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Information on EC 3.4.21.39 - chymase and Organism(s) Homo sapiens
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3.4.21.39 chymaseSpecify your search results
Word Map
- 3.4.21.39
- tryptase
- granule
-
degranulation
- histamine
-
allergic
- chemokines
- ige
- cathepsin
- cardiac
- artery
- fibrosis
- neutrophil
-
angiotensin-converting
-
eosinophil
- cardiovascular
- monocyte
- asthma
- heparin
- airway
-
renin-angiotensin
- rantes
-
chemoattractant
- carboxypeptidase
- c-kit
- eotaxin
- renin
- elastase
-
chemotactic
-
basophil
- angiotensinogen
- endothelins
- anaphylaxis
-
anaphylactic
- toluidine
-
granzyme
- mastocytosis
-
tryptase-positive
-
atopic
-
exocytosed
- fcepsilonri
- cromolyn
-
anti-ige
- nippostrongylus
-
mip-1alpha
-
cell-deficient
-
mip-1beta
- medicine
- 3clpro
-
enzyme-histochemical
-
non-ace
-
ige-mediated
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
chymase, mcp-4, mast cell chymase, mast cell protease, chymotrypsin-like protease, mmcp-1, mcp-5, alpha-chymase, rmcp i, mast cell protease 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAGE
chymase
mast cell chymase
mast cell protease I
-
-
-
-
MC chymase
MMCP-1
-
-
-
-
proteinase, mast cell serine, chymase
-
-
-
-
RMCP I
-
-
-
-
skeletal muscle protease
-
-
-
-
skin chymotryptic proteinase
-
-
-
-
CAGE
-
-
-
-
chymase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
97501-92-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Dab(DNP) + H2O
2-aminobenzoyl-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + His-Dab(DNP)
-
the enzyme cleaves between Phe and His of modified angiotensin I permitting the release of His-[2-amino-4-(2,3-dinitrophenylamino)-butyrate]
-
-
?
big-endothelin-1 (1-38) + H2O
endothelin-1 (1-31) + ?
-
chymase cleaves the tyrosine31-glycine32 peptide bond of big-endothelin-1 (1-38)
-
-
?
chemerin + H2O
?
-
mast cell chymase abolishes chemerin activity by the removal of additional amino acids from its C-terminus, this effect is specific to bioactive chemerin (chemerin-157 and to a lesser extent chemerin-156)
-
-
?
cholesteryl ester transfer protein-high density lipoprotein complex + H2O
?
-
-
-
-
?
connective tissue-activating peptide III + H2O
neutrophil-activating peptide 2 + precursorpeptide
-
i.e. CTAP-II
i.e. NAP-2
-
?
fibrinogen + H2O
fibrin + ?
-
chymase degrades the alpha-, beta- and gamma-chains of fibrinogen, while heparin enhances the degradation of the beta-chain
-
-
?
FITC-Acp-DRVYIHPFHL-DDDDDC-labelled gold nanoparticles + H2O
FITC-Acp + DRVYIHPFHL-DDDDDC-labelld gold nanoparticles
-
-
-
-
?
latent transforming growth factor-beta + H2O
active transforming growth factor-beta + ?
-
-
-
-
?
MeO-succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
MeO-succinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
-
?
methoxysuccinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-His-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-His-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-p-nitroanilide + H2O
N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine + p-nitroaniline
-
-
-
-
?
N-succinyl-L-Leu-L-Leu-L-Val-L-Tyr-4-nitroanilide + H2O
N-succinyl-L-Leu-L-Leu-L-Val-L-Tyr + 4-nitroaniline
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 fragments
-
cleaves recombinant pro-interleukin-18 at 56-Phe
16 and 20 kDa fragments, the 16 kDa fragment is biologically active
-
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
-
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
-
-
-
?
pro-transforming growth factor-beta + H2O
transforming growth factor-beta + ?
-
-
-
?
pro-transforming growth factor-beta1 + H2O
transforming growth factor-beta1 + ?
-
-
-
?
secretory leucocyte protease inhibitor + H2O
?
-
cleaved secretory leucocyte protease inhibitor is a biomarker of chymase activity
-
-
?
secretory leukocyte protease inhibitor + H2O
?
-
the cleavage of recombinant human secretory leukocyte protease inhibitor by human chymase occurres at Leu72-Met73
the cleaved form of SLPI can be used as a biomarker of chymase activity
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Gly-Gly-Phe-p-nitroanilide + H2O
succinyl-Gly-Gly-Phe + p-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-4-nitroanilide + H2O
succinyl-L-Leu-L-Leu-L-Val-L-Tyr + 4-nitroaniline
-
-
-
?
succinyl-Phe-Ser-Phe-4-nitroanilide + H2O
succinyl-Phe-Ser-Phe + 4-nitroaniline
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
selective hydrolysis at Phe8 to generate bioactive angiotensin II, which can promote cardiac hypertrophy, vascular stenosis, and hypertension
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
the enzyme cleaves Tyr4 and Phe8 at rates of 5.47 and 17800 nM/min. Selective hydrolysis at Phe8 to generate bioactive angiotensin II. Lys40 of chymase contributes to the remarkable preference for angiotensin II generation over destruction
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
-
-
-
?
additional information
?
-
-
chymase mediates a major alternative way of angiotensin II production from angiotensin I beside angiotensin converting enzyme in the final step of the renin-angiotensin system. This enzyme is also involved in other physio-pathological processes such as angiogenesis, atherosclerosis and inflammation
-
-
?
additional information
?
-
-
chymase can activate eosinophils to markedly induce the release of chemokines CCL2 (monocyte chemotactic protein-1), CXCL1 (growth-regulated oncogene-alpha), CXCL8 (IL-8), and inflammatory cytokine IL-6, chymase activates ERK, p38 mitogen-activated protein kinase, Janus-activated kinase, Akt and nuclear factor-kappaB in eosinophils by induction of phosphorylation
-
-
?
additional information
?
-
-
chymase only accepts aromatic amino acids in position P1, with a strong preference for Tyr and Phe over Trp. Aliphatic amino acids are preferred in positions P2 to P4 N-terminal of the cleaved bond. In the P1' position C-terminal of the cleaved bond, Ser is clearly over-represented and acidic amino acids Asp and Glu are strongly preferred in the P2' position. In P3', the small aliphatic amino acids Ala, Val and Gly are frequently observed.
-
-
?
additional information
?
-
-
mast cell chymase does not use prochemerin as a substrate
-
-
?
additional information
?
-
interleukin-7, interleukin-22, GM-CSF, and CCL2 are resistant to chymase degradation
-
-
?
additional information
?
-
-
interleukin-7, interleukin-22, GM-CSF, and CCL2 are resistant to chymase degradation
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
big-endothelin-1 (1-38) + H2O
endothelin-1 (1-31) + ?
-
chymase cleaves the tyrosine31-glycine32 peptide bond of big-endothelin-1 (1-38)
-
-
?
fibrinogen + H2O
fibrin + ?
-
chymase degrades the alpha-, beta- and gamma-chains of fibrinogen, while heparin enhances the degradation of the beta-chain
-
-
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
-
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
-
-
-
?
pro-transforming growth factor-beta + H2O
transforming growth factor-beta + ?
-
-
-
?
pro-transforming growth factor-beta1 + H2O
transforming growth factor-beta1 + ?
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
-
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
selective hydrolysis at Phe8 to generate bioactive angiotensin II, which can promote cardiac hypertrophy, vascular stenosis, and hypertension
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
-
-
-
?
additional information
?
-
-
chymase mediates a major alternative way of angiotensin II production from angiotensin I beside angiotensin converting enzyme in the final step of the renin-angiotensin system. This enzyme is also involved in other physio-pathological processes such as angiogenesis, atherosclerosis and inflammation
-
-
?
additional information
?
-
-
chymase can activate eosinophils to markedly induce the release of chemokines CCL2 (monocyte chemotactic protein-1), CXCL1 (growth-regulated oncogene-alpha), CXCL8 (IL-8), and inflammatory cytokine IL-6, chymase activates ERK, p38 mitogen-activated protein kinase, Janus-activated kinase, Akt and nuclear factor-kappaB in eosinophils by induction of phosphorylation
-
-
?
additional information
?
-
-
chymase only accepts aromatic amino acids in position P1, with a strong preference for Tyr and Phe over Trp. Aliphatic amino acids are preferred in positions P2 to P4 N-terminal of the cleaved bond. In the P1' position C-terminal of the cleaved bond, Ser is clearly over-represented and acidic amino acids Asp and Glu are strongly preferred in the P2' position. In P3', the small aliphatic amino acids Ala, Val and Gly are frequently observed.
-
-
?
additional information
?
-
interleukin-7, interleukin-22, GM-CSF, and CCL2 are resistant to chymase degradation
-
-
?
additional information
?
-
-
interleukin-7, interleukin-22, GM-CSF, and CCL2 are resistant to chymase degradation
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(6E)-4-[(4-chlorophenyl)sulfonyl]-6-(phenylmethylidene)-1,4-diazepane-2,5-dione
-
-
(6R)-6-(5-chloro-2-methoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
-
-
(6S)-6-(5-chloro-2-methoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
-
potent inhibitor
1-(2-Amino-3-methyl-butyryl)-pyrrolidine-2-carboxylic acid (1-benzyl-3,3,3-trifluoro-2-oxo-propyl)-amide
-
-
1-[(5-fluoro-1-benzothiophen-3-yl)methyl]-3-{[(methoxycarbonyl)(methyl)amino]methyl}-1H-indole-2-carboxylate
-
2-(2-[2-[5-amino-2-(3-amino-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
2-(2-[2-[5-amino-2-(3-methoxy-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
i.e. Y40079, novel, potent and orally active chymase inhibitor which would be a useful tool in elucidating the pathophysiological roles of chymase
2-(2-[2-[5-amino-2-(3-nitro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
2-(2-{2-[5-amino-2-(3-amino-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido}-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
2-(2-{2-[5-amino-2-(3-chloro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido}-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
2-(2-{2-[5-amino-2-(3-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido}-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
2-(2-{2-[5-amino-2-(3-nitro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido}-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
2-(2-{2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido}-3-phenyl-propionyl)-benzooxazol-5-carboxylic acid diethylamide
-
-
2-(2-{2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido}-3-phenyl-propionyl)-benzooxazol-5-carboxylic acid ethyl ester
-
-
2-(2-{2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido}-3-phenyl-propionyl)-benzooxazol-5-carboxylic acid ethylamide
-
-
2-(2-{2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido}-3-phenyl-propionyl)-benzooxazol-6-carboxylic acid methyl ester
-
-
2-(2-{2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido}-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
2-(5-Acetylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(5-Amino-6-oxo-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(5-Amino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-hydroxypropyl)acetamide
-
-
2-(5-Amino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(5-amino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(2-phenethyl)acetamide
-
-
2-(5-Benzenesulfonylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(5-Benzoylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(5-Benzyloxycarbonylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(5-formylamino-6-oxo-2-phenyl-1,6-dihydropyrimidine-1-yl)-N-[[3,4-dioxo-1-phenyl-7-(2-pyridyloxy)]-2-heptyl]acetamide
-
NK3201
2-(5-formylamino-6-oxo-2-phenyl-1,6-dihydropyrimidine-1-yl)-N-[[3,4-dioxo-1-phenyl-7-(2-pyridyloxy)]-heptyl] acetamide
-
NK3201
2-(5-Hydroxysuccinylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(5-Mehoxysuccinylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(5-Methanesulfonylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(5-Oxaloamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-(N-benzyl-N-methylamino)-4H-3,1-benzoxazin-4-one
-
inhibitor forms a stable acyl-enzyme with half-life of 53 min
2-(N-methyl-N-phenylamino)-4H-3,1-benzoxazin-4-one
-
inhibitor forms a stable acyl-enzyme with half-life of 25 min
2-amino-4-[(1R)-1-([(6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3,7-dioxo-1,4-diazepane-1-carbonyl]amino)propyl]benzoic acid
-
2-amino-4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
-
-
2-amino-4-[(1R)-1-([[(6S)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
-
-
2-amino-4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3-(ethoxyimino)-7-oxo-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
-
2-amino-4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-7-oxo-3-(phenoxyimino)-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
-
2-amino-5-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
-
-
2-[2-(4-Fluorophenyl)-5-hydroxysuccinylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[2-[2-(5-amino-6-oxo-2-m-tolyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
2-[2-[2-(5-amino-6-oxo-2-phenyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
2-[2-[2-(5-amino-6-oxo-2-pyridin-3-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
2-[2-[2-(5-amino-6-oxo-2-pyridin-4-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
2-[2-[2-[5-amino-2-(3-chloro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
2-[2-[2-[5-amino-2-(3-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
2-[2-[2-[5-amino-2-(3-methoxy-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
2-[2-[2-[5-amino-2-(3-nitro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazol-5-carboxylic acid diethylamide
-
-
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazol-5-carboxylic acid ethyl ester
-
-
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazol-5-carboxylic acid ethylamide
-
-
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazol-6-carboxylic acid methyl ester
-
-
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
2-[4-(5-fluoro-3-methylbenzo[b] thiophen-2-yl)sulfonamido-3-methansulfonylphenyl]oxazole-4-carboxylic acid
-
TY-1184
2-[4-chloro-2-([1-[(4-chlorophenyl)sulfonyl]-3,7-dioxo-1,4-diazepan-6-yl]methyl)phenoxy]-N-methylacetamide
-
-
2-[5-Amino-2-(3-chlorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-2-(3-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-2-(4-aminophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-2-(4-chlorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxazolo[4,5-b]pyridin-2-yl-2-oxo-ethyl)-acetamide
-
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(2-benzothiazol-2-yl-1-benzyl-2-oxo-ethyl)-acetamide
-
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(4,5-dihydro-oxazol-2-yl)-2-oxo-ethyl]-acetamide
-
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(5-fluoro-benzooxazol-2-yl)-2-oxo-ethyl]-acetamide
-
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(5-methoxy-benzooxazol-2-yl)-2-oxo-ethyl]-acetamide
-
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-oxo-2-(5-phenyl-benzooxazol-2-yl)-ethyl]-acetamide
-
-
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(2-benzoxazolyl)carbonyl]-2-phenylethyl]-acetamide
-
-
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-aminobenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
-
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-carbamoylbenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
-
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-carboxybenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
-
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-hydroxybenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
-
2-[5-Amino-2-(4-hydroxyphenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-2-(4-methoxyphenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-2-(4-nitrophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-6-oxo-2-(2-thienyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-6-oxo-2-(3-pyridyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-6-oxo-2-(4-pyridyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-6-oxo-2-(m-tolyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-[5-Amino-6-oxo-2-(p-tolyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
2-{1-[(1,4-dimethyl-1H-indol-3-yl)methyl]-2,4-dioxo-1,4-dihydroquinazolin-3(2H)-yl}hexanoic acid
-
2-{2-[2-(5-Amino-6-oxo-2-m-tolyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl}-benzooxazole-5-carboxylic acid methyl ester
-
-
2-{2-[2-(5-Amino-6-oxo-2-phenyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl}-benzooxazole-5-carboxylic acid methyl ester
-
-
2-{2-[2-(5-Amino-6-oxo-2-pyridin-3-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl}-benzooxazole-5-carboxylic acid methyl ester
-
novel, potent, and orally active inhibitor. Rapidly after oral administration and has satisfactory bioavailability
2-{2-[2-(5-Amino-6-oxo-2-pyridin-4-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl}-benzooxazole-5-carboxylic acid methyl ester
-
-
3-([1-[(4-chlorophenyl)sulfonyl]-3,7-dioxo-1,4-diazepan-6-yl]methyl)-4-methoxybenzonitrile
-
-
3-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
-
-
3-[(1R)-1-([[(6S)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
-
-
3-[(3,4-dimethoxyphenyl)sulfonyl]-1-(3,4-dimethylphenyl)imidazoline-2,4-dione
-
C41
3-[5-Amino-6-oxo-2-(m-tolyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)propanamide
-
-
3[(3-amino-4-carboxy) phenylsulfonyl]-7-chloroquinazolone-2,4(1H,3H)-dione
-
N-C8257
4-({1-[(4-methyl-1-benzothiophen-3-yl)methyl]-1H-benzimidazol-2-yl}sulfanyl)butanoic acid
-
4-[(1R)-1-([(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3-[(2-methylpropoxy)imino]-7-oxo-1,4-diazepane-1-carbonyl]amino)propyl]benzoic acid
-
4-[(1R)-1-([(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3-[(cyclopentyloxy)imino]-7-oxo-1,4-diazepane-1-carbonyl]amino)propyl]benzoic acid
-
4-[(1R)-1-([(6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3,7-dioxo-1,4-diazepane-1-carbonyl]amino)propyl]benzoic acid
-
4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]-2-hydroxybenzoic acid
-
-
4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
-
-
4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3-(ethoxyimino)-7-oxo-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
-
4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-7-oxo-3-(phenoxyimino)-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
-
4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-7-oxo-3-[[(propan-2-yl)oxy]imino]-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
-
4-[(4-chlorophenyl)sulfonyl]-6-(2,5-dimethoxybenzyl)-1,4-diazepane-2,5-dione
-
-
4-[(4-chlorophenyl)sulfonyl]-6-(4,5-dichloro-2-methoxybenzyl)-1,4-diazepane-2,5-dione
-
-
4-[(4-chlorophenyl)sulfonyl]-6-(5-chloro-2-propoxybenzyl)-1,4-diazepane-2,5-dione
-
-
4-[(4-chlorophenyl)sulfonyl]-6-(5-fluoro-2-methoxybenzyl)-1,4-diazepane-2,5-dione
-
-
4-[(4-chlorophenyl)sulfonyl]-6-(5-hydroxy-2-methoxybenzyl)-1,4-diazepane-2,5-dione
-
-
4-[(4-chlorophenyl)sulfonyl]-6-(naphthalen-2-ylmethyl)-1,4-diazepane-2,5-dione
-
-
4-[1-[bis-(4-methyl-phenyl)-methyl]-carbamoyl]-3-(2-ethoxy-benzyl)-4-oxo-azetidine-2-yloxy-benzoic acid
-
BCEAB
4-[1-[[bis-(4-methyl-phenyl)-methyl]-carbamoyl]-3-(2-ethoxy-benzyl)-4-oxo-azetidine-2-yloxy]-benzoic acid
-
-
5-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]-2-hydroxybenzoic acid
-
-
6-(2-butoxy-5-chlorobenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
-
-
6-(3-chloro-5-fluoro-2-methoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
-
-
6-(5-chloro-2-ethoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
-
-
6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-N-(1-phenylbutyl)-1,4-diazepane-1-carboxamide
-
-
6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-N-(1-phenylethyl)-1,4-diazepane-1-carboxamide
-
-
6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-N-(1-phenylpropyl)-1,4-diazepane-1-carboxamide
-
-
6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-N-(2-phenylethyl)-1,4-diazepane-1-carboxamide
-
-
6-(5-chloro-2-methoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
-
-
6-(5-chloro-2-methoxybenzyl)-N-(2-methyl-1-phenylpropyl)-3,7-dioxo-1,4-diazepane-1-carboxamide
-
-
6-(5-chloro-2-methoxybenzyl)-N-(diphenylmethyl)-3,7-dioxo-1,4-diazepane-1-carboxamide
-
-
L-Valyl-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)-L-prolinamide hydrochloride
-
-
methyl 3-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoate
-
-
methyl[1-naphthalen-2-yl-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphinic acid
-
-
N-benzyl-6-(5-chloro-2-methoxybenzyl)-N-methyl-3,7-dioxo-1,4-diazepane-1-carboxamide
-
-
platelet factor 4
-
i.e. PF-4, competitive inhibition of enzyme and cathepsin G
-
SF2809-I
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.0073 mM
SF2809-II
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.000041 mM
SF2809-III
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.0021 mM
SF2809-IV
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.000081
SF2809-V
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.000043 mM
SF2809-VI
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.000014 mM
succinyl-Val-Pro-PheP-(OPh)2
-
highly specific and metabolically stable chymase inhibitor with a biological half-life of more than 20 h
SUN-C8257
-
i.e. 3-[(3-amino-4-carboxy)phenylsulfonyl]-7-chloroquinazorine 2,4(1H,3H)-dione
suramin
-
i.e. 8,8'-[carbonylbis[imino-3,1-phenylenecarbonylimino(4-methyl-3,1-phenylene)carbonylimino]]bis-1,3,5-naphthalenetrisulfonic acid
TY-51184
-
highly-specific and orally active chymase inhibitor; i.e. 2-[4-(5-fluoro-3-methylbenzo[b]thiophen-2-yl)sulfonamide-3-methanesulfonylphenyl]oxazole-4-carboxylic acid
TY-51469
-
i.e. 2-[4-(5-fluoro-3-methylbenzo[b]thiophen-2-yl)sulfonamido-3-methanesulfonylphenyl]thiazole-4-carboxylic acid; inhibitor with very high affinity (IC50 0.1 nmol/kg) against chymase
Y-40018
-
i.e. 4-[5-amino-2-(3-chlorophenyl)-6-oxo-1,6-dihydropyrimidin-1-ylacetamido]-N-benzyl-2,2-difluoro-3-oxo-5-phenylpentanamide
Y-40079
-
i.e. 2-[2-[2-[5-amino-2-(3-methoxyphenyl)-6-oxo-1,6-dihydropyrimidin-1-yl]acetamido]-3-phenylpropionyl]benzoxazole-5-carboxylic acid methyl ester
[1-(1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
-
-
[1-(1-methyl-1H-indol-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
-
-
[1-(2,3-dihydro-1H-benzotriazol-1-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
-
less than 50% inhibition at 0.01 mM
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl](2-phenylethyl)phosphinic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]ethylphosphinic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]methylphosphinic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phenylphosphinic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-oxo-2-[[(E)-2-phenylethenyl]amino]ethyl]methylphosphinic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-oxo-2-[[(E)-2-phenylethenyl]amino]ethyl]phosphonic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3,4-difluorophenyl)ethenyl]amino]-2-oxoethyl]ethylphosphinic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3,4-difluorophenyl)ethenyl]amino]-2-oxoethyl]methylphosphinic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3,4-difluorophenyl)ethenyl]amino]-2-oxoethyl]phosphonic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3-chloro-5-fluorophenyl)ethenyl]amino]-2-oxoethyl]methylphosphinic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3-chlorophenyl)ethenyl]amino]-2-oxoethyl]methylphosphinic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(4-fluorophenyl)ethenyl]amino]-2-oxoethyl]phosphonic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(4-methoxyphenyl)ethenyl]amino]-2-oxoethyl]phosphonic acid
-
-
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[2-(3,4-difluorophenyl)ethyl]amino]-2-oxoethyl]methylphosphinic acid
-
-
[1-(5-chloro-1-methyl-1H-indol-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]methylphosphinic acid
-
-
[1-(5-chloro-1-methyl-1H-indol-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonate
-
[1-(5-chloro-1-methyl-1H-indol-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
-
-
[1-(5-chloro-1-methyl-1H-indol-3-yl)-2-[[(E)-2-(3,4-difluorophenyl)ethenyl]amino]-2-oxoethyl]methylphosphinic acid
-
-
[1-(5-chloro-1-methyl-1H-indol-3-yl)-2-[[(E)-2-(4-fluorophenyl)ethenyl]amino]-2-oxoethyl]phosphonic acid
-
-
[1-[(1-Benzyl-2-hydroxy-2-oxazolo[5,4-b]pyridin-2-yl-ethylcarbamoyl)-methyl]-2-(4-fluoro-phenyl)-6-oxo-1,6-dihydro-pyrimidin-5-yl]-carbamic acid benzyl ester
-
-
[2-(3-[methyl[1-(naphthalen-2-ylcarbonyl)piperidin-4-yl]carbamoyl]naphthalen-2-yl)-1-naphthalen-1-yl-2-oxoethyl]phosphonic acid
-
-
[4-chloro-2-([1-[(4-chlorophenyl)sulfonyl]-3,7-dioxo-1,4-diazepan-6-yl]methyl)phenoxy]acetic acid
-
-
chymostatin
-
i.e. (S)-1-carboxy-2-(phenylethyl)-carbamoyl-alpha-[2-iminohexahydro-4(S)-pyrimidyl]-(S)-glycyl-X-phenylalaninal
chymostatin
-
80 ng/ml chymase is significantly inhibited by 0.015 mM chymostatin. 80% inhibition at 0.05 mM
JNJ-10311795
i.e. 2-[3-[methyl[1-(2-naphthoyl) piperidin-4-yl]amino]carbonyl-2-naphthyl]-1-(1-naphthyl)-2-oxoethylphosphonic acid
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
chymase has no enzymatic activity under normal physiological conditions, but it is activated immediately after release into the extracellular matrix
-
additional information
-
chymase is activated 3fold within 60 min in basal media by scratch wounding cultured monolayers and further potentiated over 10fold at 18 h by additional serum and cytokine treatment, chymase activation is attenuated by inhibition of nitric oxide, superoxide, and peroxynitrite
-
additional information
-
high glucose causes a 3fold increase in chymase mRNA level
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.514
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
in the presence of heparin, at pH 7.4 and 37°C
0.935
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
in the absence of heparin, at pH 7.4 and 37°C
0.0157
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-thiobenzyl ester
-
in the presence of heparin, at pH 7.4 and 37°C
0.0355
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-thiobenzyl ester
-
in the absence of heparin, at pH 7.4 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
in the presence of heparin, at pH 7.4 and 37°C
3.6
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
in the absence of heparin, at pH 7.4 and 37°C
12.6
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-thiobenzyl ester
-
in the absence of heparin, at pH 7.4 and 37°C
17.8
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-thiobenzyl ester
-
in the presence of heparin, at pH 7.4 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.85
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
in the absence of heparin, at pH 7.4 and 37°C
4.86
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide
-
in the presence of heparin, at pH 7.4 and 37°C
355
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-thiobenzyl ester
-
in the absence of heparin, at pH 7.4 and 37°C
1130
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-thiobenzyl ester
-
in the presence of heparin, at pH 7.4 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000005 - 0.0000821
1-(2-Amino-3-methyl-butyryl)-pyrrolidine-2-carboxylic acid (1-benzyl-3,3,3-trifluoro-2-oxo-propyl)-amide
0.0000261
2-(2-[2-[5-amino-2-(3-chloro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
0.0000143
2-(2-[2-[5-amino-2-(3-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
0.0000418
2-(2-[2-[5-amino-2-(3-nitro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
0.0000595
2-(2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazol-5-carboxylic acid diethylamide
-
-
0.00003
2-(2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazol-5-carboxylic acid ethyl ester
-
-
0.0000686
2-(2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazol-5-carboxylic acid ethylamide
-
-
0.0000563
2-(2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazol-6-carboxylic acid methyl ester
-
-
0.0000226 - 0.000026
2-(2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
0.000105
2-(5-Acetylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.06
2-(5-Amino-6-oxo-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.03
2-(5-Amino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-hydroxypropyl)acetamide
-
-
0.000389
2-(5-Amino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.11
2-(5-amino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(2-phenethyl)acetamide
-
-
0.000369
2-(5-Benzenesulfonylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000306
2-(5-Benzoylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000146
2-(5-Benzyloxycarbonylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.0000656
2-(5-Hydroxysuccinylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000229
2-(5-Mehoxysuccinylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.00103
2-(5-Methanesulfonylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.00447
2-(5-Oxaloamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl)-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000017
2-(N-benzyl-N-methylamino)-6-methyl-4H-3,1-benzoxazin-4-one
-
pH 8.0, 25°C
0.000237
2-[2-(4-Fluorophenyl)-5-hydroxysuccinylamino-6-oxo-2-phenyl-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.0000289 - 0.0000442
2-[2-[2-(5-amino-6-oxo-2-m-tolyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
0.00000356 - 0.00000557
2-[2-[2-(5-amino-6-oxo-2-phenyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
0.00000262 - 0.0000774
2-[2-[2-(5-amino-6-oxo-2-pyridin-3-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
0.0000138 - 0.0000435
2-[2-[2-(5-amino-6-oxo-2-pyridin-4-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
0.0000056 - 0.0004
2-[2-[2-[5-amino-2-(3-amino-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
0.0000169
2-[2-[2-[5-amino-2-(3-chloro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.0000185
2-[2-[2-[5-amino-2-(3-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.0000325 - 0.0000485
2-[2-[2-[5-amino-2-(3-methoxy-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
0.0000157
2-[2-[2-[5-amino-2-(3-nitro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.00000932
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazol-5-carboxylic acid diethylamide
-
pH 7.5, 37°C
0.0000102
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazol-5-carboxylic acid ethyl ester
-
pH 7.5, 37°C
0.00000771
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazol-5-carboxylic acid ethylamide
-
pH 7.5, 37°C
0.0000102
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazol-6-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.0000166
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.000124
2-[5-Amino-2-(3-chlorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000141
2-[5-Amino-2-(3-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.00012
2-[5-Amino-2-(4-aminophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000471
2-[5-Amino-2-(4-chlorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.0000606
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxazolo[4,5-b]pyridin-2-yl-2-oxo-ethyl)-acetamide
-
-
0.00385
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
-
0.000182
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(2-benzothiazol-2-yl-1-benzyl-2-oxo-ethyl)-acetamide
-
-
0.00589
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(4,5-dihydro-oxazol-2-yl)-2-oxo-ethyl]-acetamide
-
-
0.0000907 - 0.0000931
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(5-fluoro-benzooxazol-2-yl)-2-oxo-ethyl]-acetamide
0.0000733 - 0.000489
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(5-methoxy-benzooxazol-2-yl)-2-oxo-ethyl]-acetamide
0.0000097 - 0.000174
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-oxo-2-(5-phenyl-benzooxazol-2-yl)-ethyl]-acetamide
0.000305
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.0000133 - 0.000125
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(2-benzoxazolyl)carbonyl]-2-phenylethyl]-acetamide
0.000489
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-aminobenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
pH 7.5, 37°C
0.000012 - 0.000094
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-carbamoylbenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
0.0000169 - 0.00076
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-carboxybenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
0.0000097 - 0.00212
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-hydroxybenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
0.000479
2-[5-Amino-2-(4-hydroxyphenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000487
2-[5-Amino-2-(4-methoxyphenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000547
2-[5-Amino-2-(4-nitrophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000377
2-[5-Amino-6-oxo-2-(2-thienyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000658
2-[5-Amino-6-oxo-2-(3-pyridyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.00122
2-[5-Amino-6-oxo-2-(4-pyridyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.0000506
2-[5-Amino-6-oxo-2-(m-tolyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.000186
2-[5-Amino-6-oxo-2-(p-tolyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)acetamide
-
-
0.03
3-[5-Amino-6-oxo-2-(m-tolyl)-1,6-dihydro-1-pyrimidinyl]-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)propanamide
-
-
0.000029
6-methyl-2-(N-methyl-N-phenylamino)-4H-3,1-benzoxazin-4-one
-
pH 8.0, 25°C
0.00008
L-Valyl-N-(1-benzyl-3,3,3-trifluoro-2-oxopropyl)-L-prolinamide hydrochloride
-
-
0.0000506
[1-[(1-Benzyl-2-hydroxy-2-oxazolo[5,4-b]pyridin-2-yl-ethylcarbamoyl)-methyl]-2-(4-fluoro-phenyl)-6-oxo-1,6-dihydro-pyrimidin-5-yl]-carbamic acid benzyl ester
-
pH 7.5, 37°C
0.000005
1-(2-Amino-3-methyl-butyryl)-pyrrolidine-2-carboxylic acid (1-benzyl-3,3,3-trifluoro-2-oxo-propyl)-amide
-
pH 7.5, 37°C
0.0000821
1-(2-Amino-3-methyl-butyryl)-pyrrolidine-2-carboxylic acid (1-benzyl-3,3,3-trifluoro-2-oxo-propyl)-amide
-
-
0.0000226
2-(2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
0.000026
2-(2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl)-benzooxazole-5-carboxylic acid methyl ester
-
-
0.0000289
2-[2-[2-(5-amino-6-oxo-2-m-tolyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.0000442
2-[2-[2-(5-amino-6-oxo-2-m-tolyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
0.00000356
2-[2-[2-(5-amino-6-oxo-2-phenyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.00000557
2-[2-[2-(5-amino-6-oxo-2-phenyl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
0.00000262
2-[2-[2-(5-amino-6-oxo-2-pyridin-3-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.0000774
2-[2-[2-(5-amino-6-oxo-2-pyridin-3-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
0.0000138
2-[2-[2-(5-amino-6-oxo-2-pyridin-4-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.0000435
2-[2-[2-(5-amino-6-oxo-2-pyridin-4-yl-6H-pyrimidin-1-yl)-acetylamino]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
0.0000056
2-[2-[2-[5-amino-2-(3-amino-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
0.0004
2-[2-[2-[5-amino-2-(3-amino-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.0000325
2-[2-[2-[5-amino-2-(3-methoxy-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
pH 7.5, 37°C
0.0000485
2-[2-[2-[5-amino-2-(3-methoxy-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
i.e. Y40079, novel, potent and orally active chymase inhibitor which would be a useful tool in elucidating the pathophysiological roles of chymase
0.0000907
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(5-fluoro-benzooxazol-2-yl)-2-oxo-ethyl]-acetamide
-
pH 7.5, 37°C
0.0000931
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(5-fluoro-benzooxazol-2-yl)-2-oxo-ethyl]-acetamide
-
-
0.0000733
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(5-methoxy-benzooxazol-2-yl)-2-oxo-ethyl]-acetamide
-
-
0.000489
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-(5-methoxy-benzooxazol-2-yl)-2-oxo-ethyl]-acetamide
-
pH 7.5, 37°C
0.0000097
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-oxo-2-(5-phenyl-benzooxazol-2-yl)-ethyl]-acetamide
-
pH 7.5, 37°C
0.000174
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-[1-benzyl-2-oxo-2-(5-phenyl-benzooxazol-2-yl)-ethyl]-acetamide
-
-
0.0000133
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(2-benzoxazolyl)carbonyl]-2-phenylethyl]-acetamide
-
pH 7.5, 37°C
0.000125
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(2-benzoxazolyl)carbonyl]-2-phenylethyl]-acetamide
-
-
0.000012
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-carbamoylbenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
pH 7.5, 37°C
0.000094
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-carbamoylbenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
-
0.0000169
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-carboxybenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
pH 7.5, 37°C
0.00076
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-carboxybenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
-
0.0000097
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-hydroxybenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
pH 7.5, 37°C
0.000183
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-hydroxybenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
-
0.00212
2-[5-Amino-2-(4-fluorophenyl)-6-oxo-1,6-dihydro-1-pyrimidinyl]-N-[1-[(5-hydroxybenzoxazol-2-yl)carbonyl]-2-phenylethyl]acetamide
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
(6E)-4-[(4-chlorophenyl)sulfonyl]-6-(phenylmethylidene)-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.01
(6R)-6-(5-chloro-2-methoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.000027
(6S)-6-(5-chloro-2-methoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.0000025
2-(5-formylamino-6-oxo-2-phenyl-1,6-dihydropyrimidine-1-yl)-N-[[3,4-dioxo-1-phenyl-7-(2-pyridyloxy)]-2-heptyl]acetamide
Homo sapiens
-
-
0.000025
2-(5-formylamino-6-oxo-2-phenyl-1,6-dihydropyrimidine-1-yl)-N-[[3,4-dioxo-1-phenyl-7-(2-pyridyloxy)]-heptyl] acetamide
Homo sapiens
-
-
0.0003
2-amino-4-[(1R)-1-([(6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3,7-dioxo-1,4-diazepane-1-carbonyl]amino)propyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00034 - 0.0005
2-amino-4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
0.00017 - 0.01
2-amino-4-[(1R)-1-([[(6S)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
0.000078
2-amino-4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3-(ethoxyimino)-7-oxo-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0000089
2-amino-4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-7-oxo-3-(phenoxyimino)-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00041 - 0.0142
2-amino-5-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
0.000037
2-[4-(5-fluoro-3-methylbenzo[b] thiophen-2-yl)sulfonamido-3-methansulfonylphenyl]oxazole-4-carboxylic acid
Homo sapiens
-
-
0.000042
2-[4-chloro-2-([1-[(4-chlorophenyl)sulfonyl]-3,7-dioxo-1,4-diazepan-6-yl]methyl)phenoxy]-N-methylacetamide
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.000027
3-([1-[(4-chlorophenyl)sulfonyl]-3,7-dioxo-1,4-diazepan-6-yl]methyl)-4-methoxybenzonitrile
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.00054 - 0.0043
3-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
0.00024 - 0.01
3-[(1R)-1-([[(6S)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
0.00006
3-[(3,4-dimethoxyphenyl)sulfonyl]-1-(3,4-dimethylphenyl)imidazoline-2,4-dione
Homo sapiens
-
-
0.00031
3-[(3-amino-4-carboxy) phenylsulfonyl]-7-chloroquinazolone-2,4(1H,3H)-dione
Homo sapiens
-
-
0.0012
4-[(1R)-1-([(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3-[(2-methylpropoxy)imino]-7-oxo-1,4-diazepane-1-carbonyl]amino)propyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.0024
4-[(1R)-1-([(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3-[(cyclopentyloxy)imino]-7-oxo-1,4-diazepane-1-carbonyl]amino)propyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00057
4-[(1R)-1-([(6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3,7-dioxo-1,4-diazepane-1-carbonyl]amino)propyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00046 - 0.0018
4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]-2-hydroxybenzoic acid
0.00047 - 0.005
4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
0.00024
4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-3-(ethoxyimino)-7-oxo-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00005
4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-7-oxo-3-(phenoxyimino)-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00058
4-[(1R)-1-[[(3E,6R)-6-[(5-chloro-2-methoxyphenyl)methyl]-7-oxo-3-[[(propan-2-yl)oxy]imino]-1,4-diazepane-1-carbonyl]amino]propyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000018
4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.0074
4-[(4-chlorophenyl)sulfonyl]-6-(2,5-dimethoxybenzyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.00018
4-[(4-chlorophenyl)sulfonyl]-6-(2-ethoxybenzyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.00015
4-[(4-chlorophenyl)sulfonyl]-6-(2-fluorobenzyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.00014
4-[(4-chlorophenyl)sulfonyl]-6-(2-methoxybenzyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.000023
4-[(4-chlorophenyl)sulfonyl]-6-(4,5-dichloro-2-methoxybenzyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.00022
4-[(4-chlorophenyl)sulfonyl]-6-(5-chloro-2-propoxybenzyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.000026
4-[(4-chlorophenyl)sulfonyl]-6-(5-fluoro-2-methoxybenzyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.0011
4-[(4-chlorophenyl)sulfonyl]-6-(5-hydroxy-2-methoxybenzyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.01
4-[(4-chlorophenyl)sulfonyl]-6-(cyclohexylmethyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
IC50 above 0.01 mM, in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.01
4-[(4-chlorophenyl)sulfonyl]-6-(naphthalen-2-ylmethyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
IC50 above 0.01 mM, in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.01
4-[(4-chlorophenyl)sulfonyl]-6-(pyridin-3-ylmethyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
IC50 above 0.01 mM, in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.01
4-[(4-chlorophenyl)sulfonyl]-6-(pyridin-4-ylmethyl)-1,4-diazepane-2,5-dione
Homo sapiens
-
IC50 above 0.01 mM, in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.0000054
4-[1-[bis-(4-methyl-phenyl)-methyl]-carbamoyl]-3-(2-ethoxy-benzyl)-4-oxo-azetidine-2-yloxy-benzoic acid
Homo sapiens
-
-
0.0000054
4-[1-[[bis-(4-methyl-phenyl)-methyl]-carbamoyl]-3-(2-ethoxy-benzyl)-4-oxo-azetidine-2-yloxy]-benzoic acid
Homo sapiens
-
-
0.0041
5-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]-2-hydroxybenzoic acid
Homo sapiens
-
-
0.00028
6-(2-butoxy-5-chlorobenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.00011
6-(2-chlorobenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.0042
6-(3-chloro-5-fluoro-2-methoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.00031
6-(3-chlorobenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.00046
6-(4-chlorobenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.000083
6-(5-chloro-2-ethoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.0693
6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-N-(1-phenylbutyl)-1,4-diazepane-1-carboxamide
Homo sapiens
-
-
0.0053
6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-N-(1-phenylethyl)-1,4-diazepane-1-carboxamide
Homo sapiens
-
-
0.0028
6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-N-(1-phenylpropyl)-1,4-diazepane-1-carboxamide
Homo sapiens
-
-
0.0445
6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-N-(2-phenylethyl)-1,4-diazepane-1-carboxamide
Homo sapiens
-
-
0.000034
6-(5-chloro-2-methoxybenzyl)-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.003
6-(5-chloro-2-methoxybenzyl)-N-(2-methyl-1-phenylpropyl)-3,7-dioxo-1,4-diazepane-1-carboxamide
Homo sapiens
-
-
0.1
6-(5-chloro-2-methoxybenzyl)-N-(diphenylmethyl)-3,7-dioxo-1,4-diazepane-1-carboxamide
Homo sapiens
-
IC50 above 0.1 mM
0.00042
6-benzyl-4-[(4-chlorophenyl)sulfonyl]-1,4-diazepane-2,5-dione
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.0026 - 0.0514
methyl 3-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoate
0.00021
methyl[1-naphthalen-2-yl-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphinic acid
Homo sapiens
-
-
0.0049
N-benzyl-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepane-1-carboxamide
Homo sapiens
-
-
0.1
N-benzyl-6-(5-chloro-2-methoxybenzyl)-N-methyl-3,7-dioxo-1,4-diazepane-1-carboxamide
Homo sapiens
-
IC50 above 0.1 mM
0.0073
SF2809-I
Homo sapiens
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.0073 mM
0.000041
SF2809-II
Homo sapiens
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.000041 mM
0.0021
SF2809-III
Homo sapiens
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.0021 mM
0.000081
SF2809-IV
Homo sapiens
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.000081mM
0.000043
SF2809-V
Homo sapiens
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.000043 mM
0.000014
SF2809-VI
Homo sapiens
-
the inhibitor is isolated from the fermentation broth of Dactylosporangium sp., specific chymase inhibitor with little or no inhibitory activity against chymotrypsin or cathepsin G, IC50: 0.000014 mM
0.0025
[1-(1-benzofuran-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.00012
[1-(1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.00009
[1-(1-methyl-1H-indol-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.00092
[1-(1H-indol-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.00024
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl](2-phenylethyl)phosphinic acid
Homo sapiens
-
-
0.00016
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]ethylphosphinic acid
Homo sapiens
-
-
0.00008
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]methylphosphinic acid
Homo sapiens
-
-
0.0021
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phenylphosphinic acid
Homo sapiens
-
-
0.000029
[1-(5-chloro-1-benzothiophen-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.00005
[1-(5-chloro-1-benzothiophen-3-yl)-2-oxo-2-[[(E)-2-phenylethenyl]amino]ethyl]methylphosphinic acid
Homo sapiens
-
-
0.00006
[1-(5-chloro-1-benzothiophen-3-yl)-2-oxo-2-[[(E)-2-phenylethenyl]amino]ethyl]phosphonic acid
Homo sapiens
-
-
0.000165
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3,4-difluorophenyl)ethenyl]amino]-2-oxoethyl]ethylphosphinic acid
Homo sapiens
-
-
0.000058
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3,4-difluorophenyl)ethenyl]amino]-2-oxoethyl]methylphosphinic acid
Homo sapiens
-
-
0.000011
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3,4-difluorophenyl)ethenyl]amino]-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.000017
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3-chloro-5-fluorophenyl)ethenyl]amino]-2-oxoethyl]methylphosphinic acid
Homo sapiens
-
-
0.0000035
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(3-chlorophenyl)ethenyl]amino]-2-oxoethyl]methylphosphinic acid
Homo sapiens
-
-
0.000066
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(4-fluorophenyl)ethenyl]amino]-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.00028
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[(E)-2-(4-methoxyphenyl)ethenyl]amino]-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.0104
[1-(5-chloro-1-benzothiophen-3-yl)-2-[[2-(3,4-difluorophenyl)ethyl]amino]-2-oxoethyl]methylphosphinic acid
Homo sapiens
-
-
0.00001
[1-(5-chloro-1-methyl-1H-indol-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]methylphosphinic acid
Homo sapiens
-
-
0.000013
[1-(5-chloro-1-methyl-1H-indol-3-yl)-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.000021
[1-(5-chloro-1-methyl-1H-indol-3-yl)-2-[[(E)-2-(3,4-difluorophenyl)ethenyl]amino]-2-oxoethyl]methylphosphinic acid
Homo sapiens
-
-
0.000016
[1-(5-chloro-1-methyl-1H-indol-3-yl)-2-[[(E)-2-(4-fluorophenyl)ethenyl]amino]-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.00019
[1-naphthalen-1-yl-2-(naphthalen-2-ylamino)-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.0000045
[2-(3-[methyl[1-(naphthalen-2-ylcarbonyl)piperidin-4-yl]carbamoyl]naphthalen-2-yl)-1-naphthalen-1-yl-2-oxoethyl]phosphonic acid
Homo sapiens
-
-
0.000039
[4-chloro-2-([1-[(4-chlorophenyl)sulfonyl]-3,7-dioxo-1,4-diazepan-6-yl]methyl)phenoxy]acetic acid
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.00034
2-amino-4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.0005
2-amino-4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.00017
2-amino-4-[(1R)-1-([[(6S)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.0003
2-amino-4-[(1R)-1-([[(6S)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.01
2-amino-4-[(1R)-1-([[(6S)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
IC50 above 0.01 mM
0.00041
2-amino-5-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.0025
2-amino-5-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.0061
2-amino-5-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.0142
2-amino-5-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.00054
3-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.0043
3-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.00024
3-[(1R)-1-([[(6S)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.01
3-[(1R)-1-([[(6S)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
IC50 above 0.01 mM
0.00046
4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]-2-hydroxybenzoic acid
Homo sapiens
-
-
0.0018
4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]-2-hydroxybenzoic acid
Homo sapiens
-
-
0.00047
4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.00063
4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.005
4-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoic acid
Homo sapiens
-
-
0.000043
chymostatin
Homo sapiens
-
in 50 mM Tris/HCl buffer (pH 7.5) containing 1 M NaCl and 0.01% Triton X-100
0.0026
methyl 3-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoate
Homo sapiens
-
-
0.0514
methyl 3-[(1R)-1-([[(6R)-6-(5-chloro-2-methoxybenzyl)-3,7-dioxo-1,4-diazepan-1-yl]carbonyl]amino)propyl]benzoate
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
the pH range of chymase is between 7 and 9, there is no enzymatic activity at pH 5.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
81374, 81375, 81377, 81379, 81380, 81381, 81382, 654835, 654961, 654963, 655319, 655425, 655803, 656450, 656451, 668033, 668072, 677877, 678669, 678670, 679069, 679291, 679660, 680106, 680108, 680237, 680336, 680901, 681201, 681272, 681301, 681586, 682260, 682307, 696528, 697785, 698223, 698296, 698854, 699284, 699404, 699406, 700007, 700577, 701374, 708180, 717452, 717585, 717592, 731944
-
-
patients with macular holes, proliferative diabetic retinopathy, idiopathic epiretinal membrane, or rhegmatogenous retinal detachment
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
binding of the enzyme to heparin is likely to have a storage as well as a structural role within the mast cell granule, whereas binding of chymase to heparan sulfate may have physiological significance after degranulation
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
chymase deficiency reduces abdominal aortic aneurysm lesion angiogenesis or in vitro microvessel growth
metabolism
a 6-h treatment with 60 ng/ml chymase has a maximum effect on the stimulation of transforming growth factor-beta1 expression. In addition, a 6-h treatment with 30 ng/ml chymase has a maximum effect on the stimulation of interleukin-1beta expression
physiological function
physiological function
chymase facilitates the proliferation of skin fibroblasts
physiological function
chymase is involved in the progression of diabetes
physiological function
mast cell chymase degrades alarmins and may limit inflammation
physiological function
-
mast cell chymase plays an important role in keloid formation through transforming growth factor-beta1/Smad signaling pathway. Mast cell chymase upregulates Smad proteins in keloid fibroblasts
physiological function
the enzyme indirectly influences abdominal aortic aneurysm formation
physiological function
-
chymase, through synthesis of angiotensin II and other mediators, plays a role in the derangement of liver and kidney function in chronic liver diseases
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CMA1_HUMAN
247
0
27325
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
30000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
carbohydrate content is 10%. The N-glycan contributes to the stability of the enzyme but not to its functional properties
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.2 A crystal structure in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K192M
L40A
-
mutant enzyme retains strong preference for Phe8 with angiotensin I substrate but with Tyr4 hydrolytic rates enhance 16fold compared to wild-type enzyme
R143Q
R143Q/K192M
K192M
the mutant exhibits a markedly reduced sensitivity towards inhibitors compared to the wild type enzyme
R143Q
-
mutant enzyme remains highly Phe8-selective with angiotensin I substrate
R143Q
the mutant exhibits a markedly reduced sensitivity towards inhibitors compared to the wild type enzyme
R143Q/K192M
the mutant exhibits a markedly reduced sensitivity towards inhibitors compared to the wild type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), activation by His6-tag removal by cleavage with enterokinase, heparin-Sepharose chromatography
-
recombinant enzyme, procedure for expression and purification from culture media
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enterokinase cleavage site and N-terminal His6-tag, expressed in HEK 293 EBNA cell
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression and activity of mast cell chymase in keloid are significantly higher than those in normal skin
-
the enzyme expression is increased after treatment with transforming growth factor-beta1
-
there is a significant increase in the nasal lavage chymase levels in the allergen-challenged individuals as compared with placebo-exposed individuals
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
enzyme activity is significantly enhanced in vitreous fluid of patients wth idiopathic macular holes
medicine
-
number of cells positive for enzyme, tryptase, and kit receptor is markedly increased in skin of patients after irradiation therapy
medicine
-
target in vascular disease, chymase inhibition may represent a strategy for the treatment of vascular disease
medicine
-
carriers of the high-producer allele CMA/B A have increased risk of gastric cancer development, especially Helicobacter pylori-infected patients with non-cardia gastric cancer
medicine
-
mast cell-derived chymase plays an important role in juvenile crescentic glomerulonephritis
medicine
-
there is a positive association between the CMA1-1903 G/A single nucleotide polymorphism and asthma in children
medicine
chymase inhibitors have no blood pressure-lowering effect despite blocking angiotensin II formation. Thus, chymase inhibitors may be useful for preventing damage to various organs via multiple mechanisms without lowering blood pressure. Chymase inhibitors may be widely used for prevention of angiotensin II- and inflammation-related diseases
medicine
-
the fibrinolytic enzyme with anticoagulative properties may aid in the clearance of fibrin from vessel walls in aged vasculitis lesions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Powers, J.C.; Tanaka, T.; Harper, J.W.; Minematsu, Y.; Barker, L.; Lincoln, D.; Crumley, K.V.; Fraki, J.E.; Schechter, N.M.; Lazarus, G.G.; Nakajima, K.; Nakashino, K.; Neurath, H.; Woodbury, R.G.
Mammalian chymotrypsin-like enzymes. Comparative reactivities of rat mast cell proteases, human and dog skin chymases, and human cathepsin G with peptide 4-nitroanilide substrates and with peptide chloromethyl ketone and sulfonyl fluoride inhibitors
Biochemistry
24
2048-2058
1985
Canis lupus familiaris, Homo sapiens, Rattus norvegicus
Sayama, S.; Iozzo, R.V.; Lazarus, G.S.; Schechter, N.M.
Human skin chymotrypsin-like proteinase chymase. Subcellular localization to mast cell granules and interaction with heparin and other glycosaminoglycans
J. Biol. Chem.
262
6808-6815
1987
Homo sapiens
Johnson, L.A.; Moon, K.E.; Eisenberg, M.
Purification to homogeneity of the human skin chymotryptic proteinase chymase
Anal. Biochem.
155
358-364
1986
Homo sapiens
Pereira, P.J.B.; Wang, Z.M.; Rubin, H.; Huber, R.; Bode, W.; Schechter, N.M.; Strobl, S.
The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity
J. Mol. Biol.
286
163-173
1999
Homo sapiens
McGrath, M.E.; Mirzadegan, T.; Schmidt, B.F.
Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A
Biochemistry
36
14318-14324
1997
Homo sapiens (P23946), Homo sapiens
Takao, K.; Takai, S.; Shiota, N.; Song, K.; Nishimura, K.; Ishihara, T.; Miyazaki, M.
Lack of effect of carbohydrate depletion on some properties of human mast cell chymase
Biochim. Biophys. Acta
1427
74-81
1999
Homo sapiens
Takai, S.; Shiota, N.; Sakaguchi, M.; Muraguchi, H.; Matsumura, E.; Miyazaki, M.
Characterization of chymase from human vascular tissues
Clin. Chim. Acta
265
13-20
1997
Homo sapiens
Sukenaga, Y.; Kido, H.; Neki, A.; Enomoto, M.; Ishida, K.; Takagi, K.; Katunuma, N.
Purification and molecular cloning of chymase from human tonsils
FEBS Lett.
323
119-122
1993
Homo sapiens
Schechter, N.M.; Jordan, L.M.; James, A.M.; Cooperman, B.S.; Wang, Z.; Rubin, H.
Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties
J. Biol. Chem.
268
23626-23633
1993
Homo sapiens
McGrath, M.E.; Osawa, A.E.; Barnes, M.G.; Clark, J.M.; Mortara, K.D.; Schmidt, B.F.
Production of crystallizable human chymase from a Bacillus subtilis system
FEBS Lett.
413
486-488
1997
Homo sapiens
Waldeck, K.; Lindberg, B.F.; Persson, K.; Andersson, K.E.
Characterization of angiotensin II formation in human isolated bladder by selective inhibitors of ACE and human chymase: a functional and biochemical study
Br. J. Pharmacol.
121
1081-1086
1997
Homo sapiens
Schechter, N.M.; Sprows, J.L.; Schoenberger, O.L.; Lazarus, G.S.; Cooperman, B.S.; Rubin, H.
Reaction of human skin chymotrypsin-like proteinase chymase with plasma proteinase inhibitors
J. Biol. Chem.
264
21308-21315
1989
Homo sapiens
Muilenburg, D.J.; Raymond, W.W.; Wolters, P.J.; Caughey, G.H.
Lys40 but not Arg143 influences selectivity of angiotensin conversion by human alpha-chymase
Biochim. Biophys. Acta
1596
346-356
2002
Homo sapiens
Akahoshi, F.; Ashimori, A.; Yoshimura, T.; Imada, T.; Nakajima, M.; Mitsutomi, N.; Kuwahara, S.; Ohtsuka, T.; Fukaya, C.; Miyazaki, M.; Nakamura, N.
Non-peptidic inhibitors of human chymase. Synthesis, structure-activity relationships, and pharmacokinetic profiles of a series of 5-amino-6-oxo-1,6-dihydropyrimidine-containing trifluoromethyl ketones
Bioorg. Med. Chem.
9
301-315
2001
Homo sapiens
Neumann, U.; Schechter, N.M.; Gutschow, M.
Inhibition of human chymase by 2-amino-3,1-benzoxazin-4-ones
Bioorg. Med. Chem.
9
947-954
2001
Homo sapiens
Fukami, H.; Imajo, S.; Ito, A.; Kakutani, S.; Shibata, H.; Sumida, M.; Tanaka, T.; Niwata, S.; Saitoh, M.; Kiso, Y.; Miyazaki, M.; Okunishi, H.; Urata, H.; Arakawa, K.
Substituted 3-phenylsulfonylquinazoline-2,4-dione derivatives as novel nonpeptide inhibitors of human heart chymase
Drug Des. Discov.
17
69-84
2000
Homo sapiens
Ferry, G.; Gillet, L.; Bruneau, V.; Banales, J.M.; Beauverger, P.; Coge, F.; Galizzi, J.P.; Scalbert, E.; Okamoto, T.; Urata, H.; Boutin, J.A.
Development of new assays and improved procedures for the purification of recombinant human chymase
Eur. J. Biochem.
268
5885-5893
2001
Homo sapiens
Tani, M.; Gyobu, Y.; Sasaki, T.; Takenouchi, O.; Kawamura, T.; Kamimura, T.; Harada, T.
SF2809 compounds, novel chymase inhibitors from Dactylosporangium sp. 1. Taxonomy, fermentation, isolation and biological properties
J. Antibiot.
57
83-88
2004
Homo sapiens
Akahoshi, F.; Ashimori, A.; Sakashita, H.; Yoshimura, T.; Imada, T.; Nakajima, M.; Mitsutomi, N.; Kuwahara, S.; Ohtsuka, T.; Fukaya, C.; Miyazaki, M.; Nakamura, N.
Synthesis, structure-activity relationships, and pharmacokinetic profiles of nonpeptidic alpha-keto heterocycles as novel inhibitors of human chymase
J. Med. Chem.
44
1286-1296
2001
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Akahoshi, F.; Ashimori, A.; Sakashita, H.; Yoshimura, T.; Eda, M.; Imada, T.; Nakajima, M.; Mitsutomi, N.; Kuwahara, S.; Ohtsuka, T.; Fukaya, C.; Miyazaki, M.; Nakamura, N.
Synthesis, structure-activity relationships, and pharmacokinetic profiles of nonpeptidic difluoromethylene ketones as novel inhibitors of human chymase
J. Med. Chem.
44
1297-1304
2001
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Lockhart, B.E.; Vencill, J.R.; Felix, C.M.; Johnson, D.A.
Recombinant human mast-cell chymase: an improved procedure for expression in Pichia pastoris and purification of the highly active enzyme
Biotechnol. Appl. Biochem.
41
89-95
2005
Homo sapiens
Schiemann, F.; Grimm, T.A.; Hoch, J.; Gross, R.; Lindner, B.; Petersen, F.; Bulfone-Paus, S.; Brandt, E.
Mast cells and neutrophils proteolytically activate chemokine precursor CTAP-III and are subject to counterregulation by PF-4 through inhibition of chymase and cathepsin G
Blood
107
2234-2242
2006
Homo sapiens
Maruichi, M.; Oku, H.; Takai, S.; Muramatsu, M.; Sugiyama, T.; Imamura, Y.; Minami, M.; Ueki, M.; Satoh, B.; Sakaguchi, M.; Miyazaki, M.; Ikeda, T.
Measurement of activities in two different angiotensin II generating systems, chymase and angiotensin-converting enzyme, in the vitreous fluid of vitreoretinal diseases: a possible involvement of chymase in the pathogenesis of macular hole patients
Curr. Eye Res.
29
321-325
2004
Homo sapiens
Riekki, R.; Harvima, I.T.; Jukkola, A.; Risteli, J.; Oikarinen, A.
The production of collagen and the activity of mast-cell chymase increase in human skin after irradiation therapy
Exp. Dermatol.
13
364-371
2004
Homo sapiens
Heikkilae, H.M.; Laetti, S.; Leskinen, M.J.; Hakala, J.K.; Kovanen, P.T.; Lindstedt, K.A.
Activated mast cells induce endothelial cell apoptosis by a combined action of chymase and tumor necrosis factor-alpha
Arterioscler. Thromb. Vasc. Biol.
28
309-314
2008
Homo sapiens
Tanaka, T.; Muto, T.; Maruoka, H.; Imajo, S.; Fukami, H.; Tomimori, Y.; Fukuda, Y.; Nakatsuka, T.
Identification of 6-substituted 4-arylsulfonyl-1,4-diazepane-2,5-diones as a novel scaffold for human chymase inhibitors
Bioorg. Med. Chem. Lett.
17
3431-3434
2007
Homo sapiens
Maruoka, H.; Muto, T.; Tanaka, T.; Imajo, S.; Tomimori, Y.; Fukuda, Y.; Nakatsuka, T.
Development of 6-benzyl substituted 4-aminocarbonyl-1,4-diazepane-2,5-diones as orally active human chymase inhibitors
Bioorg. Med. Chem. Lett.
17
3435-3439
2007
Homo sapiens
Bacani, C.; Frishman, W.H.
Chymase: a new pharmacologic target in cardiovascular disease
Cardiol. Rev.
14
187-193
2006
Homo sapiens
Furubayashi, K.; Takai, S.; Jin, D.; Inagaki, S.; Kimura, M.; Nishimoto, M.; Fukumoto, H.; Tanaka, K.; Katsumata, T.; Miyazaki, M.
Chymase activates promatrix metalloproteinase-9 in human abdominal aortic aneurysm
Clin. Chim. Acta
388
214-216
2008
Homo sapiens
Terakawa, M.; Tomimori, Y.; Goto, M.; Fukuda, Y.
Mast cell chymase induces expression of chemokines for neutrophils in eosinophilic EoL-1 cells and mouse peritonitis eosinophils
Eur. J. Pharmacol.
538
175-181
2006
Homo sapiens, Mus musculus
Gallwitz, M.; Hellman, L.
Rapid lineage-specific diversification of the mast cell chymase locus during mammalian evolution
Immunogenetics
58
641-654
2006
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Caughey, G.H.
Mast cell tryptases and chymases in inflammation and host defense
Immunol. Rev.
217
141-154
2007
Homo sapiens, Mus musculus
Hirata, K.; Sugama, Y.; Ikura, Y.; Ohsawa, M.; Inoue, Y.; Yamamoto, S.; Kitaichi, M.; Ueda, M.
Enhanced mast cell chymase expression in human idiopathic interstitial pneumonia
Int. J. Mol. Med.
19
565-570
2007
Homo sapiens
Zanini, A.; Chetta, A.; Saetta, M.; Baraldo, S.; DIppolito, R.; Castagnaro, A.; Neri, M.; Olivieri, D.
Chymase-positive mast cells play a role in the vascular component of airway remodeling in asthma
J. Allergy Clin. Immunol.
120
329-333
2007
Homo sapiens
Caughey, G.H.; Beauchamp, J.; Schlatter, D.; Raymond, W.W.; Trivedi, N.N.; Banner, D.; Mauser, H.; Fingerle, J.
Guinea pig chymase is leucine-specific: A novel example of functional plasticity in the chymase/granzyme family of serine peptidases
J. Biol. Chem.
283
13943-13951
2008
Homo sapiens, Cavia porcellus (A7WPL7), Cavia porcellus
Omoto, Y.; Tokime, K.; Yamanaka, K.; Habe, K.; Morioka, T.; Kurokawa, I.; Tsutsui, H.; Yamanishi, K.; Nakanishi, K.; Mizutani, H.
Human mast cell chymase cleaves pro-IL-18 and generates a novel and biologically active IL-18 fragment
J. Immunol.
177
8315-8319
2006
Homo sapiens
Lee-Rueckert, M.; Vikstedt, R.; Metso, J.; Jauhiainen, M.; Kovanen, P.T.
Association of cholesteryl ester transfer protein with HDL particles reduces its proteolytic inactivation by mast cell chymase
J. Lipid Res.
49
358-368
2008
Homo sapiens
Greco, M.N.; Hawkins, M.J.; Powell, E.T.; Almond, H.R.; de Garavilla, L.; Hall, J.; Minor, L.K.; Wang, Y.; Corcoran, T.W.; Di Cera, E.; Cantwell, A.M.; Savvides, S.N.; Damiano, B.P.; Maryanoff, B.E.
Discovery of potent, selective, orally active, nonpeptide inhibitors of human mast cell chymase
J. Med. Chem.
50
1727-1730
2007
Homo sapiens
Miyazaki, M.; Takai, S.
Tissue angiotensin II generating system by angiotensin-converting enzyme and chymase
J. Pharmacol. Sci.
100
391-397
2006
Homo sapiens
Miyazaki, M.; Takai, S.; Jin, D.; Muramatsu, M.
Pathological roles of angiotensin II produced by mast cell chymase and the effects of chymase inhibition in animal models
Pharmacol. Ther.
112
668-676
2006
Canis lupus familiaris, Homo sapiens, Mesocricetus auratus
Wang, Y.; Gu, Y.; Zhang, Y.; Lewis, D.F.; Alexander, J.S.; Granger, D.N.
Increased chymotrypsin-like protease (chymase) expression and activity in placentas from women with preeclampsia
Placenta
28
263-269
2007
Homo sapiens
Belkowski, S.M.; Masucci, J.; Mahan, A.; Kervinen, J.; Olson, M.; de Garavilla, L.; DAndrea, M.R.
Cleaved SLPI, a novel biomarker of chymase activity
Biol. Chem.
389
1219-1224
2008
Homo sapiens
Cristovam, P.C.; Arnoni, C.P.; de Andrade, M.C.; Casarini, D.E.; Pereira, L.G.; Schor, N.; Boim, M.A.
ACE-dependent and chymase-dependent angiotensin II generation in normal and glucose-stimulated human mesangial cells
Exp. Biol. Med.
233
1035-1043
2008
Homo sapiens
Wong, C.K.; Ng, S.S.; Lun, S.W.; Cao, J.; Lam, C.W.
Signalling mechanisms regulating the activation of human eosinophils by mast-cell-derived chymase: implications for mast cell-eosinophil interaction in allergic inflammation
Immunology
126
579-587
2009
Homo sapiens
Andersson, M.K.; Enoksson, M.; Gallwitz, M.; Hellman, L.
The extended substrate specificity of the human mast cell chymase reveals a serine protease with well-defined substrate recognition profile
Int. Immunol.
21
95-104
2009
Homo sapiens
Firth, J.D.; Uitto, V.J.; Putnins, E.E.
Mechanical induction of an epithelial cell chymase associated with wound edge migration
J. Biol. Chem.
283
34983-34993
2008
Homo sapiens
Sugimoto, M.; Furuta, T.; Kodaira, C.; Nishino, M.; Yamade, M.; Ikuma, M.; Sugimura, H.; Hishida, A.
Polymorphisms of matrix metalloproteinase-7 and chymase are associated with susceptibility to and progression of gastric cancer in Japan
J. Gastroenterol.
43
751-761
2008
Homo sapiens
Hossny, E.M.; Amr, N.H.; Elsayed, S.B.; Nasr, R.A.; Ibraheim, E.M.
Association of polymorphisms in the mast cell chymase gene promoter region (-1903 g/A) and (TG)n(GA)m repeat downstream of the gene with bronchial asthma in children
J. Investig. Allergol. Clin. Immunol.
18
376-381
2008
Homo sapiens
Guillabert, A.; Wittamer, V.; Bondue, B.; Godot, V.; Imbault, V.; Parmentier, M.; Communi, D.
Role of neutrophil proteinase 3 and mast cell chymase in chemerin proteolytic regulation
J. Leukoc. Biol.
84
1530-1538
2008
Homo sapiens
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
Togawa, H.; Nakanishi, K.; Shima, Y.; Obana, M.; Sako, M.; Nozu, K.; Tanaka, R.; Iijima, K.; Yoshikawa, N.
Increased chymase-positive mast cells in children with crescentic glomerulonephritis
Pediatr. Nephrol.
24
1071-1075
2009
Homo sapiens
DOrleans-Juste, P.; Houde, M.; Rae, G.A.; Bkaily, G.; Carrier, E.; Simard, E.
Endothelin-1 (1-31): from chymase-dependent synthesis to cardiovascular pathologies
Vascul. Pharmacol.
49
51-62
2008
Homo sapiens, Mus musculus
Belkowski, S.M.; Boot, J.D.; Mascelli, M.A.; Diamant, Z.; de Garavilla, L.; Hertzog, B.; Polkovitch, D.; Towers, M.; Batheja, A.; DAndrea, M.R.
Cleaved secretory leucocyte protease inhibitor as a biomarker of chymase activity in allergic airway disease
Clin. Exp. Allergy
39
1179-1186
2009
Homo sapiens
Bot, I.; Bot, M.; van Heiningen, S.H.; van Santbrink, P.J.; Lankhuizen, I.M.; Hartman, P.; Gruener, S.; Hilpert, H.; van Berkel, T.J.; Fingerle, J.; Biessen, E.A.
Mast cell chymase inhibition reduces atherosclerotic plaque progression and improves plaque stability in ApoE-/- mice
Cardiovasc. Res.
89
244-252
2011
Homo sapiens
Andersson, M.K.; Thorpe, M.; Hellman, L.
Arg143 and Lys192 of the human mast cell chymase mediate the preference for acidic amino acids in position P2 of substrates
FEBS J.
277
2255-2267
2010
Homo sapiens
Korkmaz, B.; Jegot, G.; Lau, L.C.; Thorpe, M.; Pitois, E.; Juliano, L.; Walls, A.F.; Hellman, L.; Gauthier, F.
Discriminating between the activities of human cathepsin G and chymase using fluorogenic substrates
FEBS J.
278
2635-2646
2011
Homo sapiens
Dong, X.; Zhang, C.; Ma, S.; Wen, H.
Mast cell chymase in keloid induces profibrotic response via transforming growth factor-beta1/Smad activation in keloid fibroblasts
Int. J. Clin. Exp. Pathol.
7
3596-3607
2014
Homo sapiens
Roy, A.; Ganesh, G.; Sippola, H.; Bolin, S.; Sawesi, O.; Dagaelv, A.; Schlenner, S.M.; Feyerabend, T.; Rodewald, H.R.; Kjellen, L.; Hellman, L.; Abrink, M.
Mast cell chymase degrades the alarmins heat shock protein 70, biglycan, HMGB1, and interleukin-33 (IL-33) and limits danger-induced inflammation
J. Biol. Chem.
289
237-250
2014
Mus musculus (P21812), Mus musculus, Homo sapiens (P23946), Homo sapiens
Takai, S.; Jin, D.; Miyazaki, M.
Multiple mechanisms for the action of chymase inhibitors
J. Pharmacol. Sci.
118
311-316
2012
Homo sapiens (P23946)
Dong, X.; Chen, J.; Zhang, Y.; Cen, Y.
Mast cell chymase promotes cell proliferation and expression of certain cytokines in a dose-dependent manner
Mol. Med. Rep.
5
1487-1490
2012
Homo sapiens (P23946), Homo sapiens
Ahooghalandari, P.; Hanke, N.; Thorpe, M.; Witte, A.; Messinger, J.; Hellman, L.
Mutations in Arg143 and Lys192 of the human mast cell chymase markedly affect the activity of five potent human chymase inhibitors
PLoS ONE
8
e65988
2013
Homo sapiens (P23946), Homo sapiens
Smith, E.T.; Perry, E.T.; Sears, M.B.; Johnson, D.A.
Expression of recombinant human mast cell chymase with Asn-linked glycans in glycoengineered Pichia pastoris
Protein Expr. Purif.
102
69-75
2014
Homo sapiens
Wang, Y.; Shi, G.P.
Mast cell chymase and tryptase in abdominal aortic aneurysm formation
Trends Cardiovasc. Med.
22
150-155
2012
Homo sapiens (P23946), Homo sapiens
Dubey, A.; Marabotti, A.; Ramteke, P.W.; Facchiano, A.
Interaction of human chymase with ginkgolides, terpene trilactones of Ginkgo biloba investigated by molecular docking simulations
Biochem. Biophys. Res. Commun.
473
449-454
2016
Homo sapiens (P23946), Homo sapiens
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
Futamura-Takahashi, J.; Tanaka, T.; Sugawara, H.; Iwashita, S.; Imajo, S.; Oyama, Y.; Muto, T.
Structure-based design, synthesis, and binding mode analysis of novel and potent chymase inhibitors
Bioorg. Med. Chem. Lett.
28
188-192
2018
Homo sapiens (P23946), Homo sapiens
Lipitsae, T.; Siiskonen, H.; Naukkarinen, A.; Harvima, I.T.
Mast cell chymase degrades fibrinogen and fibrin
Br. J. Dermatol.
181
296-303
2019
Homo sapiens
Sansoe, G.; Aragno, M.; Mastrocola, R.; Mengozzi, G.; Novo, E.; Parola, M.
Role of chymase in the development of liver cirrhosis and its complications experimental and human data
PLoS ONE
11
e0162644
2016
Homo sapiens, Rattus norvegicus
Chang, H.; Sun, Y.; Yeh, F.; Tseng, I.; Chang, C.; Lin, C.
Detection of chymase activity using a specific peptide probe conjugated onto gold nanoparticles
RSC Adv.
8
29013-29021
2018
Homo sapiens
-
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