3.4.21.39: chymase
This is an abbreviated version!
For detailed information about chymase, go to the full flat file.
Word Map on EC 3.4.21.39
-
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
- 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
Reaction
preferential cleavage: Phe-/- > Tyr-/- > Trp-/- > Leu-/- =
Synonyms
alpha-chymase, beta-chymase, CAGE, Chy, chymase, chymase 1, chymostatin sensitive angiotensin generating enzyme, chymotrypsin-like protease, chymotryptic mast cell peptidase, CLP, CMA, CMA1, HAM1, mast cell chymase, mast cell chymases 4, mast cell protease, mast cell protease 1, mast cell protease 4, mast cell protease I, mast cell protease-2, mast cell protease-4, mast cell specific chymase, mast cell-derived chymase, mast-cell-derived chymase, MC chymase, MC protease 4, MC-chymase, MC-derived chymase, MC-specific chymase, MCC, MCP-1, MCP-2, MCP-4, MCP-5, MCP-8, MCP2, MCP4, Mcpt, MCPT-4, MCPT4, MMCP-1, mucosal mast cell protease, mucosal mast cell protease-1, proteinase, mast cell serine, chymase, RMCP I, skeletal muscle protease, skin chymotryptic proteinase
ECTree
3.4.21.39 chymaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.39 - chymase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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]
-
-
?
atrial natriuretic peptide clearance receptor + H2O
?
-
potential substrate
-
-
?
benzoyl-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Arg + 4-methylcoumarin 7-amide
-
1.2% of the activity with succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
no activity with enzyme forms 1D and 1E
-
-
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-L-Tyr + 4-nitroaniline
-
activity with enzyme form 1A, no activity with enzyme form 1B, 1C, 1D, 1E
-
-
?
benzyloxycarbonyl-Ala-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Ala + 4-nitrophenyl
-
-
-
-
?
benzyloxycarbonyl-Arg-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Arg + 4-nitrophenol
-
no activity with enzyme form 1B, 1C and 1E
-
-
?
benzyloxycarbonyl-D-Ala-4-nitrophenyl ester + H2O
benzyloxycarbonyl + D-Ala-4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Phe-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Phe + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Trp-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Trp + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Tyr-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Tyr-4-nitrophenyl ester
-
no activity with enzyme form 1C and 1E
-
-
?
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
-
-
-
-
?
MeO-succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
MeO-succinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Met-p-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Met + p-nitroaniline
-
low cleavage efficiency
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + p-nitroaniline
methoxysuccinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Ala-Tyr + 4-nitroaniline
methoxysuccinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Pro-Tyr + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-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 metalloprotease 2 + H2O
matrix metalloprotease 2 + propeptide
-
-
-
-
?
pro-matrix metalloprotease 9 + H2O
matrix metalloprotease 9 + ?
-
-
-
-
?
pro-matrix metalloprotease 9 + H2O
matrix metalloprotease 9 + propeptide
-
-
-
-
?
pro-matrix metalloproteinase-1 + H2O
matrix metalloproteinase-1 + ?
-
-
-
?
pro-matrix metalloproteinase-3 + H2O
matrix metalloproteinase-3 + ?
-
-
-
?
Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
4.6% of the activity with succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide
-
-
?
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-AAPL-4-nitroanilide + H2O
succinyl-AAPL + 4-nitroaniline
low activity
-
-
?
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-Ala-L-Ala-L-Pro-L-Phe-7-amido-4-methylcoumarin + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 7-amino-4-methylcoumarin
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-4-nitroanilide + H2O
succinyl-L-Leu-L-Leu-L-Val-L-Tyr + 4-nitroaniline
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Met-Val-Pro-Phe-4-nitroanilide + H2O
succinyl-Met-Val-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Phe-4-nitroanilide + H2O
succinyl-Phe + 4-nitroaniline
-
no activity with enzyme form 1C and 1D
-
-
?
succinyl-Phe-Val-Pro-Phe-4-nitroanilide + H2O
succinyl-Phe-Val-Pro-Phe + 4-nitroaniline
-
-
-
-
?
t-butyloxycarbonyl-Ala-Ala-Ser-thiobenzyl ester + H2O
?
-
weak activity
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarin 7-amide + H2O
?
-
2.6% of the activity with succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide
-
-
?
transforming growth factor beta-binding protein + H2O
transforming growth factor beta + protein
-
-
-
-
?
Ala-Ala-Pro-Leu-4-nitroanilide + H2O
Ala-Ala-Pro-Leu + 4-nitroaniline
-
-
-
?
Ala-Ala-Pro-Met-4-nitroanilide + H2O
Ala-Ala-Pro-Met + 4-nitroaniline
-
-
-
?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
negligible activity
-
-
?
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
-
-
?
angiotensin I + H2O
angiotensin II + His-Leu
-
hamster chymase cleaves the Phe8-His9 bond of angiotensin I
-
-
?
big-endothelin-1 (1-38) + H2O
endothelin-1 (1-31) + ?
-
chymase cleaves the tyrosine31-glycine32 peptide bond of big-endothelin-1 (1-38)
-
-
?
big-endothelin-1 (1-38) + H2O
endothelin-1 (1-31) + ?
-
chymase cleaves the tyrosine31-glycine32 peptide bond of big-endothelin-1 (1-38)
-
-
?
latent transforming growth factor-beta + H2O
active transforming growth factor-beta + ?
-
-
-
-
?
latent transforming growth factor-beta + H2O
active transforming growth factor-beta + ?
-
-
-
-
?
latent transforming growth factor-beta + H2O
active transforming growth factor-beta + ?
-
-
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
-
cleavage specificity as determined by substrate phage display P4: (Gly)Val, P3: Gly/Val, P2: Arg > Gly, P1: Phe > Tyr > Trp, P1': Leu > Val, P2': Ser > Glu/Asp > Leu, P3': Leu/Val
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
-
high activity
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + p-nitroaniline
-
-
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + p-nitroaniline
-
-
-
-
?
methoxysuccinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
-
?
methoxysuccinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
-
?
methoxysuccinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-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
-
-
-
?
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-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9 + ?
-
-
-
?
succinyl-AAPF-4-nitroanilide + H2O
succinyl-AAPF + 4-nitroaniline
-
-
-
-
?
Succinyl-Ala-Ala-Pro-Phe-4-methylcoumarin 7-amide + H2O
?
-
26.6% of the activity with succinyl-Leu-Leu-Val-Tyr-4-methylcoumarin 7-amide
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-epsilon-(2-picolinyl)Lys-Val-Pro-Phe-4-nitroanilide + H2O
?
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-7-amido-4-methylcoumarin + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-7-amido-4-methylcoumarin + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-LLVY-4-nitroanilide + H2O
succinyl-LLVY + 4-nitroaniline
-
-
-
-
?
succinyl-Phe-Ser-Phe-4-nitroanilide + H2O
succinyl-Phe-Ser-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-Phe-Ser-Phe-4-nitroanilide + H2O
succinyl-Phe-Ser-Phe + 4-nitroaniline
-
-
-
-
?
additional information
?
-
lacks elastase-like preference for P1 Val or Ala, and does not cleave angiotensin I
-
-
?
additional information
?
-
-
lacks elastase-like preference for P1 Val or Ala, and does not cleave angiotensin I
-
-
?
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
-
-
?
additional information
?
-
-
no activity with succinyl-AAPL-4-nitroanilide, succinyl-AAPI-4-nitroanilide, succinyl-AAPA-4-nitroanilide, succinyl-AAPV-4-nitroanilide, succinyl-VLGR-4-nitroanilide, benzyloxycarbonyl-GPR-4-nitroanilide, acetyl-YVAD-4-nitroanilide, acetyl-VEID-4-nitroanilide, and acetyl-IEPD-4-nitroanilide
-
-
?
additional information
?
-
-
the enzyme does not have a particular preference for any of the three aromatic amino acids, Phe, Tyr and Trp, in the P1 position of substrates and also efficiently cleaves after Leu (with a 3fold lower cleavage activity on Leu compared to substrates with P1 aromatic amino acids). The enzyme has a strong preference for negatively charged amino acids in the P2' position
-
-
?
additional information
?
-
-
shows chymotryptic activity and a strong preference for Trp over Phe and Tyr in the P1 position
-
-
?
additional information
?
-
-
in position P1 a distinct preference for Phe and Ser is observed, in position P2 a high selectivity for Phe, Trp and Leu is detected, while P3 and P4 show specificity for aliphatic amino acids
-
-
?
additional information
?
-
-
no activity with acetyl-Ile-Glu-Pro-Asp-p-nitroanilide, acetyl-Tyr-Val-Ala-Asp-p-nitroanilide, methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide, N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, H-D-Ile-Pro-Arg-p-nitroanilide, N-(p-tosyl)-Gly-Pro-Arg-p-nitroanilide, N-(p-tosyl)-Gly-Pro-Lys-p-nitroanilide, N-succinyl-Ala-Ala-Ala-p-nitroanilide, methoxy-succinyl-Ala-Ala-Pro-Met-p-nitroanilide, acetyl-Ile-Glu-Pro-Asp-p-nitroanilide, methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide, and N-(p-tosyl)-Gly-Pro-Lys-p-nitroanilide
-
-
?
additional information
?
-
-
prefers Phe in the P1 position (56%), followed by Tyr (28%) and Trp (16%), position P2 is most often occupied by Leu (22%), in positions P3 Val is the preferred amino acid, in position P4 is a preference for Val (20%) and Trp (19%) over other hydrophobic amino acids
-
-
?
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
-
-
?
additional information
?
-
no activity with succinyl-AAPI-4-nitroanilide, succinyl-AAPA-4-nitroanilide, succinyl-AAPV-4-nitroanilide, succinyl-VLGR-4-nitroanilide, benzyloxycarbonyl-GPR-4-nitroanilide, acetyl-YVAD-4-nitroanilide, acetyl-VEID-4-nitroanilide, and acetyl-IEPD-4-nitroanilide
-
-
?
additional information
?
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no activity with succinyl-AAPI-4-nitroanilide, succinyl-AAPA-4-nitroanilide, succinyl-AAPV-4-nitroanilide, succinyl-VLGR-4-nitroanilide, benzyloxycarbonyl-GPR-4-nitroanilide, acetyl-YVAD-4-nitroanilide, acetyl-VEID-4-nitroanilide, and acetyl-IEPD-4-nitroanilide
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additional information
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the enzyme shows preference for aromatic residues (Phe, Tyr, Trp) in the P1 position of substrates and a preference for aliphatic residues in most other substrate positions around the cleavage site. The enzyme also cleaves, albeit with relatively low efficiency, after Leu in the P1 position and exhibits unspecific preference in the P2' position
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additional information
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the enzyme shows preference for aromatic residues (Phe, Tyr, Trp) in the P1 position of substrates and a preference for aliphatic residues in most other substrate positions around the cleavage site. The enzyme also cleaves, albeit with relatively low efficiency, after Leu in the P1 position and exhibits unspecific preference in the P2' position
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additional information
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the enzyme from lymphocytes has a substrate preference for tryptophan, a preference distinct from rat mast cell chymase
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additional information
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the enzyme plays a crucial or significant role in the process of degranulation
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additional information
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the enzyme plays a role in production of a chemotactic factor for neutrophil leukocytes after degranulation
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additional information
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proteolytic degradation of low density lipoproteins by mast cell granules results from coordinated action of the two granule-bound enzymes - chymase and carboxypeptidase A. The chymase first cleaves peptides from the apolipoprotein B of low density lipoproteins, and thereafter the carboxypeptidase A cleaves amino acids from the peptides formed
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additional information
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prefers Phe in the P1 position (59%), followed by Trp (29%) and Tyr (12%), position P2 is most often occupied by Leu (24%) or Arg (22%), in positions P3 and P4 Val is the preferred amino acid
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