl-L-prolinamide, selective inhibitor of mast cell tryptase
Bovine pancreatic trypsin inhibitor
-
may play a physiological role in regulation of tryptase proteolytic activity
-
Bovine pancreatic trypsin inhibitor
-
the functional unit of bovine tryptase is formed of at least 4 binding sites for this inhibitor
-
polybrene
-
heparin antagonist, potent inhibitor, noncompetitive inhibition, recombinant tryptase
protamine
-
heparin antagonist, potent inhibitor, competitive inhibition, recombinant tryptase
Soybean trypsin inhibitor
-
inhibition of rat peritoneal mast cell enzyme, no inhibition of skin enzyme
-
additional information
-
alpha2-macroglobulin; not: alpha1-proteinase inhibitor
-
additional information
-
not affected by the protein inhibitors of serine proteinases normally present in human extracellular fluids
-
additional information
-
antileukoprotease; antithrombin III; hirudin; low-molecular weight elastase inhibitor from human lung; no specific physiologic inhibitor has yet been found for the protease
-
additional information
-
lima bean trypsin inhibitor; ovomucoid inhibitor; plasma (human)
-
additional information
-
unique tryptase inasmuch as it has no endogenous inhibitors
-
additional information
-
no inhibition of native or recombinant enzyme by soybean trypsin inhibitor SBTI
-
additional information
-
library screening and inhibitor design and synthesis, inhibition mechanism, overview
-
additional information
-
design of potent and selective enzyme inhibitors based on alpha-keto-[1,2,4]-oxadiazoles, overview
-
additional information
-
synthesis and inhibitory potency of spirocyclic piperidine amide derivatives as enzyme inhibitors, overview
-
additional information
-
CXCL4 does not act as a direct beta-tryptase inhibitor, but destabilizes active tetrameric enzyme by antagonizing the heparin component required for the integrity of the tetramer
-
additional information
aprotinin only inhibits monomeric beta-tryptase mutant
-
additional information
-
aprotinin only inhibits monomeric beta-tryptase mutant
-
additional information
due to its tetrameric organization, tryptase is resistant to all known physiological protease inhibitors
-
additional information
-
tryptase-small-interfering RNA vector inhibits tryptase expression in P815 cells, reduced tryptase expression significantly inhibits the synthesis and release of interleukin-6 and tissue necrosis factor-alpha in vascular endothelial cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dsDNA
heparin is necessary for stabilizing the tetrameric, active organization of tryptase, and the absence of stabilizing heparin is accompanied by a rapid loss of enzymatic activity. DNA can substitute for heparin in stabilizing the active tryptase in the nuclear environment, similar to heparin, DNA has a high negative charge density. DNA preserves the enzymatic activity of tryptase. DNA stabilizes tryptase activity at 37°C and pH 7.2. dsDNA fragments of sizes down to, at least, 400 base pairs had an equal stabilizing effect as that of intact dsDNA. DNA promotes histone degradation by tryptase
-
heparin
-
is required for stabilization of the enzyme tetramer as a prerequisite for catalytic activity, the enzyme activity is 70fold increased, pH-dependent complex formation and complex structure, overview
heparin
heparin both stabilizes the tetramer and allosterically conditions the active site
heparin
heparin is necessary for stabilizing the tetrameric, active organization of tryptase, and the absence of stabilizing heparin is accompanied by a rapid loss of enzymatic activity. The storage of tryptase within the granules is critically dependent on serglycin, i.e., proteoglycans having strongly negatively charged glycosaminoglycan side chains of heparin (or chondroitin sulfate) type attached to the serglycin core protein. DNA can substitute for heparin in stabilizing the active tryptase in the nuclear environment, similar to heparin, DNA has a high negative charge density. Neither heparin nor DNA has the capacity to reverse the loss of activity in the absence of either of the stabilizing factors
additional information
-
tryptase levels do not increase in patients undergoing elective defibrillation or electro convulsive therapy with the administration of suxamethonium
-
additional information
-
acute exposure of human skin to ultraviolet or infrared radiation or heat stimuli increases mast cell numbers and tryptase expression in human skin in vivo
-
additional information
heparin is more efficient than dsDNA in providing tryptase stabilization, but with increasing concentration, dsDNA attains an equal tryptase-stabilizing effect compared to heparin. Single-stranded DNA is not capable of preserving the enzymatic activity of tryptase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.062
D-Ile-Pro-Arg-4-nitroanilide
-
pH 8.0, 25°C, active enzyme tetramer, in presence of heparin and Na+
0.081
D-Ile-Pro-Arg-4-nitroanilide
-
pH 6.8, 25°C, active enzyme tetramer, in presence of heparin and Na+
0.21
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
-
pH 6.0, 25°C, 800 ng or 1000 ng polybrene
additional information
additional information
-
overview: Km values of peptide 4-nitroanilide substrates
-
additional information
additional information
-
overview: Km values of peptide 4-nitroanilide substrates
-
additional information
additional information
-
overview: kinetic constant for the hydrolysis of synthetic thioester substrates and 4-nitroanilide substrates by the lung and by the skin enzyme
-
additional information
additional information
-
kinetics and binding constants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
45.7
Benzyloxycarbonyl-Lys-Arg 4-trifluoromethylcoumarin 7-amide
-
skin and lung enzyme
97
D-Ile-Pro-Arg-4-nitroanilide
-
pH 6.8, 25°C, active enzyme tetramer, in presence of heparin and Na+
170
D-Ile-Pro-Arg-4-nitroanilide
-
pH 8.0, 25°C, active enzyme tetramer, in presence of heparin and Na+
additional information
additional information
-
overview: kinetic constant for the hydrolysis of synthetic thioester substrates and 4-nitroanilide substrates by the lung and by the skin enzyme
-
additional information
additional information
-
effect of NaCl on turnover number
-
additional information
additional information
-
of peptide 4-nitroanilide substrates
-
additional information
additional information
-
of peptide 4-nitroanilide substrates
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00017
(Arg-Trp-Lys-Gly)4(Lys)2Lys-NH2
-
22°C, pH not specified in the publication
0.000006
1-acetyl-N-[(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-pyrrolidin-3-ylpropyl]prolinamide
-
-
0.000005
1-methylethyl [5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.000005
2-methoxyethyl [5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.000018
3-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-1,1-diethylurea
-
-
0.0000096
3-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-1,1-dimethylurea
-
-
0.001
4-amino-N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]butanamide
-
-
0.000012
5-amino-N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]pentanamide
-
-
0.0000000953
6-amidino-2-naphthyl p-guanidinobenzoate dimethane sulfonate
-
pH 7.8, 37°C
0.000007
6-amino-N-[(9S,12R,16R)-12-[(2S)-butan-2-yl]-16-(3-carbamimidamidopropyl)-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]hexanamide
-
-
0.000016
6-amino-N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]hexanamide
-
-
0.000023
7-amino-N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]heptanamide
-
-
0.000003
acetyl [(1S)-5-amino-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
0.00047
benzyl 4-[(3-[N2-[(benzyloxy)carbonyl]-L-lysyl]-1,2,4-oxadiazol-5-yl)methyl]piperazine-1-carboxylate
-
-
0.012
benzyl [(1S)-2-(1,3-benzothiazol-2-yl)-1-(1H-indol-2-ylmethyl)-2-oxoethyl]carbamate
-
-
0.045
benzyl [(1S)-2-(1,3-benzothiazol-2-yl)-2-oxo-1-(1H-pyrrolo[2,3-c]pyridin-2-ylmethyl)ethyl]carbamate
-
-
0.0073
benzyl [(1S)-5-amino-1-(1,3-benzothiazol-2-ylcarbonyl)pentyl]carbamate
-
-
0.0000037
benzyl [(1S)-5-amino-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
0.000037
benzyl [(1S)-5-amino-1-([5-[4-(benzylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
0.000012
benzyl [(1S)-5-amino-1-([5-[4-(benzyloxy)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
0.0000082
benzyl [(1S)-5-amino-1-([5-[4-([2-[3-(trifluoromethyl)phenyl]ethyl]carbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
0.00022
benzyl [(1S)-5-amino-1-([5-[4-([2-[4-(trifluoromethyl)phenyl]ethyl]carbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
0.0000024
benzyl [(1S)-5-amino-1-[(5-[4-[(2-thiophen-2-ylethyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.000039
benzyl [(1S)-5-amino-1-[(5-[4-[(3,4-dimethylbenzyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.0000099
benzyl [(1S)-5-amino-1-[(5-[4-[(3-methylbutyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.000003 - 0.0000032
benzyl [(1S)-5-amino-1-[(5-[4-[(3-phenylpropyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
0.00006
benzyl [(1S)-5-amino-1-[(5-[4-[(4-phenylbutyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.000013
benzyl [(1S)-5-amino-1-[(5-[4-[(naphthalen-1-ylmethyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.000011
benzyl [(1S)-5-amino-1-[(5-[4-[(naphthalen-2-ylmethyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.00023
benzyl [(1S)-5-amino-1-[(5-[[4-(3-phenylpropanoyl)piperazin-1-yl]methyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.000011
benzyl [(1S)-5-amino-1-[(5-[[4-(3-phenylpropyl)piperazin-1-yl]methyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.000034
benzyl [(1S)-5-amino-1-[(5-[[4-(4-phenylbutanoyl)piperazin-1-yl]methyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.0000058
benzyl [(1S)-5-amino-1-[(5-[[4-(4-phenylbutyl)piperazin-1-yl]methyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.00077
benzyl [(1S)-5-amino-1-[[5-(4-methoxybenzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
0.0000036
benzyl [(1S)-5-amino-1-[[5-(4-[[(2E)-3-phenylprop-2-en-1-yl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
0.000016
benzyl [(1S)-5-amino-1-[[5-(4-[[2-(3,4-dichlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
0.0000035
benzyl [(1S)-5-amino-1-[[5-(4-[[2-(3,5-difluorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
0.0000018
benzyl [(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
0.0000029
benzyl [(1S)-5-amino-1-[[5-(4-[[2-(4-fluorophenoxy)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
0.00014
benzyl [(1S)-5-amino-1-[[5-(4-[[4-(2-fluorobenzyl)piperazin-1-yl]carbonyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
0.025
benzyl [(1S,3E)-5-amino-1-(1,3-benzothiazol-2-ylcarbonyl)pent-3-en-1-yl]carbamate
-
-
0.000096
benzyl((1S)-5-amino-1-[(5-(4-[(2,4-dichlorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
0.00001
benzyl((1S)-5-amino-1-[(5-(4-[(3,4-dichlorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
0.000024
benzyl((1S)-5-amino-1-[(5-(4-[(3,4-dimethoxybenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
0.000013
benzyl((1S)-5-amino-1-[(5-(4-[(3-chlorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
0.000041
benzyl((1S)-5-amino-1-[(5-(4-[(3-methoxybenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
0.000014
benzyl((1S)-5-amino-1-[(5-(4-[(4-chlorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
0.000016
benzyl((1S)-5-amino-1-[(5-(4-[(4-fluorobenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
0.000019
benzyl((1S)-5-amino-1-[(5-(4-[(4-methoxybenzyl)oxy]benzyl)-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
0.0027
benzyl((1S)-5-amino-1-[(5-benzyl-1,2,4-oxadiazol-3-yl)carbonyl]pentyl)carbamate
-
-
0.00036
benzyl[(1S)-5-amino-1-((5-[3-(2-phenylethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
0.00012
benzyl[(1S)-5-amino-1-((5-[3-(3-phenylpropoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
0.000012
benzyl[(1S)-5-amino-1-((5-[4-(2-phenylethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
0.000025
benzyl[(1S)-5-amino-1-((5-[4-(3-phenylpropoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
0.00018
benzyl[(1S)-5-amino-1-((5-[4-(benzyloxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
0.0011
benzyl[(1S)-5-amino-1-((5-[4-(cyclohexylmethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
0.000078
benzyl[(1S)-5-amino-1-((5-[4-(naphthalen-1-ylmethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
0.000027
benzyl[(1S)-5-amino-1-((5-[4-(naphthalen-2-ylmethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
0.04
c[-Pro-beta3hArg(3-H2N-CH2)-D-allo-Ile-vTyr-NH-CH2-CH(NHAc)-CO-]
-
pH not specified in the publication, temperature not specified in the publication
0.000007
c[-Pro-beta3hArg(3-H2N-CH2)-D-allo-Ile-vTyr-NH-CH2-CH(NHCO-(CH2)5-NH2)-CO-]
-
pH not specified in the publication, temperature not specified in the publication
0.000025
c[-Pro-beta3hPhe(3-H2N-CH2)-D-allo-Ile-vTyr-NH-CH2-CH(NHCO-(CH2)5-NH2)-CO-]
-
pH not specified in the publication, temperature not specified in the publication
0.38
c[-Pro-beta3Lys(3-H2N-CH2)-D-allo-Ile-vTyr-NH-CH2-CH(NHAc)-CO-]
-
pH not specified in the publication, temperature not specified in the publication
0.0000028
ethyl [(1S)-5-amino-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]carbamate
-
-
0.0000019
ethyl [(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]carbamate
-
-
0.0000047
ethyl [5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.0000054
ethyl[(1S)-5-amino-1-((5-[4-(2-phenylethoxy)benzyl]-1,2,4-oxadiazol-3-yl)carbonyl)pentyl]carbamate
-
-
0.05
MCoTI-II[K10V], MCoTI-II[K10V]-[I11P], MCoTI-II[PKI]-[AVP]
-
IC50 above 0.05 mM
-
0.000011
methyl 4'-[3-([(6-chloronaphthalen-2-yl)sulfonyl][2-[(2-hydroxyethyl)(methyl)amino]-2-oxoethyl]amino)-2-oxopiperidin-1-yl]-3'-fluorobiphenyl-2-sulfinate
-
-
0.00013
methyl [(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-pyrrolidin-3-ylpropyl]carbamate
-
-
0.000017
methyl [5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.00045
N-[(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-piperidin-4-ylpropyl]-3,4-difluorobenzamide
-
-
0.000021
N-[(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-pyrrolidin-3-ylpropyl]-3,4-difluorobenzamide
-
-
0.00059
N-[(1S)-3-azetidin-3-yl-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)propyl]-3,4-difluorobenzamide
-
-
0.000004
N-[(1S)-5-amino-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)pentyl]-3,4-difluorobenzamide
-
-
0.0000021
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-1,3-benzodioxole-5-carboxamide
-
-
0.0000017
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-3,4-difluorobenzamide
-
-
0.0000015
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-3,5-difluorobenzamide
-
-
0.0000017
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-3-fluorobenzamide
-
-
0.0000019
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-4-chlorobenzamide
-
-
0.0000018
N-[(1S)-5-amino-1-[[5-(4-[[2-(3-chlorophenyl)ethyl]carbamoyl]benzyl)-1,2,4-oxadiazol-3-yl]carbonyl]pentyl]-4-fluorobenzamide
-
-
0.04
N-[(9S,12R,16R)-12-[(2S)-butan-2-yl]-16-(3-carbamimidamidopropyl)-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]acetamide
-
-
0.38
N-[(9S,12R,16R)-16-(4-aminobutyl)-12-[(2S)-butan-2-yl]-9-(4-hydroxybenzyl)-2,6,11,14,18-pentaoxo-1,5,10,13,17-pentaazabicyclo[17.2.1]docos-7-en-3-yl]acetamide
-
-
0.000002
N-[2-(3-chlorophenyl)ethyl]-4-([3-[N2-(2,2-dimethylpropanoyl)-L-lysyl]-1,2,4-oxadiazol-5-yl]methyl)benzamide
-
-
0.00019
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(1,2,3,4-tetrahydroisoquinolin-7-ylsulfanyl)ethane-1,2-diamine
-
-
0.00013
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(1-benzothiophen-2-ylsulfanyl)ethane-1,2-diamine
-
-
0.00021
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(1-benzothiophen-5-ylsulfanyl)ethane-1,2-diamine
-
-
0.0002
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(2,3-dihydro-1H-inden-5-ylsulfanyl)ethane-1,2-diamine
-
-
0.000073
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(naphthalen-2-ylsulfanyl)ethane-1,2-diamine
-
-
0.00076
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-(phenylsulfanyl)ethane-1,2-diamine
-
-
0.00027
N-[3-[4-(aminomethyl)phenyl]propyl]-N'-[(2-methyl-1,3-benzothiazol-6-yl)sulfanyl]ethane-1,2-diamine
-
-
0.0000029
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2,2,2-trifluoroacetamide
-
-
0.0000038
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2,2-dimethylpropanamide
-
-
0.0000033
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2,4-difluorobenzamide
-
-
0.000046
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2,5-dimethylfuran-3-carboxamide
-
-
0.0000062
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2-fluorobenzamide
-
-
0.0000037
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2-methoxyacetamide
-
-
0.0000068
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-2-methylpropanamide
-
-
0.0000076
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-3,4-difluorobenzamide
-
-
0.0000058
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-3-fluorobenzamide
-
-
0.0000066
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-4-chlorobenzamide
-
-
0.0000025
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]-4-fluorobenzamide
-
-
0.0000065
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]cyclopentanecarboxamide
-
-
0.0000046
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]cyclopropanecarboxamide
-
-
0.0000023
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]furan-2-carboxamide
-
-
0.0000098
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]hexanamide
-
-
0.0000057
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]morpholine-4-carboxamide
-
-
0.0000092
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]piperidine-1-carboxamide
-
-
0.000032
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]pyrrolidine-1-carboxamide
-
-
0.000022
N-[5-amino-1-[(5-[4-[2-(3,4-dichlorophenyl)ethoxy]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]tetrahydrofuran-3-carboxamide
-
-
0.000025
prop-2-en-1-yl [(1S)-1-([5-[4-(2,3-dihydro-1H-inden-2-ylcarbamoyl)benzyl]-1,2,4-oxadiazol-3-yl]carbonyl)-3-pyrrolidin-3-ylpropyl]carbamate
-
-
0.000323
(Lys-Lys-Phe-Gly)4(Lys)2Lys-NH2
-
22°C, pH not specified in the publication
0.00063
(Lys-Lys-Phe-Gly)4(Lys)2Lys-NH2
-
22°C, pH not specified in the publication
0.000003
benzyl [(1S)-5-amino-1-[(5-[4-[(3-phenylpropyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
0.0000032
benzyl [(1S)-5-amino-1-[(5-[4-[(3-phenylpropyl)carbamoyl]benzyl]-1,2,4-oxadiazol-3-yl)carbonyl]pentyl]carbamate
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00078
4'-[[5-(phenylethynyl)furan-2-yl]carbonyl]spiro[1-benzofuran-3,1'-cyclohexane]-5-carboximidamide
Homo sapiens
-
pH 7.4, 37°C
0.000015
[1'-(acetyloxy)-5'-(aminomethyl)-1',2'-dihydrospiro[cyclohexane-1,3'-indol]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.000023
[5'-(aminomethyl)-1',2'-dihydrospiro[cyclohexane-1,3'-indol]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0000018
[5'-(aminomethyl)-1'-[(methylsulfinyl)oxy]-1',2'-dihydrospiro[cyclohexane-1,3'-indol]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0000057
[5'-(aminomethyl)-1'-[(phenylsulfinyl)oxy]-1',2'-dihydrospiro[cyclohexane-1,3'-indol]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.000028
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl](5-benzylfuran-2-yl)methanone
Homo sapiens
-
pH 7.4, 37°C
0.000082
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-(2-phenylethyl)furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0000045
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-(phenylethynyl)furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.00009
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-(phenylsulfanyl)furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0000052
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(2-chlorophenyl)ethynyl]furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0000043
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(2-fluorophenyl)ethynyl]furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.000013
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(2-methoxyphenyl)ethynyl]furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0000012
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(2-methylphenyl)ethynyl]furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0032
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(4-hydroxyphenyl)ethynyl]furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0000083
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(4-methylphenyl)ethynyl]furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0007
[5-(aminomethyl)spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-[(4-tert-butylphenyl)ethynyl]furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.000059
[5-[(1E)-1-aminoprop-1-en-1-yl]spiro[1-benzofuran-3,1'-cyclohexan]-4'-yl][5-(phenylethynyl)furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
0.0000031
[6'-(aminomethyl)-2',3'-dihydrospiro[cyclohexane-1,1'-inden]-4-yl][5-(phenylethynyl)furan-2-yl]methanone
Homo sapiens
-
pH 7.4, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000000055
-
substrate tosyl-Gly-Pro-Lys-4-nitroanilide, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
specific activity for hydrolysis of model substrates by HAST and rHTs, micromol of nitroanilide min-1/nmol subunit
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
29373, 29375, 29376, 29377, 29378, 29379, 29383, 29384, 29387, 29388, 29394, 29396, 29397, 29398, 29399, 29400, 29403, 29405, 29406, 29407, 29408, 29409, 650078, 664220, 667310, 667981, 668951, 670795, 683129, 683153, 683232, 683234, 683237, 683249, 683455, 683728, 683768, 683808, 695292, 697021, 697023, 697086, 697405, 697416, 697722, 698446, 700007, 700537, 701375, 701383, 707086, 707571, 708126, 708165, 708185, 708207, 708302, 708375, 708431
-
-
brenda
-
709351, 709454, 709533, 709767, 710170, 710207, 710653, 717090, 717164, 717380, 717677, 717843, 717896, 718068, 718426, 731592, 732170, 732491, 732599, 752908, 752910, 753506, 753767
-
-
brenda
human
649421, 650140, 650476, 650825, 651154, 651867, 651932, 652145, 652169, 652713, 652748, 652893, 652996, 653005, 653333, 653618, 653635, 653718
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
significantly more tryptase in peritumoral tissue than in normal breast tissue
brenda
-
tryptase is present in the nucleus of both viable and dying mast cell leukemia cells
brenda
-
secretory activity in mast cells is manifested in the excretion of individual granules into the extracellular matrix of the ovarian stroma. Of crucial importance is the detection of tryptase and CPA3 in the nuclei of both cytogenic stroma cells and mast cells, which is increased in pathological ovarian endometriomas cells
brenda
-
-
brenda
additional information
-
basophils preferentially express mast cell protease 11 among the mast cell tryptase family, basophils rather than mast cells are the major source of mast cell protease-11
brenda
-
-
brenda
-
cell line HMC-1 obtained from a patient with mast cell leukemia
brenda
-
mast cell tryptase activates peripheral blood eosinophils to release granule-associated enzymes
brenda
-
airway mast cells and mast cell-like cell line, HMC-1, delta-tryptase is primarily expressed by mast cells, in tissues such as colon, lung and heart as well as in HMC-1 cells
brenda
-
-
708725, 708790, 709351, 710207, 708126, 708431, 717896, 717164, 717380, 717677, 717843, 752908, 752910, 753506, 753767
brenda
-
in the ovaries without pathological changes, the mast cells are located mainly in the medulla, represented by the loose fibrous connective tissue with a large number of vessels, having a wide lumen. Isolated mast cells are detected under the ovarian surface epithelium in the albuginea. In the medulla, the mast cells are localized near the elements of the vascular bed, are rather large in size, and are located in close contact with the cells of the cytogenic stroma. Tryptase is localized preferentially to the secretory granules, and to a smaller extent to the cytoplasm. In a few MCs, their secretory granules are located predominantly in the peripheral layer of the cytoplasm, ensuring the excretion of tryptase into the extracellular matrix using the transgranulation mechanism. Mast cell secretory granules can be located near the karyolemma of the stromal cell nuclei
brenda
tryptase is a tetrameric serine protease located within the secretory granules of mast cells. In the secretory granules, tryptase is stored in complex with negatively charged heparin proteoglycans and it is known that heparin is essential for stabilizing the enzymatic activity of tryptase. DNA can substitute for heparin in stabilizing the active tryptase in the nuclear environment, similar to heparin, DNA has a high negative charge density
brenda
-
mMCP-6 is exclusively expressed in connective tissuetype mast cells, mMCP-7 occurs in early stage cultures of bone marrow-derived mast cells, MCP-11 expression is highest at early stages of mast cell development
brenda
-
mast cell protease-11 is highly expressed by primary basophils and to a much lesser extent, by some mast cells
brenda
additional information
-
tryptase is localized preferentially to the secretory granules in mast cells. Certain amounts of specific proteases are also detected in the mast cell cytoplasm, reflecting the ongoing stages of their biogenesis, as well as the gradual maturation of the secretory granules and the exchange of secretome components, including tryptase and CPA3. Enzyme localization study, histological identifcation, overview
brenda
additional information
-
mMCP-6, mMCP-7 can be detected in plasma as early as 20 min after mast cell degranulation
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
during the cell death process, tryptase relocalizes from granules into the cytosol and nucleus
brenda
-
alpha-tryptase is present at low levels in the circulation, even in the absence of mast cell degranulation
-
brenda
-
extracellular matrix that surrounds the degranulated mast cell, MCP-6
-
brenda
-
tryptase is present in the nucleus of both viable and dying mast cell leukemia cells, i.e. HMC-1 cells
brenda
mechanism by which tryptase can execute enzymatic functions within the nucleus, overview
brenda
-
during the cell death process, tryptase relocalizes from granules into the cytosol and nucleus
brenda
-
-
brenda
-
tryptase and cathepsin-G are colocalized in skin mast cell secretory granules
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
-
tryptase, chymase, and CPA3 are polyfunctional components of the secretome, which can be accumulated in large quantities in the composition of secretory granules in mast cells. Mast cells are key cells that are involved in both innate and adaptive immune processes, which are essential in physiological and pathological conditions, including allergies, tumor, cardiovascular, and autoimmune and respiratory diseases, and in the progression of fibrosis and many others
physiological function
additional information
out of the mast cell proteases, beta-tryptase is unique with respect to its tetrameric organization, where all of its active sites are facing a narrow, central pore. Due to this organization, tryptase is resistant to all known physiological protease inhibitors, and has a relatively restricted substrate cleavage profile. Mechanism by which tryptase can execute enzymatic functions within the nucleus, overview
evolution
-
phylogenetic analysis and tree, comparison of granzymes' genetic organization and substrate specificity from different vertebrates, overview. Evolutionary enzyme development analysis
evolution
-
the locus encoding the enzyme is present in birds, reptiles and amphibians but it has been lost in mammals
malfunction
-
tryptase deficiency results in defective proteolytic modification of core histones
malfunction
-
tryptase inhibition causes a complete blockade of such processing. HMC-1 cell death is associated with a major reduction of several epigenetic histone marks, including H3 lysine-4-mono-methylation (H3K4me1), H3K9me2, H3 serine-10-phosphorylation (H3S10p) and H2B lysine-16-acetylation (H2BK16ac). Tryptase inhibition reverses the effect of cell death on these epigenetic mark. Tryptase inhibition causes increased proliferation of the mast cell leukemia cells. Tryptase inhibition causes increased late apoptosis/necrosis over apoptosis in HMC-1 cells, and tryptase inhibition blocks (LLME-induced) H3 cleavage in HMC-1 cells. Both tryptase inhibitors Pefabloc SC and nafamostat cause a slight increase in the levels of the H3K4me1 and H3K9me2 marks also at baseline conditions, i.e., in the absence of cell death-inducing agent. Tryptase inhibition modulates epigenetic histone modification in HMC-1 cells
malfunction
-
an increased number of chymase- and tryptase-positive mast cells in endometriosis foci can contribute to the development of pain and hyperalgesia, due to a direct effect on nerve fibers. Secretory pathways of specific ovarian mast cell proteases in the development of endometriomas, pathological phenotype, detailed overview. The enzyme is involved in the development of endometriosis
malfunction
the absence of stabilizing heparin is accompanied by a rapid loss of enzymatic activity. When tryptase alone is incubated at room temperature in a neutral pH-buffer, it loses enzymatic activity in a time-dependent manner, with essentially a complete loss of activity seen after 6 h
physiological function
-
tryptase does not alter paracellular permeability in human airway cells over min or hours, and tryptase does not alter the structure of the cell tight junction
physiological function
-
tryptase-positive mast cells play a role in breast cancer angiogenesis
physiological function
-
tryptase promotes the invasion and migration of breast cancer cells along with activation of matrix metalloproteinase-2. Tryptase does not affect the proliferation of the cells. Tryptase promotes breast cancer migration and invasion
physiological function
-
tryptase increases the lipid accumulation in human monocyte THP-1-derived macrophages and promotes foam cell formation in vitro via suppressing LXRalpha activation
physiological function
-
tryptase plays an important role in the control of human colonic mucosal permeability, and enhanced tryptase activity is responsible for the increased permeability of rectal mucosa in irritable bowel syndrome patients
physiological function
-
can induce microvascular leakage via prostaglandins in a mast cell-independent manner and may contribute to the development of basophil-mediated inflammatory responses
physiological function
-
activates isolated adult cardiac fibroblasts (Mus musculus) via protease activated receptor-2 (PAR-2)
physiological function
-
angiogenic activity (shown in a chick embryo chorioallantoic membrane in vivo assay)
physiological function
-
up-regulates vascular endothelial growth factor production in acute myeloid leukemia bone marrow stromal cells via the proteinase-activated receptor-2, ERK1/2, and p38MAPK signaling pathways
physiological function
-
an essential mast cell-restricted mediator in chemically induced colitis, acts upstream of many of the factors implicated in inflammatory bowel disease
physiological function
-
tryptase can increase the expression of matrix metalloproteinase 9 by activation of proteinase-activated receptor 2 in corneal epithelial cells and compromise the epithelial barrier
physiological function
-
mast cell tryptase induces microglia activation via protease-activated receptor 2-mitogen-activated protein kinase-nuclear factor kappa B signaling pathway, which will contribute to the development of microglia-mediated inflammation in brain
physiological function
-
mast cell tryptase induces eosinophil recruitment in the pleural cavity of mice via proteinase-activated receptor 2
physiological function
-
mast cell-derived tryptase potentiates cancer-associated fibroblast-induced morphology changes of prostate epithelia indirectly via the tumour microenvironment
physiological function
-
tryptase interacts directly with endothelial cells to induce angiogenesis
physiological function
-
tryptase interacts directly with endothelial cells to induce angiogenesis. Tryptase affects angiogenesis in myocardial microvascular endothelial cells via angiopoietin-2/Tie-2
physiological function
-
the enzyme is involved in angiogenesis after its release from activated mast cell granules. The enzyme is released with histamine from human skin mast cells in acute and chronic in vivo responses to allergens. The enzyme is a potent activator of fibroblast migration and proliferation, and collagen synthesis, stimulating tissue repair in wound healing and fibrosis. The enzyme tryptase plays an important role in host defense, linking adaptive and innate immunity
physiological function
-
the enzyme is involved in the pathogenesis of various diseases, including cardio-vascular, respiratory, digestive, reproductive, and nervous system disorders, such as multiple sclerosis and autoimmune encephalomyelitis, as well as diseases of the musculoskeletal system, skin disorders, sepsis, sudden infant death syndrome, and others. The enzyme also participates in angiogenesis, fibrous and amorphous component degradation of the extracellular matrix of the connective tissue and growth factor release. The enzyme boosts wound healing and tumour deposition. The enzyme has the ability to stimulate cultivated vascular endothelial cells to form provascular tubules
physiological function
the enzyme is an important mediator of the allergic inflammatory responses in asthma
physiological function
-
two granzyme A/K homologues in Zebra mbuna have different specificities, one classical tryptase and one with chymase activity. Granzyme A1 shows a high preference for aromatic amino acids, such as Phe and Trp, in the P2 position just N-terminally of the cleavage site, similar to what has been seen for human granzyme K. In comparisons, granzyme A2, shows a high preference for tyrosine in the P1 position of substrates, thereby being a strict chymase. Granzyme A1 is a tryptase with preference for arginine in the P1 position of substrates, while granzyme A2 prefers small amino acids such as Gly and Ala in this position
physiological function
-
the highly specific tryptase from Gallus gallus shows preference for two arginines and a lysine residue preceded by the aromatic amino acid tryptophane (WRRK), high selectivity. The most interesting potential targets are PDGF-A, coagulation factor V and low-density lipoprotein receptor like-8
physiological function
-
mast cells are immune cells that store large amounts of mast cell-restricted proteases in their secretory granules, including tryptase, chymase and carboxypeptidase A3. Tryptase, in addition to its canonical location in secretory granules, can be found in the nuclear compartment where it can impact on core histones. Tryptase can execute core histone processing in human mast cell leukemia cells, and tryptase regulates the epigenetic modification of core histones in mast cell leukemia cells. Tryptase has a major role in executing H3 cleavage in the context of cell death in HMC-1 cells
physiological function
-
potential roles of MC tryptase and CPA3 in the development of ovarian endometriomas. An increased number of chymase- and tryptase-positive mast cells in endometriosis foci can contribute to the development of pain and hyperalgesia, due to a direct effect on nerve fibers
physiological function
the enzyme can degrade core histones H2A, H2B, H3, and H4 in the nucleus, promoted by DNA, which also stabilizes the enzyme in the nucleus. Tryptase alone has minimal capacity to degrade any of the core histones
physiological function
-
tryptase activates enteric glial cells (EGCs) followed by affecting neuronal properties possibly via the stimuli-associated mediators. Mast cell-derived tryptase causes neuronal elongation/sensitization leading to visceral hypersensitivity. EGCs (commercial preparation, from rat myenteric plexus from the jejunum) are activated by tryptase, and proliferate (by 1.8fold) with cytoplasmic expansion and process elongation. Intercellular connections of EGCs are more complexed. Tryptase induces mRNA expression (2.5fold) and protein expression of NGF. Netrin-1 (3fold) and GDNF (3fold) mRNA expressions are increased at 30 min. Increase in netrin-1 continues until 6 h, whereas the latter decreases by 3 h. The conditioned medium of EGC after tryptase stimulation expands neuronal cytoplasm (round or ramified shapes) and neurite outgrowth with elongation of cytoskeletal filaments in time-dependent and dose-dependent manners. These changes are similar to those after nerve growth factor (NGF) stimulation. Growth cone proteins of neurons are also increased by the conditioned medium. EGCs are activated by tryptase change neuronal morphology (process elongation and cytoplasm expansion) possibly via the stimuli-associated mediators
Show AA Sequence and Transmembrane Helices (842 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
132000
134000
150000
200000
31000
32000
33000
34000
35000
360000
additional information
-
MW of the complex of tryptase and trypstatin: 144000, rat, gel filtration, MW of trypstatin is 7600 on gel filtration
31000
-
x * 31000 + x * 33000, human, SDS-PAGE, the enzyme is apparently a noncovalently linked tetramer with two sets of dissimilar, although antigenically related polypeptides
33000
-
x * 31000 + x * 33000, human, SDS-PAGE, the enzyme is apparently a noncovalently linked tetramer with two sets of dissimilar, although antigenically related polypeptides
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
monomer
-
a homotetramer with the active sites facing into the central cavity of the four monomers, the monomers are active, when stabilized by heparin-proteoglycan, and have expanded substrate specificities, overview
oligomer
tetramer
additional information
tetramer
-
x * 31000 + x * 33000, human, SDS-PAGE, the enzyme is apparently a noncovalently linked tetramer with two sets of dissimilar, although antigenically related polypeptides
tetramer
-
a homotetramer with the active sites facing into the central cavity of the four monomers, the monomers are active, when stabilized by heparin-proteoglycan, and have expanded substrate specificities, overview
tetramer
-
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, probably due to a cryptic active site, 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, overview
tetramer
-
a homotetramer of four catalytically active subunits, unless stabilized by heparin or high salt, the active tetramer converts to an inactive state consisting of an inactive-destabilized tetramer that reversibly dissociates to inactive monomers upon dilution, overview
tetramer
active organization of tryptase. Out of the mast cell proteases, beta-tryptase is unique with respect to its tetrameric organization, where all of its active sites are facing a narrow, central pore. In addition to promoting the storage of tryptase, it is known that heparin also is necessary for the assembly of enzymatically active tryptase tetramers
additional information
-
enzyme domain structure an structure comparisons, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
-
the recombinant inactive enzyme is cleaved and activated by enterokinase (EK) and results in the removal of the His6-tag and a subsequent reduction in size
glycoprotein
-
some of the MW heterogeneity of the multiple forms results from N-linked glycosylation
glycoprotein
-
treatment of the enzyme with N-glycosidase decreases the subunit MW by 4000
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.2 A crystal structure of mature alpha1-tryptase, crytallized by vapor diffusion method, space group P2(1)2(1)2(1), with unit cell dimensions of a = 91.44 A, b = 110.69 A, c = 130.09 A
-
3A crystal structure in a complex with 4-amidinophenyl pyruvic acid, large crystals of the tetragonal space group P4(1) with cell axes a = b = 82.93 A
-
beta-tryptase by the hanging drop vapour diffusion, 2 mg/ml protein in 10 mM MES, pH 6.1, and 2 M NaCl mixed with 0.1 M NaOAc, pH 4.6, 0.2 M ammonium sulfate, and 30% PEG 1500, 2-5 days at room temperature, X-ray diffraction structure determination and analysis at 1.6-2.5 A resolution, molecular modeling
-
co-crystallization of free and of leupeptin-complexed alphaI-tryptase mutants, 12 mg/ml protein in 10 mM Mops, pH 6.8, 0.7 M NaCl and 0.2 mM leupeptin at room temperature, sitting drop vapor diffusion method, equilibration against reservoir buffer containing 28% PEG 1500, 2 weeks, X-ray diffraction structure determination and anaylsis at 1.6 A resolution, molecular replacement
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D216G
G215D
the mutation distorts the substrate binding site and limits peptidase activity
I99C*/Y75A/Y37bA
the monomeric mutant (where C* is cysteinylated Cys-99) cannot form a dimer or tetramer, yet it is active (2.9% of wild type activity) but only in the presence of heparin
K192Q
K192Q/D216G
additional information
D216G
-
site-directed mutagenesis, alphaI-tryptase mutant, crystal structure determination and analysis, the sole mutation of Asp216 to Gly produces a protease with catalytic and instability properties intermediate between those of alpha and beta-tryptases
K192Q
-
site-directed mutagenesis, alphaI-tryptase mutant, crystal structure determination and analysis, the single mutation of Lys192 to Gln had no effect on activity or enzyme stability
K192Q/D216G
-
site-directed mutagenesis, alphaI-tryptase mutant, crystal structure determination and analysis
additional information
-
verification of phage display sequences using a two-trx system. The phage display-derived consensus sequence and a number of variants of this sequence are added in between two adjacent trx proteins expressed in Escherichia coli and subjected to chicken cathepsin G
additional information
dysfunctional tryptase alleles are always coinherited with functional alleles
additional information
dysfunctional tryptase alleles are always coinherited with functional alleles
additional information
-
dysfunctional tryptase alleles are always coinherited with functional alleles
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 7.5
-
25°C, 2 h, relatively stable in this range, rapid loss of activity below and above
additional information
-
inactivation of active monomers at neutral pH without stabilization by heparin-proteoglycans
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
-
HST, half-life 1 min, rHtbeta 0.5 min, rHTbeta-E149T 1.0 min, rHTalpha-D216G 85 min, rHTalpha-K192Q-D216G 1.8 min
additional information
-
presence of 1 M NaCl improves thermal stability, heparin does not stabilize the enzyme against thermal denaturation
25
-
HST, half-life 24 min, rHtbeta 8.5 min, rHTbeta-E149T 7.5 min, rHTalpha-K192Q-D216G 35 min
30
-
HST, half-life 4.3 min, rHtbeta 1.7 min, rHTbeta-E149T 2.3 min, rHTalpha-D216G 385 min, rHTalpha-K192Q-D216G 14 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of protein to the tryptase-heparin mixture is needed to keep the enzyme stable
-
heparin glycosaminoglycan stabilizes, maximal stabilization at a weight ratio to tryptase equal to or greater than unity
-
heparin stabilizes
heparin stabilizes human and dog enzyme
heparin stabilizes the beta-tryptase structure mainly through salt bridge interaction
-
heparin stabilizes the enzyme, retains about 50% activity in a low-salt solution after 2 h incubation at 25°C
-
In low-salt buffer the enzyme is labile, at least 1.4 M KCl is needed to keep the enzyme stable if incubated at 37°C for 30 min
-
increasing the NaCl concentration from 0.01 M to 1.0 M increases stability of free tryptase, in the presence of stabilizing polysaccharides it decreases the stability of tryptase until dissociation of tryptase from each polysaccharide occurs, thereafter tryptase stability increases as does that of free tryptase
-
poly-D-glutamic acid stabilizes, prolongs t1/2 at 37°C 55fold: Dextran sulfate and heparin provide complete stabilization of tryptase activity for 120 min at 37°C
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for at least 6 months in buffer containing NaCl, rapid loss of activity without addition of NaCl
-
the storage of tryptase within the granules is critically dependent on serglycin, i.e., proteoglycans having strongly negatively charged glycosaminoglycan side chains of heparin (or chondroitin sulfate) type attached to the serglycin core protein
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression and purification of recombinant human enzyme in a baculovirus system
-
low MW and high MW isoforms, may represent different gene products or they may result from post-translational modification
-
recombinant enzyme
recombinant inactive N-terminally His6-tagged enzyme from HEK-293 cells by nickel affinity chromatography
-
with an associated protein (trypstatin) that inhibits the protease activity above pH 7.5 (enzyme from peritoneal mast cells)
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloned and expressed in the methylotrophic yeast Pichia pastoris as protryptase
-
expression of gamma-tryptase as either a soluble, single-chian enzyme with a C-terminal His tag or as a soluble pseudozymogen activated by enterokinase cleavage to form a two-chain protein with an N-terminal His tag. Both recombinant proteins are expressed at high levels in Pichia pastoris
-
expression pattern and sequence comparisons of isozymes, overview
gene mtc1, DNA and amino acid sequence determination and analysis, equine tryptase has alanine at residue 216, rather than glycine, which confers increased arginine substrate specificity in vitro and may restrict fibrinogenolysis in vivo
genetic localization
phylogenetic analysis, recombinant expression of the inactive N-terminally His6-tagged (followed by an EK site) enzyme in HEK-293 cells
-
tryptases alpha and beta/II cDNA cloned and expressed in baculovirus-infected high five TM insect cells
-
tryptases betaI and betaII heterolougously expressed in the yeast Pichia pastoris
-
version with Flag peptide and enterokinase-cleavage site expressed in Sf9 insect cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
elevated tryptase levels are found to cluster in patients with myeloid neoplasms, including chronic myeloid leukaemia, chronic myelomonocytic leukaemia, myelodysplastic syndromes, acute myeloid leukaemia, and mastocytosis
-
Hymenoptera venom immunotherapy is associated with a small, but continuous decrease of baseline serum mast cell tryptase concentration over time
-
increased tryptase is associated with higher tumor grade and more lymph node metastasis in breast cancer tissue
-
mast cell tryptase level is significantly lower in pregnant women with preeclampsia and healthy pregnant women than in healthy non-pregnant women
-
mast cells from IL1RL1-null mice exhibit a marked reduction in MCP-6 expression
-
mast cells lacking IL1RL1 exhibit defective fibroblast-driven tryptase accumulation
-
microphthalmia-associated transcription factor plays a role in regulating the transcription of tryptase gene in human mast cells
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morphometric analysis shows a significantly higher positivity for tryptase in the cords of liveborn fetuses than in those of stillborn fetuses
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serum tryptase levels are positively associated with beekeeping activities, Hymenoptera venom allergy, age, and male sex
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significantly higher concentrations of tryptase are found in peripheral blood of sarcoidosis patients than controls, patients with progressive disease show the highest tryptase concentrations in serum
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the transcriptional activity of tryptase gene is specifically higher in HMC-1 cells compared to the tryptase-negative cells
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tryptase (MCP-6 and MCP-7) expression and activity are increased during progression of skin tumors in mice
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tryptase levels are higher in individuals that are non-atopic, overweight, or have metabolic syndrome compared to individuals that are atopic, normal weight, or do not have the metabolic syndrome, however, these associations are attenuated after adjusting for age
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
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beta-tryptases are the major focus of drug development for therapeutic inhibition
medicine
medicine
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viruses utilizes the enzyme to trigger their infectivity and multiplication in lungs, an inhibitor may regulate the enzyme activity and viral infections in vivo
medicine
-
heparin antagonists potentially may be used in treatment of mast cell-mediated diseases, potent and selective inhibitor of tryptase will be an essential tool to determine the role of tryptase in inflammation and other processes, tryptase plays a role in asthma and other allergic and inflammatory skin diseases like psoriasis and atopic dermatitis
medicine
-
tryptase is a potent activator of pro-uPA, the zymogen form of a protease asociated with tumor metastasis and invasion, viable drug target to create therapeutically useful inhibitors
medicine
-
potent and selective inhibitor of tryptase will be an essential tool to determine the role of tryptase in inflammation and other processes, tryptase plays a role in asthma and other allergic and inflammatory skin diseases like psoriasis and atopic dermatitis
medicine
-
potent and selective inhibitor of tryptase will be an essential tool to determine the role of tryptase in inflammation and other processes, tryptase plays a role in asthma and other allergic and inflammatory skin diseases like psoriasis and atopic dermatitis
medicine
-
serum mast cell tryptase level is significantly increased in untreated patients with mastocytosis
medicine
-
the serum basal tryptase level can be the indirect link between systemic mastocytosis and Hymenoptera venom allergy
medicine
-
there is no correlation of serum tryptase level with either the severity of psoriasis or the severity of atopic dermatitis, serum total tryptase does not prove to be a useful tool in assessing severity of psoriasis or atopic dermatitis
medicine
-
the number of both tryptase- and cathepsin-G-positive mast cells is significantly higher in cutaneous mastocytosis as compared to normal skin
medicine
-
the concomitant presence of systemic reactions (especially anaphylaxis) after Hymenoptera stings and increased serum baseline tryptase levels strongly suggests that a bone marrow examination is indicated for the diagnosis of clonal mast cell disease
medicine
-
mast cell tryptase can be an indicator of type I hypersensitivity reaction and thus may serve as a surrogate marker of anaphylaxis
medicine
-
tryptase serum concentrations can discriminate between the allergic and histamine fish poisoning syndromes
medicine
-
tryptase is a diagnostic marker of myeloid neoplasms and a useful test in clinical haematology
medicine
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increased tryptase concentrations are a risk marker for the severity of reactions to Hymenoptera stings or venom immunotherapy
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Release 2026.1 (March 2026)
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