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Information on EC 3.4.21.59 - Tryptase and Organism(s) Homo sapiens and UniProt Accession P20231

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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
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P20231 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group 2 tryptase
-
Mast cell tryptase
-
tryptase beta-2
alpha 1-tryptase
-
-
alpha tryptase
-
alpha-tryptase
basal serum tryptase
-
-
beta tryptase I
-
-
beta tryptase II
-
-
beta-tryptase
betaI-tryptase
-
betaII-tryptase
-
-
delta-tryptase
gamma-tryptase
group 2 tryptase
P15157, Q15661
-
HAST
-
-
HMC-1 tryptase
-
-
HTbeta
-
-
human beta-tryptase
-
-
human betaII-tryptase
-
-
human lung tryptase
-
-
human mast cell tryptase
-
-
human mast cell tryptase beta I
-
-
human tryptase alpha
-
-
human tryptase beta
-
-
human tryptase beta/2
-
-
human tryptase-beta
-
-
Lung tryptase
-
-
-
-
Mast cell neutral proteinase
-
-
-
-
Mast cell protease II
-
-
-
-
Mast cell proteinase II
-
-
-
-
mast cell specific tryptase
-
-
Mast cell tryptase
mast cell tryptase beta
-
-
mast cell-derived tryptase
-
-
mast cell-specific protease
-
-
mast cell-specific tryptase
-
-
Pituitary tryptase
-
-
-
-
Proteinase, mast cell neutral
-
-
-
-
Proteinase, mast cell serine, II
-
-
-
-
Proteinase, mast cell serine, tryptase
-
-
-
-
Rat mast cell protease II
-
-
-
-
S-tryptase
-
commercial name UNICAP Tryptase
serine protease tryptase
-
-
serum baseline tryptase
-
-
serum mast cell tryptase
-
-
serum tryptase
-
-
Skin tryptase
-
-
-
-
TPSAB1
-
-
TPSB2
-
-
transmembrane tryptase
-
-
tryptase
tryptase alpha
-
-
tryptase alpha-1
P15157
isoform
tryptase beta
-
-
tryptase beta-1
isoform
Tryptase M
-
-
-
-
Tryptase, skin
-
-
-
-
tryptase-beta
-
-
tryptase-beta1
-
isoform
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
97501-93-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
chromogenic substrate
-
-
?
Ac-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
chromogenic substrate
-
-
?
Ac-PANKAAC + H2O
Ac-PANK + Ala-Ala-Cys
show the reaction diagram
-
betaI and betaII tryptase
-
?
Ac-PRNKAAC + H2O
Ac-PRNK + Ala-Ala-Cys
show the reaction diagram
-
betaI and betaII tryptase
-
?
Ac-PRNRAAC + H2O
Ac-PRNR + Ala-Ala-Cys
show the reaction diagram
-
betaI and betaII tryptase
-
?
Ac-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
chromogenic substrate, best peptide substrate
-
-
?
Ac-PRTKAAC + H2O
Ac-PRTK + Ala-Ala-Cys
show the reaction diagram
-
betaI and betaII tryptase
-
?
Ala-Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
chromogenic substrate, high activity
-
-
?
Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
chromogenic substrate
-
-
?
alpha2-antiplasmin + H2O
?
show the reaction diagram
-
substrate binding and interaction with the enzyme, overview
-
-
?
Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
chromogenic substrate
-
-
?
benzoyl-Arg 4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Benzoyl-L-Lys-Gly-L-Arg 4-nitroanilide + H2O
Benzoyl-L-Lys-Gly-L-Arg + 4-nitroaniline
show the reaction diagram
-
best of the substrates screened
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-4-nitroanilide + H2O
benzoyl-L-Phe-L-Val-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys 4-methoxy-2-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Arg 4-nitroanilide + H2O
Benzyloxycarbonyl-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
Benzyloxycarbonyl-Glu-Phe-Arg 4-nitroanilide + H2O
Benzyloxycarbonyl-Glu-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
best substrate for lung enzyme
-
-
?
Benzyloxycarbonyl-Gly-Arg 4-trifluoromethylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Gly-Arg + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Gly-Pro-Arg 4-nitroanilide + H2O
Benzyloxycarbonyl-Gly-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-L-Ala-L-Arg-L-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-L-Ala-L-Arg-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Ala-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Ala-L-Leu-L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-L-Ala-L-Lys-L-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-L-Ala-L-Lys-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-L-Ala-L-Lys-L-Lys 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-L-Ala-L-Lys-L-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Lys-Arg 4-trifluoromethylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Lys-Arg + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Lys-Arg-S-CH2(CH3)2 + H2O
Benzyloxycarbonyl-Lys-Arg + S-CH2(CH3)2
show the reaction diagram
-
best substrate for skin enzyme
-
-
?
Bz-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
complement component 3 + H2O
?
show the reaction diagram
-
digestion
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Ile-Pro-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
D-Phe-Pip-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Pro-Phe-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
D-Val-Leu-Arg 4-methoxy-2-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
D-Val-Leu-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen + H2O
fibrin + ?
show the reaction diagram
fibrinogen + H2O
fibrinogen fragments
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
Gelatinase + H2O
?
show the reaction diagram
-
digestion of the 72000 MW form to a 62000 MW form
-
-
?
Glu-Gly-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
Glu-Pro-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
High-molecular mass kininogen + H2O
?
show the reaction diagram
-
-
-
-
?
Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
chromogenic substrate
-
-
?
kininogen + H2O
?
show the reaction diagram
-
-
-
-
?
LL-37 + H2O
LL-37 fragments
show the reaction diagram
-
the platelet-derived chemokine CXCL4 protects LL-37 from cleavage by beta-tryptase
-
-
?
MeOCO-Nle-Gly-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
N-benzoyl-DL-Arg-4-nitroanilide + H2O
N-benzoyl-DL-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-benzoyl-DL-Arg-p-nitroanilide + H2O
N-benzoyl-DL-Arg + p-nitroaniline
show the reaction diagram
-
measurements of tryptase activity in sputum of chronic obstructive pulmonary disease patiens
-
-
?
N-benzoyl-DL-arginine-4-nitroanilide + H2O
N-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-Carbobenzoxy-Arg-Arg 4-methylcoumarin 7-amide + H2O
N-Carbobenzoxy-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-GPR-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
N-Carbobenzoxy-Phe-Arg 4-methylcoumarin 7-amide + H2O
N-Carbobenzoxy-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
?
show the reaction diagram
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
show the reaction diagram
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-L-arginine-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
plasminogen + H2O
plasmin + ?
show the reaction diagram
-
-
-
-
?
Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
chromogenic substrate, best peptide substrate
-
-
?
pro-matrix metalloprotease-3 + H2O
?
show the reaction diagram
-
digestion
-
-
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
show the reaction diagram
-
-
-
-
?
pro-matrix metalloproteinase-13 + H2O
matrix metalloproteinase-13 + ?
show the reaction diagram
-
-
-
-
?
pro-matrix metalloproteinase-2 + H2O
matrix metalloproteinase-2 + ?
show the reaction diagram
-
-
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
show the reaction diagram
-
-
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
show the reaction diagram
-
-
-
-
?
pro-nerve growth factor + H2O
mature nerve growth factor and smaller fragments
show the reaction diagram
-
-
analyzed by MS/MS
-
?
Pro-urokinase + H2O
?
show the reaction diagram
-
digestion
-
-
?
protease activated receptor-2 + H2O
?
show the reaction diagram
-
-
-
-
?
protease-activated receptor-2 + H2O
?
show the reaction diagram
-
digestion
-
-
?
proteinase-activated receptor 2 + H2O
?
show the reaction diagram
-
-
-
-
?
proteinase-activated receptor-2 + H2O
?
show the reaction diagram
-
tryptase may contribute to cyclooxygenase-2 upregulation by epithelial proteinase-activated receptor-2 activation during early lip carcinogenesis
-
-
?
prothrombin + H2O
thrombin + ?
show the reaction diagram
-
-
-
?
S-2288 + H2O
D-Ile-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
TGFbeta + H2O
activated TGFbeta + ?
show the reaction diagram
Tos-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Tos-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Tosyl-Arg methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Arg-p-nitroanilide + H2O
tosyl-Gly-Pro-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
Tosyl-Gly-Pro-Lys 4-nitroanilide + H2O
Tosyl-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
tosyl-glycine-L-proline-L-arginine-4-nitroanilide + H2O
tosyl-glycine-L-proline-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
tosyl-GPK-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
tosyl-GPR-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
-
-
-
-
?
urokinase plasminogen activator + H2O
?
show the reaction diagram
-
-
-
-
?
Vasoactive intestinal peptide + H2O
?
show the reaction diagram
-
-
-
-
?
Z-D-Arg-Gly-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
complement component 3 + H2O
?
show the reaction diagram
-
digestion
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen + H2O
fibrin + ?
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
kininogen + H2O
?
show the reaction diagram
-
-
-
-
?
plasminogen + H2O
plasmin + ?
show the reaction diagram
-
-
-
-
?
pro-matrix metalloprotease-3 + H2O
?
show the reaction diagram
-
digestion
-
-
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
show the reaction diagram
-
-
-
-
?
pro-matrix metalloproteinase-13 + H2O
matrix metalloproteinase-13 + ?
show the reaction diagram
-
-
-
-
?
pro-matrix metalloproteinase-2 + H2O
matrix metalloproteinase-2 + ?
show the reaction diagram
-
-
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
show the reaction diagram
-
-
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
show the reaction diagram
-
-
-
-
?
pro-nerve growth factor + H2O
mature nerve growth factor and smaller fragments
show the reaction diagram
-
-
analyzed by MS/MS
-
?
Pro-urokinase + H2O
?
show the reaction diagram
-
digestion
-
-
?
protease activated receptor-2 + H2O
?
show the reaction diagram
-
-
-
-
?
protease-activated receptor-2 + H2O
?
show the reaction diagram
-
digestion
-
-
?
proteinase-activated receptor 2 + H2O
?
show the reaction diagram
-
-
-
-
?
proteinase-activated receptor-2 + H2O
?
show the reaction diagram
-
tryptase may contribute to cyclooxygenase-2 upregulation by epithelial proteinase-activated receptor-2 activation during early lip carcinogenesis
-
-
?
TGFbeta + H2O
activated TGFbeta + ?
show the reaction diagram
-
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
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
-
-
-
-
?
urokinase plasminogen activator + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
(Arg-Trp-Lys-Gly)4(Lys)2Lys-NH2
-
noncompetitive
(Lys-Lys-Phe-Gly)4(Lys)2Lys-NH2
-
noncompetitive
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
1,2-benzisothiazol-3-one 1,1-dioxide
-
-
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
-
-
4-aminobenzamidine
-
-
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
-
-
acetyl-PRNK-chloromethylketone
-
-
alpha-turmerone
-
alpha1-antitrypsin
-
human and dog enzyme insensitive
-
antipain
-
-
antithrombin III
-
-
-
APC-1167
-
-
APC-366
APC366
Aprotinin
Arg-Trp-Lys-Gly-NH2
-
noncompetitive
BABIM
-
-
benzamidine
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-(1,3-benzothiazol-2-ylcarbonyl)pentyl]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
-
-
beta-turmerone
-
bisdemethoxycurcumin
-
BMS-262084
-
-
BPTI
-
CaCl2
-
-
Calcium
-
5 mM is needed to cause an irreversible 50% loss of activity after 60 min at room temperature
ck-MCoEeTI
-
-
-
CRA-2059
curcumin enol
-
curcumin glucuronide
-
curcumin sulfate
-
cyclocurcumin
-
cyclotheonamide E4
-
-
c[-Pro-beta3hArg(3-H2N-CH2)-D-allo-Ile-vTyr-NH-CH2-CH(NHAc)-CO-]
-
-
c[-Pro-beta3hArg(3-H2N-CH2)-D-allo-Ile-vTyr-NH-CH2-CH(NHCO-(CH2)5-NH2)-CO-]
-
-
c[-Pro-beta3hPhe(3-H2N-CH2)-D-allo-Ile-vTyr-NH-CH2-CH(NHCO-(CH2)5-NH2)-CO-]
-
-
c[-Pro-beta3Lys(3-H2N-CH2)-D-allo-Ile-vTyr-NH-CH2-CH(NHAc)-CO-]
-
-
D-Tyr-Glu-Phe-Lys-Arg-CH2Cl
-
-
Dansyl-L-glutamyl-glycyl-L-arginine chloromethyl ketone
-
-
demethoxycurcumin
-
dihydrocurcumin
-
diisopropyl fluorophosphate
-
-
diisopropylfluorophosphate
-
-
DTNB
-
-
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
-
-
FUT175
-
a selective tryptase inhibitor
gabexate mesilate
-
-
Glu-Gly-Arg chloromethyl ketone
-
hexahydrocurcumin
-
HgCl2
-
-
histamine
-
-
JNJ-27390467
-
-
LDTI
-
only naturally occuring inhibitor, leech-derived tryptase inhibitor
-
leech-derived tryptase inhibitor
-
nanomolar inhibitor
-
leupeptin
Lys-Lys-Phe-Gly-NH2
-
noncompetitive
M58539
-
i.e. N-[3-[4-(aminomethyl)phenyl]propyl]-N'-[(1-chloronaphthalen-2-yl)sulfanyl]ethane-1,2-diamine, a highly selective inhibitor
MCoEeTI
-
-
-
MCoEeTI[K10R]
-
-
-
MCoTI-I
-
-
-
MCoTI-II
-
-
-
MCoTI-II derived miniprotein
-
nanomolar inhibitor
-
MCoTI-II-DELTA[DG]
-
-
-
MCoTI-II-DELTA[GSDGV]
-
-
-
MCoTI-II-DELTA[SDGGV]
-
-
-
MCoTI-II-DELTA[SDGG]
-
-
-
MCoTI-II-DELTA[SDGG][K10R]
-
-
-
MCoTI-II[K10A]
-
-
-
MCoTI-II[K10F]
-
-
-
MCoTI-II[K10Q]
-
-
-
MCoTI-II[K10R]
-
-
-
MCoTI-II[K10V]
-
-
-
MCoTI-II[K10V]-[I11P]
-
-
-
MCoTI-II[PKI]-[AVP]
-
-
-
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-tosyl-L-Lys chloromethyl ketone
-
-
N-tosyl-L-Phe chloromethyl ketone
-
-
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'-(phenylsulfanyl)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
-
-
NaCl
-
reversible at 1 M
Nafamostat
-
complete inhibition at 0.1 mM
nafamostat mesilate
-
-
nafamostat mesylate
-
-
neutrophil myeloperoxidase
-
important component of the neutrophil response to microbial infection, high concentrations of heparin can prevent the inhibition of tryptase by MPO
-
octahydrocurcumin
-
p-Aminophenylmethanesulfonyl fluoride
-
lung enzyme is inhibited over 3times faster than the skin enzyme
p-chloromercuribenzoate
-
-
Pentamidine
-
nonselective inhibitor
polybrene
-
heparin antagonist, potent inhibitor, noncompetitive inhibition
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
-
-
protamine
-
heparin antagonist, potent inhibitor, competitive inhibition
rLDTI
-
recombinant leech-derived tryptase inhibitor
-
RWJ-56423
-
-
RWJ-58643
-
-
SBTII
-
-
Soybean trypsin inhibitor
-
not
-
tetrahydrocurcumin
-
Trypstatin
-
purification
-
Tryptase inhibitor
-
derived from the medical leech Hirudo medicinalis
-
ZnSO4
-
-
[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
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heparin
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
Ac-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
0.062
Ac-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
0.1105 - 0.1333
Ac-PANK-AAC
0.0089 - 0.0145
Ac-PRNK-AAC
0.0165 - 0.0186
Ac-PRNR-AAC
0.071
Ac-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
0.0147 - 0.0234
Ac-PRTK-AAC
0.04
Ala-Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
0.053
Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
0.1
Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
0.0409
Benzyloxycarbonyl-L-Ala-L-Arg-L-Arg 4-methylcoumarin 7-amide
-
-
0.323
benzyloxycarbonyl-L-Ala-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
-
-
0.0138
Benzyloxycarbonyl-L-Ala-L-Lys-L-Arg 4-methylcoumarin 7-amide
-
-
0.0148
Benzyloxycarbonyl-L-Ala-L-Lys-L-Lys 4-methylcoumarin 7-amide
-
-
0.3 - 5
Bz-Arg-p-nitroanilide
0.062 - 0.081
D-Ile-Pro-Arg-4-nitroanilide
0.4 - 8.2
D-Ile-Pro-Arg-p-nitroanilide
0.7 - 0.79
D-Phe-Pip-Arg-p-nitroanilide
1.64 - 13.5
D-Pro-Phe-Arg-p-nitroanilide
1.12 - 3.49
D-Val-Leu-Arg-p-nitroanilide
5.03 - 10.5
Glu-Gly-Arg-p-nitroanilide
0.37 - 0.64
Glu-Pro-Arg-p-nitroanilide
0.111
Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
0.58 - 1.16
MeOCO-Nle-Gly-Arg-p-nitroanilide
0.049 - 0.12
N-p-tosyl-Gly-Pro-Arg-p-nitroanilide
3.5 - 4.2
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
0.044
Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
0.32 - 1.6
S-2288
0.35 - 0.49
tosyl-Gly-Pro-Lys-p-nitroanilide
0.04 - 0.36
Z-D-Arg-Gly-Arg-p-nitroanilide
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
141
Ac-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
367
Ac-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
1.1 - 3.5
Ac-PANK-AAC
0.97 - 0.99
Ac-PRNK-AAC
3.8 - 21.8
Ac-PRNR-AAC
378
Ac-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
0.99 - 1.1
Ac-PRTK-AAC
187
Ala-Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
233
Ala-Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
159
Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
5.35 - 5.52
benzyloxycarbonyl-Arg 4-nitroanilide
104 - 107
Benzyloxycarbonyl-Gly-Arg 4-trifluoromethylcoumarin 7-amide
551 - 553
Benzyloxycarbonyl-Gly-Pro-Arg 4-nitroanilide
2040
Benzyloxycarbonyl-L-Ala-L-Arg-L-Arg 4-methylcoumarin 7-amide
-
-
1870
benzyloxycarbonyl-L-Ala-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
-
-
3290
Benzyloxycarbonyl-L-Ala-L-Lys-L-Arg 4-methylcoumarin 7-amide
-
-
1520
Benzyloxycarbonyl-L-Ala-L-Lys-L-Lys 4-methylcoumarin 7-amide
-
-
45.7
Benzyloxycarbonyl-Lys-Arg 4-trifluoromethylcoumarin 7-amide
-
skin and lung enzyme
0.03 - 8.9
Bz-Arg-p-nitroanilide
97 - 170
D-Ile-Pro-Arg-4-nitroanilide
3 - 40
D-Ile-Pro-Arg-p-nitroanilide
24.1 - 59.5
D-Phe-Pip-Arg-p-nitroanilide
2.8 - 5.3
D-Pro-Phe-Arg-p-nitroanilide
0.833 - 31
D-Val-Leu-Arg-p-nitroanilide
9 - 183
Glu-Gly-Arg-p-nitroanilide
1.5 - 56.9
Glu-Pro-Arg-p-nitroanilide
199
Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
15.2 - 2630
MeOCO-Nle-Gly-Arg-p-nitroanilide
1.9 - 21
N-p-tosyl-Gly-Pro-Arg-p-nitroanilide
490 - 540
N-p-tosyl-Gly-Pro-Lys-p-nitroanilide
435
Pro-Ile-Arg-Asn-Lys-5-amino-2-nitrobenzoylamide
-
-
5.8 - 87
S-2288
27.9 - 75.5
tosyl-Gly-Pro-Lys-p-nitroanilide
1.9 - 10.3
Z-D-Arg-Gly-Arg-p-nitroanilide
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4 - 180
S-2288
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00017
(Arg-Trp-Lys-Gly)4(Lys)2Lys-NH2
-
22°C, pH not specified in the publication
0.000323 - 0.00063
(Lys-Lys-Phe-Gly)4(Lys)2Lys-NH2
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
-
-
0.05697
4-aminobenzamidine
-
22°C, pH not specified in the publication
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
-
-
0.0092 - 0.0097
APC-1167
0.00053 - 0.25
APC-366
0.25 - 0.369
Aprotinin
0.3058
Arg-Trp-Lys-Gly-NH2
-
22°C, pH not specified in the publication
0.0025 - 0.0046
BABIM
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
-
-
0.00011
ck-MCoEeTI
-
-
-
0.00000062
CRA-2059
-
pH 8.0, 25°C, tryptase-beta
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
-
-
0.0000951
gabexate mesilate
-
pH 7.8, 37°C
0.4717
Lys-Lys-Phe-Gly-NH2
-
22°C, pH not specified in the publication
0.000005
M58539
-
-
0.000033
MCoEeTI
-
-
-
0.000028
MCoEeTI[K10R]
-
-
-
0.0016
MCoTI-I
-
-
-
0.0006
MCoTI-II, MCoTI-II-DELTA[DG]
-
-
-
0.002
MCoTI-II-DELTA[GSDGV]
-
Ki above 0.002 mM
-
0.003
MCoTI-II-DELTA[SDGGV]
-
Ki above 0.003 mM
-
0.000009
MCoTI-II-DELTA[SDGG]
-
-
-
0.00001
MCoTI-II-DELTA[SDGG][K10R]
-
-
-
0.05
MCoTI-II[K10A], MCoTI-II[K10F], MCoTI-II[K10Q]
-
IC50 above 0.05 mM
-
0.085
MCoTI-II[K10R]
-
-
-
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
-
-
0.0023 - 0.0028
Pentamidine
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
-
-
0.0000012
rLDT1
-
pH 7.6, 25°C
-
0.000001
RWJ-56423
-
pH 7.4, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.0000051
cyclotheonamide E4
Homo sapiens
-
-
0.0000036
JNJ-27390467
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1000
-
purified commercial preparation from lung
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
assay at
6 - 8.5
-
in complex with heparin
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
isoelectric focusing
5.7
-
lung mast cell lysate and lung tryptase, isoelectric focusing
5.8
-
skin mast cell lysate, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
beta-tryptase
Manually annotated by BRENDA team
-
significantly more tryptase in peritumoral tissue than in normal breast tissue
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
tryptase is not cleared by the kidneys into the urine
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
of degranulated mast cells
Manually annotated by BRENDA team
-
alpha-, beta-, and delta-tryptase
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TRYB2_HUMAN
275
0
30515
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
enzyme-antithrombin III complex, gel filtration
110000
-
human, gel filtration in presence of 0.3 M NaCl
120000
132000
-
human, gel filtration
134000
135000 - 144000
-
human
147000
enzyme in complex with murine B12 Fab, gel filtration
150000
16000 - 120000
-
gel filtration
200000
-
gel filtration
29000
-
x * 29000 + x * 33000, human, SDS-PAGE
29000 - 40000
-
immunoreaction
30000
-
4 * 30000, rHTalpha, mutant D216G, SDS-PAGE, recombinant rHTbeta
30000 - 37000
-
Western blotting with monoclonal antibody AA5
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
32000
-
x * 32000 + x * 35000, human cell line HMC-1, SDS-PAGE
33000
34000
35000
-
x * 32000 + x * 35000, human cell line HMC-1, SDS-PAGE
38000
-
x * 34000 + x * 38000, human, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
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
-
9-12 * 31000-38000, SDS-PAGE
tetramer
additional information
-
activity of different enzyme conformations, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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
-
3-A crystal structure of beta/II-tryptase
-
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
-
mutant I99C, vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D215G
-
site-directed mutagenesis, derivative of tryptase alpha and beta/II
D216G
E149T
-
active site variant of rHTbeta
G215D
the mutation distorts the substrate binding site and limits peptidase activity
I16G
the inactive mutant cannot tetramerize
I99C
the mutant shows 33% of wild type 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
I99C/Y75A/Y37bA
the dimeric mutant shows 2.1% of wild type activity
K192Q
K192Q/D216G
R3Q
-
site-directed mutagenesis, derivative of tryptase beta/II
S195A
the mutant is catalytically incompetent in its protease form
Y75C
the mutant shows 63% of wild type activity
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
inactivation of active monomers at neutral pH without stabilization by heparin-proteoglycans
683545
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of protein to the tryptase-heparin mixture is needed to keep the enzyme stable
-
calcium destabilizes
-
chondroitin monosulfate stabilizes, prolongs t1/2 at 37°C 20fold
-
chondroitin sulfate E stabilizes, prolongs t1/2 at 37°C 69fold
-
heparan sufate stabilizes, prolongs t1/2 at 37°C 20fold
-
heparin glycosaminoglycan fragments of MW greater than 5700 stabilizes
-
heparin glycosaminoglycan partially stabilizes the tryptase
-
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 active tetramer
-
heparin stabilizes the beta-tryptase structure mainly through salt bridge interaction
-
heparin-proteoglycan stabilizes the active enzyme monomers
-
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
-
kinetic characterization of spontaneous inactivation
-
mature alpha1-tryptase does not require heparin-binding for stability
-
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
-
stabilized by heparin proteoglycans
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
commercial preparation
-
expression and purification of recombinant human enzyme in a baculovirus system
-
HST and rHT
-
immunoaffinity purification with mouse monoclonal antibody, B2, G4, B2 and C11
-
low MW and high MW isoforms, may represent different gene products or they may result from post-translational modification
-
lung beta-tryptase, commercial preparation
-
multiple electrophoretic forms
-
multiple forms
-
native enzyme by gel filtration
-
Ni-NTA column chromatography and S200 gel filtration
recombinant alpha1-tryptase
-
recombinant alphaI-tryptase mutants from insect cells
-
recombinant enzyme
-
recombinant tryptases alpha and beta/II
-
recombinant tryptases betaI and betaII
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloned and expressed in the methylotrophic yeast Pichia pastoris as protryptase
-
commercial preparation
-
expressed in baculovirus-infected Trichoplusia ni insect cells
expressed in Pichia pastoris
-
expressed in Pichia pastoris yeast system pPICZa
-
expression of alphaI-tryptase mutants in insect cells
-
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
-
genetic localization
-
human mast cell tryptases are the products of a multigene family
-
lung beta-tryptase, commercial preparation
-
skin beta-tryptase, commercial preparation
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
elevated postmortem mast cell tryptase level indicate anaphylaxis
-
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
-
microphthalmia-associated transcription factor plays a role in regulating the transcription of tryptase gene in human mast cells
-
morphometric analysis shows a significantly higher positivity for tryptase in the cords of liveborn fetuses than in those of stillborn fetuses
-
serum tryptase levels are positively associated with beekeeping activities, Hymenoptera venom allergy, age, and male sex
-
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
-
the transcriptional activity of tryptase gene is specifically higher in HMC-1 cells compared to the tryptase-negative cells
-
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
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of active tetramer from inactive monomers, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
beta-tryptases are the major focus of drug development for therapeutic inhibition
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Harvima, I.T.; Schechter, N.M.; Harvima, R.J.; Frki, J.E.
Human skin tryptase: purification, partial characterization and comparison with human lung tryptase
Biochim. Biophys. Acta
957
71-80
1988
Homo sapiens
Manually annotated by BRENDA team
Tanaka, T.; McRae, B.J.; Cho, K.; Cook, R.; Fraki, J.E.; Johnson, D.A.; Powers, J.C.
Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin with peptide 4-nitroanilide and thioester substrates
J. Biol. Chem.
258
13552-13557
1983
Homo sapiens
Manually annotated by BRENDA team
Vanderslice, P.; Ballinger, S.M.; Tam, E.K.; Goldstein, S.M.; Craik, C.S.; Caughey, G.H.
Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family
Proc. Natl. Acad. Sci. USA
87
3811-3815
1990
Homo sapiens
Manually annotated by BRENDA team
Cromlish, J.A.; Seidah, N.G.; Marcinkiewicz, M.; Hamelin, J.; Jonson, D.A.; Chretien, M.
Human pituitary tryptase: molecular forms, NH2-terminal sequence, immunocytochemical localization, and specificity with prohormone and fluorogenic substrates
J. Biol. Chem.
262
1363-1373
1987
Homo sapiens
Manually annotated by BRENDA team
Schwartz, L.B.
Tryptase: a mast cell serine protease
Methods Enzymol.
244
88-100
1994
Bos taurus, Canis lupus familiaris, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Rest, R.F.
Human neutrophil and mast cell proteases implicated in inflammation
Methods Enzymol.
163
309-327
1988
Homo sapiens
Manually annotated by BRENDA team
Alter, S.C.; Metcalfe, D.D.; Bradford, T.R.; Schwartz, L.B.
Regulation of human mast cell tryptase. Effects of enzyme concentration, ionic strength and the structure and negative charge density of polysaccharides
Biochem. J.
248
821-827
1987
Homo sapiens
Manually annotated by BRENDA team
Schwartz, L.B.; Bradford, T.R.
Regulation of tryptase from human lung mast cells by heparin. Stabilization of the active tetramer
J. Biol. Chem.
261
7372-7379
1986
Homo sapiens
Manually annotated by BRENDA team
Alter, S.C.; Schwartz, L.B.
Effect of histamine and divalent cations on the activity and stability of tryptase from human mast cells
Biochim. Biophys. Acta
991
426-430
1989
Homo sapiens
Manually annotated by BRENDA team
Alter, S.C.; Kramps, J.A.; Janoff, A.; Schwartz, L.B.
Interactions of human mast cell tryptase with biological protease inhibitors
Arch. Biochem. Biophys.
276
26-31
1990
Homo sapiens
Manually annotated by BRENDA team
Walls, A.F.; Bennett, A.R.; Sueiras-Diaz, J.; Olsson, H.
The kininogenase activity of human mast cell tryptase
Biochem. Soc. Trans.
20
260S
1992
Homo sapiens
Manually annotated by BRENDA team
Dietze, S.C.; Auerswald, E.A.; Fritz, H.
A new, highly sensitive enzymic assay for human tryptase and its use for identification of tryptase inhibitors
Biol. Chem. Hoppe-Seyler
371
65-73
1990
Homo sapiens
Manually annotated by BRENDA team
Schwartz, L.B.; Bradford, T.R.; Lee, D.C.; Chlebowski, J.F.
Immunologic and physicochemical evidence for conformational changes occurring on conversion of human mast cell tryptase from active tetramer to inactive monomer. Production of monoclonal antibodies recognizing active tryptase
J. Immunol.
144
2304-2311
1990
Homo sapiens
Manually annotated by BRENDA team
Sommerhoff, C.P.; Sllner, C.; Mentele, R.; Piechottka, G.P.; Auerswald, E.A.; Fritz, H.
A Kazal-type inhibitor of human mast cell tryptase: isolation from the medical leech Hirudo medicinalis, characterization, and sequence analysis
Biol. Chem. Hoppe-Seyler
375
685-694
1994
Homo sapiens
Manually annotated by BRENDA team
Sturzebecher, J.; Prasa, D.; Sommerhoff, C.P.
Inhibition of human mast cell tryptase by benzamidine derivatives
Biol. Chem. Hoppe-Seyler
373
1025-1030
1992
Homo sapiens
Manually annotated by BRENDA team
Schechter, N.M.; Eng, G.Y.; McCaslin, D.R.
Human skin tryptase: kinetic characterization of its spontaneous inactivation
Biochemistry
32
2617-2625
1993
Homo sapiens
Manually annotated by BRENDA team
Little, S.S.; Johnson, D.A.
Human mast cell tryptase isoforms: separation and examination of substrate-specificity differences
Biochem. J.
307
341-346
1995
Homo sapiens
Manually annotated by BRENDA team
Osman, I.A.R.; Garrett, J.R.; Smith, R.E.
Enzyme histochemical discrimination between tryptase and chymase in mast cells of human gut
J. Histochem. Cytochem.
37
415-421
1989
Homo sapiens
Manually annotated by BRENDA team
Sakai, K.; Long, S.D.; Pettit, D.A.D.; Cabral, G.A.; Schwartz, L.B.
Expression and purification of recombinant human tryptase in a baculovirus system
Protein Expr. Purif.
7
67-73
1996
Homo sapiens
Manually annotated by BRENDA team
Lohi, J.; Harvima, I.; Keski-Oja, J.
Pericellular substrates of human mast cell tryptase: 72,000 dalton gelatinase and fibronectin
J. Cell. Biochem.
50
337-349
1992
Homo sapiens
Manually annotated by BRENDA team
Butterfield, J.H.; Weiler, D.A.; Hunt, L.W.; Wynn, S.R.; Roche, P.C.
Purification of tryptase from a human mast cell line
J. Leukocyte Biol.
47
409-419
1990
Homo sapiens
Manually annotated by BRENDA team
Millner, J.S.; Westin, E.H.; Schwartz, L.B.
Cloning and characterization of complementary DNA for human tryptase
J. Clin. Invest.
84
1188-1195
1989
Homo sapiens
Manually annotated by BRENDA team
Cregar, L.; Elrod, K.C.; Putnam, D.; Moore, W.R.
Neutrophil myeloperoxidase is a potent and selective inhibitor of mast cell tryptase
Arch. Biochem. Biophys.
366
125-130
1999
Homo sapiens
Manually annotated by BRENDA team
Hallgren, J.; Estrada, S.; Karlson, U.; Alving, K.; Pejler, G.
Heparin antagonists are potent inhibitors of mast cell tryptase
Biochemistry
40
7342-7349
2001
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Selwood, T.; Wang, Z.M.; McCaslin, D.R.; Schechter, N.M.
Diverse stability and catalytic properties of human tryptase alpha and beta isoforms are mediated by residue differences at the S1 pocket
Biochemistry
41
3329-3340
2002
Homo sapiens
Manually annotated by BRENDA team
Selwood, T.; Elrod, K.C.; Schechter, N.M.
Potent bivalent inhibition of human tryptase-beta by a synthetic inhibitor
Biol. Chem.
384
1605-1611
2003
Homo sapiens
Manually annotated by BRENDA team
Schaschke, N.; Matschiner, G.; Zettl, F.; Marquardt, U.; Bergner, A.; Bode, W.; Sommerhoff, C.P.; Moroder, L.
Bivalent inhibition of human beta-tryptase
Chem. Biol.
8
313-327
2001
Homo sapiens
Manually annotated by BRENDA team
Peng, Q.; McEuen, A.R.; Benyon, R.C.; Walls, A.F.
The heterogeneity of mast cell tryptase from human lung and skin. Differences in size, charge and substrate affinity
Eur. J. Biochem.
270
270-283
2003
Homo sapiens
Manually annotated by BRENDA team
Stubbs, M.T.; Morenweiser, R.; Sturzebecher, J.; Bauer, M.; Bode, W.; Huber, R.; Piechottka, G.P.; Matschiner, G.; Sommerhoff, C.P.; Fritz, H.; Auerswald, E.A.
The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition
J. Biol. Chem.
272
19931-19937
1997
Homo sapiens
Manually annotated by BRENDA team
Huang, C.; Li, L.; Krilis, S.A.; Chanasyk, K.; Tang, Y.; Li, Z.; Hunt, J.E.; Stevens, R.L.
Human tryptases alpha and beta/II are functionally distinct due, in part, to a single amino acid difference in one of the surface loops that forms the substrate-binding cleft
J. Biol. Chem.
274
19670-19676
1999
Homo sapiens
Manually annotated by BRENDA team
Huang, C.; De Sanctis, G.T.; O'Brien, P.J.; Mizgerd, J.P.; Friend, D.S.; Drazen, J.M.; Brass, L.F.; Stevens, R.L.
Evaluation of the substrate specificity of human mast cell tryptase beta I and demonstration of its importance in bacterial infections of the lung
J. Biol. Chem.
276
26276-26284
2001
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Harris, J.L.; Niles, A.; Burdick, K.; Maffitt, M.; Backes, B.J.; Ellman, J.A.; Kuntz, I.; Haak-Frendscho, M.; Craik, C.S.
Definition of the extended substrate specificity determinants for b-tryptases I and II
J. Biol. Chem.
276
34941-34947
2001
Homo sapiens
Manually annotated by BRENDA team
Combrink, K.D.; Guelgeze, H.B.; Meanwell, N.A.; Pearce, B.C.; Zulan, P.; Bisacchi, G.S.; Roberts, D.G.; Stanley, P.; Seiler, S.M.
1,2-Benzisothiazol-3-one 1,1-dioxide inhibitors of human mast cell tryptase
J. Med. Chem.
41
4854-4860
1998
Homo sapiens
Manually annotated by BRENDA team
Costanzo, M.J.; Yabut, S.C.; Almond, H.R., Jr.; Andrade-Gordon, P.; Corcoran, T.W.; De Garavilla, L.; Kauffman, J.A.; Abraham, W.M.; Recacha, R.; Chattopadhyay, D.; Maryanoff, B.E.
Potent, small-molecule inhibitors of human mast cell tryptase. Antiasthmatic action of a dipeptide-based transition-state analogue containing a benzothiazole ketone
J. Med. Chem.
46
3865-3876
2003
Homo sapiens
Manually annotated by BRENDA team
Marquardt, U.; Zettl, F.; Huber, R.; Bode, W.; Sommerhoff, C.
The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region
J. Mol. Biol.
321
491-502
2002
Homo sapiens
Manually annotated by BRENDA team
Qian, X.; Zheng, B.; Burke, B.; Saindane, M.T.; Kronenthal, D.R.
A stereoselective synthesis of BMS-262084, an azetidinone-based tryptase inhibitor
J. Org. Chem.
67
3595-3600
2002
Homo sapiens
Manually annotated by BRENDA team
Mori, S.; Itoh, Y.; Shinohata, R.; Sendo, T.; Oishi, R.; Nishibori, M.
Nafamostat mesilate is an extremely potent inhibitor of human tryptase
J. Pharm. Sci.
92
420-423
2003
Homo sapiens
Manually annotated by BRENDA team
Pereira, P.J.B.; Bergner, A.; Macedo-Ribeiro, S.; Huber, R.; Matschiner, G.; Fritz, H.; Sommerhoff, C.P.; Bode, W.
Human b-tryptase is a ring-like tetramer with active sites facing a central pore
Nature
392
306-311
1998
Homo sapiens
Manually annotated by BRENDA team
Sommerhoff, C.P.; Bode, W.; Pereira, P.J.; Stubbs, M.T.; Stuerzebecher, J.; Piechottka, G.P.; Matschiner, G.; Bergner, A.
The structure of the human betaII-tryptase tetramer: fo(u)r better or worse
Proc. Natl. Acad. Sci. USA
96
10984-10991
1999
Homo sapiens
Manually annotated by BRENDA team
Burgess, L.E.; Newhouse, B.J.; Ibrahim, P.; Rizzi, J.; Kashem, M.A.; Hartman, A.; Brandhuber, B.J.; Wright, C.D.; Thomson, D.S.; Vigers, G.P.; Koch, K.
Potent selective nonpeptidic inhibitors of human lung tryptase
Proc. Natl. Acad. Sci. USA
96
8348-8352
1999
Homo sapiens
Manually annotated by BRENDA team
Chan, H.; Elrod, K.C.; Numerof, R.P.; Sideris, S.; Clark, J.M.
Expression and characterization of recombinant mast cell tryptase
Protein Expr. Purif.
15
251-257
1999
Homo sapiens
Manually annotated by BRENDA team
Ma, Y.; Zhang, B.; Qian, R.; Lu, C.; Zhao, F.; Yin, L.
Tryptase activates PKB in inflammatory reaction in ECV304 cells
Biochim. Biophys. Acta
1763
313-321
2006
Homo sapiens
Manually annotated by BRENDA team
Wong, T.; Groutas, C.S.; Mohan, S.; Lai, Z.; Alliston, K.R.; Vu, N.; Schechter, N.M.; Groutas, W.C.
1,2,5-Thiadiazolidin-3-one 1,1-dioxide-based heterocyclic sulfides are potent inhibitors of human tryptase
Arch. Biochem. Biophys.
436
1-7
2005
Homo sapiens
Manually annotated by BRENDA team
Sperandio, D.; Tai, V.W.; Lohman, J.; Hirschbein, B.; Mendonca, R.; Lee, C.S.; Spencer, J.R.; Janc, J.; Nguyen, M.; Beltman, J.; Sprengeler, P.; Scheerens, H.; Lin, T.; Liu, L.; Gadre, A.; Kellogg, A.; Green, M.J.; McGrath, M.E.
Novel, potent, selective, and orally bioavailable human betaII-tryptase inhibitors
Bioorg. Med. Chem. Lett.
16
4085-4089
2006
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Vliagoftis, H.; Lacy, P.; Luy, B.; Adamko, D.; Hollenberg, M.; Befus, D.; Moqbel, R.
Mast cell tryptase activates peripheral blood eosinophils to release granule-associated enzymes
Int. Arch. Allergy Immunol.
135
196-204
2004
Homo sapiens
Manually annotated by BRENDA team
Yuan, J.; Beltman, J.; Gjerstad, E.; Nguyen, M.T.; Sampang, J.; Chan, H.; Janc, J.W.; Clark, J.M.
Expression and characterization of recombinant gamma-tryptase
Protein Expr. Purif.
49
47-54
2006
Homo sapiens
Manually annotated by BRENDA team
Caughey, G.H.
Mast cell tryptases and chymases in inflammation and host defense
Immunol. Rev.
217
141-154
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Tatler, A.L.; Porte, J.; Knox, A.; Jenkins, G.; Pang, L.
Tryptase activates TGFbeta in human airway smooth muscle cells via direct proteolysis
Biochem. Biophys. Res. Commun.
370
239-242
2008
Homo sapiens
Manually annotated by BRENDA team
McGrath, M.E.; Sprengeler, P.A.; Hirschbein, B.; Somoza, J.R.; Lehoux, I.; Janc, J.W.; Gjerstad, E.; Graupe, M.; Estiarte, A.; Venkataramani, C.; Liu, Y.; Yee, R.; Ho, J.D.; Green, M.J.; Lee, C.S.; Liu, L.; Tai, V.; Spencer, J.; Sperandio, D.; Katz, B.A.
Structure-guided design of peptide-based tryptase inhibitors
Biochemistry
45
5964-5973
2006
Homo sapiens
Manually annotated by BRENDA team
Schechter, N.M.; Choi, E.J.; Selwood, T.; McCaslin, D.R.
Characterization of three distinct catalytic forms of human tryptase-beta: their interrelationships and relevance
Biochemistry
46
9615-9629
2007
Homo sapiens
Manually annotated by BRENDA team
Miyazaki, Y.; Kato, Y.; Manabe, T.; Shimada, H.; Mizuno, M.; Egusa, T.; Ohkouchi, M.; Shiromizu, I.; Matsusue, T.; Yamamoto, I.
Synthesis and evaluation of 4-substituted benzylamine derivatives as beta-tryptase inhibitors
Bioorg. Med. Chem. Lett.
16
2986-2990
2006
Homo sapiens
Manually annotated by BRENDA team
Palmer, J.T.; Rydzewski, R.M.; Mendonca, R.V.; Sperandio, D.; Spencer, J.R.; Hirschbein, B.L.; Lohman, J.; Beltman, J.; Nguyen, M.; Liu, L.
Design and synthesis of selective keto-1,2,4-oxadiazole-based tryptase inhibitors
Bioorg. Med. Chem. Lett.
16
3434-3439
2006
Homo sapiens
Manually annotated by BRENDA team
Lee, C.S.; Liu, W.; Sprengeler, P.A.; Somoza, J.R.; Janc, J.W.; Sperandio, D.; Spencer, J.R.; Green, M.J.; McGrath, M.E.
Design of novel, potent, and selective human beta-tryptase inhibitors based on alpha-keto-[1,2,4]-oxadiazoles
Bioorg. Med. Chem. Lett.
16
4036-4040
2006
Homo sapiens
Manually annotated by BRENDA team
Costanzo, M.J.; Yabut, S.C.; Zhang, H.C.; White, K.B.; de Garavilla, L.; Wang, Y.; Minor, L.K.; Tounge, B.A.; Barnakov, A.N.; Lewandowski, F.; Milligan, C.; Spurlino, J.C.; Abraham, W.M.; Boswell-Smith, V.; Page, C.P.; Maryanoff, B.E.
Potent, nonpeptide inhibitors of human mast cell tryptase. Synthesis and biological evaluation of novel spirocyclic piperidine amide derivatives
Bioorg. Med. Chem. Lett.
18
2114-2121
2008
Homo sapiens
Manually annotated by BRENDA team
Hallgren, J.; Pejler, G.
Biology of mast cell tryptase. An inflammatory mediator
FEBS J.
273
1871-1895
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Fukuoka, Y.; Schwartz, L.B.
Active monomers of human beta-tryptase have expanded substrate specificities
Int. Immunopharmacol.
7
1900-1908
2007
Homo sapiens
Manually annotated by BRENDA team
Pang, L.; Nie, M.; Corbett, L.; Sutcliffe, A.; Knox, A.J.
Mast cell beta-tryptase selectively cleaves eotaxin and RANTES and abrogates their eosinophil chemotactic activities
J. Immunol.
176
3788-3795
2006
Homo sapiens
Manually annotated by BRENDA team
Rohr, K.B.; Selwood, T.; Marquardt, U.; Huber, R.; Schechter, N.M.; Bode, W.; Than, M.E.
X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-beta-tryptase transition
J. Mol. Biol.
357
195-209
2006
Homo sapiens
Manually annotated by BRENDA team
Spichalska, B.; Lesner, A.; Wysocka, M.; Sledz, M.; Legowska, A.; Jaskiewicz, A.; Miecznikowska, H.; Rolka, K.
The influence of substrate peptide length on human beta-tryptase specificity
J. Pept. Sci.
14
917-923
2008
Homo sapiens
Manually annotated by BRENDA team
Storjord, E.; Nielsen, E.W.
Tryptase levels after suxamethonium administration and defibrillation
Acta Anaesthesiol. Scand.
52
838-840
2008
Homo sapiens
Manually annotated by BRENDA team
Kim, M.S.; Kim, Y.K.; Lee, D.H.; Seo, J.E.; Cho, K.H.; Eun, H.C.; Chung, J.H.
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
Br. J. Dermatol.
160
393-402
2009
Homo sapiens
Manually annotated by BRENDA team
Gerdes, S.; Kurrat, W.; Mrowietz, U.
Serum mast cell tryptase is not a useful marker for disease severity in psoriasis or atopic dermatitis
Br. J. Dermatol.
160
736-740
2009
Homo sapiens
Manually annotated by BRENDA team
Ribatti, D.; Nico, B.; Finato, N.; Crivellato, E.; Beltrami, C.A.
Co-localization of tryptase and cathepsin-G in mast cells in cutaneous mastocytosis
Cancer Lett.
279
209-212
2009
Homo sapiens
Manually annotated by BRENDA team
Potier, A.; Lavigne, C.; Chappard, D.; Verret, J.L.; Chevailler, A.; Nicolie, B.; Drouet, M.
Cutaneous manifestations in Hymenoptera and Diptera anaphylaxis: relationship with basal serum tryptase
Clin. Exp. Allergy
39
717-725
2009
Homo sapiens
Manually annotated by BRENDA team
Masuko, K.; Murata, M.; Xiang, Y.; Nakamura, H.; Yudoh, K.; Nishioka, K.; Beppu, M.; Kato, T.
Tryptase enhances release of vascular endothelial growth factor from human osteoarthritic chondrocytes
Clin. Exp. Rheumatol.
25
860-865
2008
Homo sapiens
Manually annotated by BRENDA team
de Rossi, T.M.; Krauss, N.; Wilken, V.; Giera, B.; Konturek, P.C.; Kressel, J.; Hahn, E.G.; Raithel, M.
Mast cell tryptase in sera of patients with Crohns disease and mastocytosis
Eur. J. Gastroenterol. Hepatol.
21
273-277
2009
Homo sapiens
Manually annotated by BRENDA team
Bonadonna, P.; Perbellini, O.; Passalacqua, G.; Caruso, B.; Colarossi, S.; Dal Fior, D.; Castellani, L.; Bonetto, C.; Frattini, F.; Dama, A.; Martinelli, G.; Chilosi, M.; Senna, G.; Pizzolo, G.; Zanotti, R.
Clonal mast cell disorders in patients with systemic reactions to Hymenoptera stings and increased serum tryptase levels
J. Allergy Clin. Immunol.
123
680-686
2009
Homo sapiens
Manually annotated by BRENDA team
McEuen, A.R.; Walls, A.F.
Purification and characterization of mast cell tryptase and chymase from human tissues
Methods Mol. Med.
138
299-317
2008
Homo sapiens
Manually annotated by BRENDA team
Rojas, I.G.; Martinez, A.; Brethauer, U.; Grez, P.; Yefi, R.; Luza, S.; Marchesani, F.J.
Actinic cheilitis: epithelial expression of COX-2 and its association with mast cell tryptase and PAR-2
Oral Oncol.
45
284-290
2009
Homo sapiens
Manually annotated by BRENDA team
Carr, M.N.; Torres, S.M.; Koch, S.N.; Reiter, L.V.
Investigation of the pruritogenic effects of histamine, serotonin, tryptase, substance P and interleukin-2 in healthy dogs
Vet. Dermatol.
20
105-110
2009
Homo sapiens
Manually annotated by BRENDA team
Fineschi, V.; Riezzo, I.; Cantatore, S.; Pomara, C.; Turillazzi, E.; Neri, M.
Complement C3a expression and tryptase degranulation as promising histopathological tests for diagnosing fatal amniotic fluid embolism
Virchows Arch.
454
283-290
2009
Homo sapiens
Manually annotated by BRENDA team
Chang, E.H.; Lee, J.H.; Zabner, J.
Tryptase does not alter transepithelial conductance or paracellular permeability in human airway epithelial cells
Am. J. Rhinol. Allergy
24
126-128
2010
Homo sapiens
Manually annotated by BRENDA team
Yeong, P.; Ning, Y.; Xu, Y.; Li, X.; Yin, L.
Tryptase promotes human monocyte-derived macrophage foam cell formation by suppressing LXRalpha activation
Biochim. Biophys. Acta
1801
567-576
2010
Homo sapiens
Manually annotated by BRENDA team
Schaschke, N.; Sommerhoff, C.
Upgrading a natural product: Inhibition of human beta-tryptase by cyclotheonamide analogues
ChemMedChem
5
367-370
2010
Homo sapiens
Manually annotated by BRENDA team
Gonzalez-Quintela, A.; Vizcaino, L.; Gude, F.; Rey, J.; Meijide, L.; Fernandez-Merino, C.; Linneberg, A.; Vidal, C.
Factors influencing serum total tryptase concentrations in a general adult population
Clin. Chem. Lab. Med.
48
701-706
2010
Homo sapiens
Manually annotated by BRENDA team
Dugas-Breit, S.; Przybilla, B.; Dugas, M.; Arnold, A.; Pfundstein, G.; Kuechenhoff, H.; Rueff, F.
Serum concentration of baseline mast cell tryptase: evidence for a decline during long-term immunotherapy for Hymenoptera venom allergy
Clin. Exp. Allergy
40
643-649
2010
Homo sapiens
Manually annotated by BRENDA team
Ricci, G.; Zannoni, M.; Cigolini, D.; Caroselli, C.; Codogni, R.; Caruso, B.; Bonello, E.; Rocca, G.P.
Tryptase serum level as a possible indicator of scombroid syndrome
Clin. Toxicol. (Phila.)
48
203-206
2010
Homo sapiens
Manually annotated by BRENDA team
Lee, J.W.; Park, J.H.; Park, D.I.; Park, J.H.; Kim, H.J.; Cho, Y.K.; Sohn, C.I.; Jeon, W.K.; Kim, B.I.
Subjects with diarrhea-predominant IBS have increased rectal permeability responsive to tryptase
Digest. Dis. Sci.
55
2922-2928
2010
Homo sapiens
Manually annotated by BRENDA team
Sperr, W.R.; El-Samahi, A.; Kundi, M.; Girschikofsky, M.; Winkler, S.; Lutz, D.; Endler, G.; Rumpold, H.; Agis, H.; Sillaber, C.; Jaeger, U.; Valent, P.
Elevated tryptase levels selectively cluster in myeloid neoplasms: a novel diagnostic approach and screen marker in clinical haematology
Eur. J. Clin. Invest.
39
914-923
2009
Homo sapiens
Manually annotated by BRENDA team
Lee, S.H.; Lee, J.H.; Lee, J.H.; Kim, D.K.
Involvement of MITF-A, an alternative isoform of mi transcription factor, on the expression of tryptase gene in human mast cells
Exp. Mol. Med.
42
366-375
2010
Homo sapiens
Manually annotated by BRENDA team
Reimer, J.M.; Samollow, P.B.; Hellman, L.
High degree of conservation of the multigene tryptase locus over the past 150-200 million years of mammalian evolution
Immunogenetics
62
369-382
2010
Mus musculus, Canis lupus familiaris (P15944), Canis lupus familiaris, Homo sapiens (P20231), Homo sapiens (Q15661), Homo sapiens, Meriones unguiculatus (P50342), Equus caballus (Q7YS62), Ovis aries (Q9XSM1), Ovis aries (Q9XSM2)
Manually annotated by BRENDA team
Bargagli, E.; Mazzi, A.; Mezzasalma, F.; Perrone, A.; Olivieri, C.; Prasse, A.; Bianchi, N.; Pieroni, M.G.; Rottoli, P.
The analysis of tryptase in serum of sarcoidosis patients
Inflammation
32
310-314
2009
Homo sapiens
Manually annotated by BRENDA team
Simon, M.R.; Jan, M.; Yee, J.; Nori, U.S.; Hu, J.; Akin, C.; Schwartz, L.B.
Tryptase is not cleared by the kidneys into the urine
Int. Arch. Allergy Immunol.
152
28-31
2010
Homo sapiens
Manually annotated by BRENDA team
Ranieri, G.; Ammendola, M.; Patruno, R.; Celano, G.; Zito, F.A.; Montemurro, S.; Rella, A.; Di Lecce, V.; Gadaleta, C.D.; Battista De Sarro, G.; Ribatti, D.
Tryptase-positive mast cells correlate with angiogenesis in early breast cancer patients
Int. J. Oncol.
35
115-120
2009
Homo sapiens
Manually annotated by BRENDA team
Trivedi, N.N.; Tamraz, B.; Chu, C.; Kwok, P.Y.; Caughey, G.H.
Human subjects are protected from mast cell tryptase deficiency despite frequent inheritance of loss-of-function mutations
J. Allergy Clin. Immunol.
124
1099-105
2009
Homo sapiens (P20231), Homo sapiens (Q15661), Homo sapiens
Manually annotated by BRENDA team
Schiemann, F.; Brandt, E.; Gross, R.; Lindner, B.; Mittelstaedt, J.; Sommerhoff, C.P.; Schulmistrat, J.; Petersen, F.
The cathelicidin LL-37 activates human mast cells and is degraded by mast cell tryptase: counter-regulation by CXCL4
J. Immunol.
183
2223-2231
2009
Homo sapiens
Manually annotated by BRENDA team
Thongyoo, P.; Bonomelli, C.; Leatherbarrow, R.J.; Tate, E.W.
Potent inhibitors of beta-tryptase and human leukocyte elastase based on the MCoTI-II scaffold
J. Med. Chem.
52
6197-6200
2009
Homo sapiens
Manually annotated by BRENDA team
Sommerhoff, C.P.; Avrutina, O.; Schmoldt, H.U.; Gabrijelcic-Geiger, D.; Diederichsen, U.; Kolmar, H.
Engineered cystine knot miniproteins as potent inhibitors of human mast cell tryptase beta
J. Mol. Biol.
395
167-175
2010
Homo sapiens
Manually annotated by BRENDA team
Carson, H.J.; Cook, B.A.
Mast cell tryptase in a case of anaphylaxis due to repeat antibiotic exposure
Leg. Med.
11
234-236
2009
Homo sapiens
Manually annotated by BRENDA team
Xiang, M.; Gu, Y.; Zhao, F.; Lu, H.; Chen, S.; Yin, L.
Mast cell tryptase promotes breast cancer migration and invasion
Oncol. Rep.
23
615-619
2010
Homo sapiens
Manually annotated by BRENDA team
Neri, M.; DErrico, S.; Fiore, C.; Pomara, C.; Rabozzi, R.; Riezzo, I.; Turillazzi, E.; Greco, P.; Fineschi, V.
Stillborn or liveborn? Comparing umbilical cord immunohistochemical expression of vitality markers (tryptase, alpha1-antichymotrypsin and CD68) by quantitative analysis and confocal laser scanning microscopy
Pathol. Res. Pract.
205
534-541
2009
Homo sapiens
Manually annotated by BRENDA team
Noyan, T.; Kolusari, A.; Kamaci, M.
Serum mast cell tryptase, eosinophil cationic protein, endothelin-1 and cytokine levels in preeclampsia and healthy pregnancy
Turk. J. Biochem.
34
19-24
2009
Homo sapiens
-
Manually annotated by BRENDA team
Wich, P.; Schmuck, C.
Reversible and noncompetitive inhibition of ?-tryptase by protein surface binding of tetravalent peptide ligands identified from a combinatorial split-mix library
Angew. Chem. Int. Ed. Engl.
49
4113-4116
2010
Homo sapiens
Manually annotated by BRENDA team
Santos, P.P.; Nonaka, C.F.; Pinto, L.P.; de Souza, L.B.
Immunohistochemical expression of mast cell tryptase in giant cell fibroma and inflammatory fibrous hyperplasia of the oral mucosa
Arch. Oral Biol.
56
231-237
2011
Homo sapiens
Manually annotated by BRENDA team
Janke, D.; Sommerhoff, C.P.; Schaschke, N.
The arginine mimicking beta-amino acid beta3hPhe(3-H2N-CH2) as S1 ligand in cyclotheonamide-based beta-tryptase inhibitors
Bioorg. Med. Chem.
19
7236-7243
2011
Homo sapiens
Manually annotated by BRENDA team
Ribatti, D.; Ranieri, G.; Nico, B.; Benagiano, V.; Crivellato, E.
Tryptase and chymase are angiogenic in vivo in the chorioallantoic membrane assay
Int. J. Dev. Biol.
55
99-102
2011
Homo sapiens
Manually annotated by BRENDA team
Spinnler, K.; Froehlich, T.; Arnold, G.J.; Kunz, L.; Mayerhofer, A.
Human tryptase cleaves pro-nerve growth factor (pro-NGF): hints of local, mast cell-dependent regulation of NGF/pro-NGF action
J. Biol. Chem.
286
31707-31713
2011
Homo sapiens
Manually annotated by BRENDA team
Murray, D.; McLarty-Williams, J.; Nagalla, K.; Janicki, J.
Tryptase activates isolated adult cardiac fibroblasts via protease activated receptor-2 (PAR-2)
J. Cell Commun. Signal.
6
45-51
2011
Homo sapiens
Manually annotated by BRENDA team
Yang, X.P.; Li, Y.; Wang, Y.; Wang, Y.; Wang, P.
beta-Tryptase up-regulates vascular endothelial growth factor expression via proteinase-activated receptor-2 and mitogen-activated protein kinase pathways in bone marrow stromal cells in acute myeloid leukemia
Leuk. Lymphoma
51
1550-1558
2010
Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Zheng, H.; Ma, W.; Wang, F.; Zeng, X.; Liu, C.; He, S.
Tryptase enzyme activity is correlated with severity of chronic obstructive pulmonary disease
Tohoku J. Exp. Med.
224
179-187
2011
Homo sapiens
Manually annotated by BRENDA team
Li, Q.; Jie, Y.; Wang, C.; Zhang, Y.; Guo, H.; Pan, Z.
Tryptase compromises corneal epithelial barrier function
Cell Biochem. Funct.
32
183-187
2014
Homo sapiens
Manually annotated by BRENDA team
Melo, F.R.; Vita, F.; Berent-Maoz, B.; Levi-Schaffer, F.; Zabucchi, G.; Pejler, G.
Proteolytic histone modification by mast cell tryptase, a serglycin proteoglycan-dependent secretory granule protease
J. Biol. Chem.
289
7682-7690
2014
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Wang, Y.; Zheng, Q.C.; Kong, C.P.; Tian, Y.; Zhan, J.; Zhang, J.L.; Zhang, H.X.
Heparin makes differences: a molecular dynamics simulation study on the human betaII-tryptase monomer
Mol. Biosyst.
11
252-261
2015
Homo sapiens
Manually annotated by BRENDA team
Jiang, Q.Q.; Bartsch, L.; Sicking, W.; Wich, P.R.; Heider, D.; Hoffmann, D.; Schmuck, C.
A new approach to inhibit human beta-tryptase by protein surface binding of four-armed peptide ligands with two different sets of arms
Org. Biomol. Chem.
11
1631-1639
2013
Homo sapiens
Manually annotated by BRENDA team
Pereira, B.A.; Lister, N.L.; Hashimoto, K.; Teng, L.; Flandes-Iparraguirre, M.; Eder, A.; Sanchez-Herrero, A.; Niranjan, B.; Niranjan, B.
Tissue engineered human prostate microtissues reveal key role of mast cell-derived tryptase in potentiating cancer-associated fibroblast (CAF)-induced morphometric transition in vitro
Biomaterials
197
72-85
2019
Homo sapiens
Manually annotated by BRENDA team
de Souza Junior, D.A.; Santana, A.C.; da Silva, E.Z.; Oliver, C.; Jamur, M.C.
The role of mast cell specific chymases and tryptases in tumor angiogenesis
BioMed Res. Int.
2015
142359
2015
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Ribatti, D.; Ranieri, G.
Tryptase, a novel angiogenic factor stored in mast cell granules
Exp. Cell Res.
332
157-162
2015
Homo sapiens
Manually annotated by BRENDA team
Atiakshin, D.; Buchwalow, I.; Samoilova, V.; Tiemann, M.
Tryptase as a polyfunctional component of mast cells
Histochem. Cell Biol.
149
461-477
2018
Homo sapiens
Manually annotated by BRENDA team
Wongrattanakamon, P.; Ampasavate, C.; Sirithunyalug, B.; Jiranusornkul, S.
An integrated molecular modeling approach for the tryptase monomer-curcuminoid recognition analysis conformational and bioenergetic features
J. Bioenerg. Biomembr.
50
447-459
2018
Homo sapiens (Q15661), Homo sapiens
Manually annotated by BRENDA team
Maun, H.R.; Liu, P.S.; Franke, Y.; Eigenbrot, C.; Forrest, W.F.; Schwartz, L.B.; Lazarus, R.A.
Dual functionality of beta-tryptase protomers as both proteases and cofactors in the active tetramer
J. Biol. Chem.
293
9614-9628
2018
Homo sapiens (Q15661), Homo sapiens
Manually annotated by BRENDA team