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Information on EC 3.4.21.37 - leukocyte elastase
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3.4.21.37 leukocyte elastaseSpecify your search results
Word Map
- 3.4.21.37
- proteases
- trypsin
- pulmonary
- pancreatic
- proteinase
- cathepsin
- aeruginosa
- chymotrypsin
- elastin
- cytokine
- emphysema
- myeloperoxidase
- airway
- porcine
-
lavage
- arterial
- fibrosis
- collagen
- granule
-
cystic
- alveolar
-
bronchoalveolar
- collagenase
- aortic
-
elastolytic
-
degranulation
- aneurysm
- leucocyte
- hne
- thrombin
- sputum
- lactoferrin
-
1-antitrypsin
-
intratracheal
- serpins
-
instil
- interleukin-8
-
cardiopulmonary
-
antiprotease
-
azurophilic
-
2-macroglobulin
- kallikrein
- fmlp
- alpha1-antitrypsin
-
crevicular
-
antineutrophil
-
ancas
-
neutrophil-mediated
-
thrombin-antithrombin
- drug development
- diagnostics
-
wegener
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Hydrolysis of proteins, including elastin. Preferential cleavage Val-/- > Ala-/-
Synonyms
bone marrow serine protease, EC 3.4.21.11, EC 3.4.4.7, ELA2, Elane, elastase, elaszym, granulocyte elastase, H2A specific protease, H2Asp, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bone marrow serine protease
-
-
-
-
EC 3.4.21.11
-
-
formerly
-
EC 3.4.4.7
-
-
formerly
-
ELA2
Elane
elastase
elaszym
-
-
-
-
granulocyte elastase
HLE
HNE
leukocyte elastase
lysosomal elastase
-
-
-
-
NE
-
-
-
-
neutrophil elastase
PMN elastase
PMNE
serine elastase
-
-
-
-
elastase
-
-
-
-
granulocyte elastase
-
-
-
-
HNE
-
-
-
-
HNE
-
-
leukocyte elastase
-
-
neutrophil elastase
-
-
-
-
neutrophil elastase
-
-
683043, 683056, 683536, 683956, 695509, 696938, 697718, 697826, 698305, 698311, 698394, 698506, 698834, 699427, 699523, 699737, 699857, 700135, 700570, 700848, 700892, 701181, 701184, 701431, 707645, 707673, 707710, 707735, 707850, 707913, 708182, 708208, 708305, 708306, 708387, 708680, 708691, 708812, 708813, 709357, 709363, 709383, 709493, 709714, 709937, 709989, 710206, 717334, 717369, 717378, 717832, 717895, 718417, 718423, 731124, 731591, 731991, 732294, 732438, 732564, 732600, 732758, 732907, 752482, 753664, 754279, 754758, 755135, 755426
neutrophil elastase
-
-
neutrophil elastase
-
-
PMN elastase
-
-
-
-
PMNE
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins, including elastin. Preferential cleavage Val-/- > Ala-/-
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
peptides
-
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CAS REGISTRY NUMBER
COMMENTARY
9004-06-2
eastase
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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
(VGVAPG)2V + H2O
VGVAPGVGV + APGV + VGVAPG + VGVAPGV
-
human elastin exon 24-derived peptide substrate, hydrolysis by the enzyme occurs when its active site is fully occupied by the substrate, cleavage at Val-Ala and at Gly-Val bonds, the latter to a lesser extent
-
-
?
(VGVAPG)3V + H2O
VGVAPGVGV + APGVGVAPGV + VGVAPGVGVAPGVGV + APGV + VGVAPG + VGVAPGVGVAPGV + GVAPGV
-
human elastin exon 24-derived peptide substrate, hydrolysis by the enzyme occurs when its active site is fully occupied by the substrate, cleavage at Val-Ala and at Gly-Val bonds, the latter to a lesser extent
-
-
?
1-ethyl-3,3-dimethyl-2-[(E)-2-[6-(2,2,3,3,3-pentafluoropropanamido)-2,3-dihydro-1H-xanthen-4-yl]ethenyl]-3H-indol-1-ium + H2O
2-[(E)-2-(6-amino-2,3-dihydro-1H-xanthen-4-yl)ethenyl]-1-ethyl-3,3-dimethyl-3H-indol-1-ium + 2,2,3,3,3-pentafluoropropanal
-
-
-
-
ir
2-aminobenzoyl-APEEIMDQQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-APEEI + MDQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
kcat/Km is 136times greater for neutrophil elastase than for proteinase 3
-
-
?
2-aminobenzoyl-APEEIMDRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-APEEI + MDRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
kcat/Km is 47times greater for neutrophil elastase than for proteinase 3
-
-
?
2-aminobenzoyl-APEEIMDRYQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-APEEI + MDRYQ-N-(2,4-dinitrophenyl)ethylenediamine
-
kcat/Km is 30times greater for neutrophil elastase than for proteinase 3
-
-
?
2-aminobenzoyl-APEEIMDYQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-APEEI + MDYQ-N-(2,4-dinitrophenyl)ethylenediamine
-
kcat/Km is 114times greater for neutrophil elastase than for proteinase 3
-
-
?
2-aminobenzoyl-APEEIMPRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-APEEI + MPRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
kcat/Km is over 11times greater for neutrophil elastase than for proteinase 3
-
-
?
2-aminobenzoyl-APEEIMRRQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-APEEI + MRRQ-N-(2,4-dinitrophenyl)ethylenediamine
-
kcat/Km is over 500times greater for neutrophil elastase than for proteinase 3
-
-
?
Abz-APEEIMDDQ-ethylene diamine 2,4 dinitrophenyl + H2O
2-aminobenzoyl-APEEI + MDDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
kcat/Km is 45times greater for neutrophil elastase than for proteinase 3
-
-
?
acetyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
acetyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
alpha1-PI + H2O
?
-
important antiprotease of the lung, enzyme reduces the lungs’ primary protection against proteolysis
-
-
?
APG(VGVAPG)2 + H2O
APGVGV + APGVAPGV + APGVGVAPGVGV + APGVGVAPG + APGV + VGVAPGV
-
human elastin exon 24-derived peptide substrate, hydrolysis by the enzyme occurs when its active site is fully occupied by the substrate, cleavage at Val-Ala and at Gly-Val bonds, the latter to a lesser extent
-
-
?
benzyloxycarbonyl-Ala-4-nitrophenol + H2O
benzyloxycarbonyl-Ala + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-L-Ala 2-naphthyl ester + H2O
benzyloxycarbonyl-Ala + 2-naphthol
-
-
-
-
?
BP180/type XVII collagen + H2O
peptide p561 + peptide p506
-
neutrophil elastase degrades recombinant mouse BP180 within the immunodominant extracellular domain at amino acid positions 506 and 561
-
-
?
Factor VIIIa + H2O
?
-
neutrophil elastase inactivates factor VIIIa. The enzyme proteolyses the heavy chain of factor VIIIa into two terminal products, A11-358 and A2375-708, by limited proteolysis at Val358, Val374, and Val708
-
-
?
IgA + H2O
?
-
involved in the regulation of inflammation by a feedback mechanism, elastase treated IgA preparations are unable to induce oxidative burst of polymorphonuclear leukocytes
protein cleaved in the hinge region
-
?
IgG + H2O
?
-
involved in the regulation of inflammation by a feedback mechanism, elastase treated IgG preparations are unable to induce oxidative burst of polymorphonuclear leukocytes
protein cleaved in the hinge region
-
?
interleukin-36 receptor antagonist + H2O
activated interleukin-36 receptor antagonist V2 + ?
-
the enzyme cleaves 9 amino acids upstream of the A-X-D consensus of interleukin-36 receptor antagonist
-
-
?
IpaB protein + H2O
?
-
neutrophil elastase cleaves IpaB protein after alanine, valine, isoleucine, or threonine residues
-
-
?
laminin-332 + H2O
?
-
neutrophil elastase shows the greatest activity toward the gamma2 chain of laminin-332, in addition, neutrophil elastase cleaves a synthetic peptide derived from the region of human laminin gamma2 containing the matrix metalloproteinase-2 cleavage site, suggesting that neutrophil elastase may generate laminin-332 fragments that are also promigratory
-
-
?
matrix metalloprotease 9 + H2O
matrix metalloprotease 9 peptide fragments
-
i.e. MMP-9, neutrophil elastase cleaves and activates at two specific cleavage sites, between Val38 and Ala39, and between Ala 39 and Glu40
-
-
?
matrix metalloproteinase-7 + H2O
?
-
human leukocyte elastase may be a natural inactivator of matrix metalloproteinase-7 which can counteract matrix metalloproteinase-7-induced apoptosis resistance
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-methylcoumarin 7-amide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 7-amino-4-methylcoumarin
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Va + 4-nitroanilide
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
methoxysuccinyl-Ala-Ala-Pro-Val-7-amido-4-methylcoumarin + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 7-amino-4-methylcoumarin
-
-
-
-
?
methoxysuccinyl-Val-4-nitroanilide
methoxysuccinyl-Val + 4-nitroaniline
-
-
-
-
?
N-methoxy-succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxy-succinyl-Ala-Ala-Pro-Val + 4-nitroaniline
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
N-methoxysuccinyl-Ala-Ala-Pro-Val-7-amido-4-methylcoumarin + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 7-amino-4-methylcoumarin
-
-
-
-
?
N-methoxysuccinyl-L-Ala-L-Ala-L-Pro-L-Val-4-nitroanilide + H2O
N-methoxysuccinyl-L-Ala-L-Ala-L-Pro-L-Val + 4-nitroaniline
-
-
-
-
?
N-methoxysuccinyl-L-Ala-L-Ala-L-Pro-L-Val-7-amido-4-methylcoumarin + H2O
N-methoxysuccinyl-L-Ala-L-Ala-L-Pro-L-Val + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
Nalpha-methoxysuccinyl-Nepsilon-2-picolinoyl-L-lysinyl-L-Ala-L-Pro-L-Val 4-nitroanilide + H2O
?
-
-
-
-
-
native type I collagen + H2O
3/4 length fragments similar in size to those produced by interstitial collagenase
-
human, bovine and rat type I collagen, the enzyme can cleave native type I collagen in the helix
-
?
o-aminobenzoic acid-Ala-Pro-Glu-Glu-Ile-Met-Asp-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoic acid-Glu-Ala-Ile-Pro-Met-Ser-Ile-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoic acid-Glu-Ala-Ile-Pro-Met-Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoic acid-Gly-Ile-Ala-Thr-Phe-Cys-Met-Leu-Met-Pro-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoic acid-Ile-Val-Ser-Ala-Arg-Met-Ala-Pro-Glu-Glu-Ile-Ile-Met-Asp-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoic acid-Met-Met-Arg-Cys-Ala-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoic acid-Thr-Phe-Cys-Met-Leu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoic acid-Val-Ala-Asp-Cys-Ala-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoic acid-Val-Ala-Glu-Cys-Cys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoic acid-Val-Ser-Ala-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
oxytalan fibre + H2O
?
-
the elastase degrades the interfibrillar substances in the periodontal ligament and exposed individual collagen fibrils but not the collagen fibers of the transverse sections of rat mandibular first molars
-
-
?
procarboxypeptidase R + H2O
carboxypeptidase R + ?
-
generation of activated carboxypeptidase R from procarboxypeptidase R by elastase from activated neutrophils at the site of inflammation should contribute to the suppression of excessive inflammation and any abnormality in this mechanism can induce serious hyper-inflammation such as seen in multiple organ failure
-
-
?
Protein + H2O
?
-
enzyme capable of degrading proteins of the lung extracellular matrix in vitro
-
-
?
proteinase-activated receptor 2 N-terminus + H2O
GPNSKGRSLIGRLDTPPPITGKGAPVEPGFSVDEFSAS + VLTGKLTTVFLP
-
-
-
-
?
SLPI + H2O
?
-
important antiprotease of the lung, enzyme reduces the lungs’ primary protection against proteolysis
-
-
?
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala-Ala + p-nitroaniline
-
-
-
-
?
syndecan-1 + H2O
?
-
the heparan sulfate moiety of shed syndecan-1 binds and restricts neutrophil elastase from inhibition by alpha-1-antitrypsin
-
-
?
tert-butyloxycarbonyl-Ala-2-naphthyl ester + H2O
tert-butyloxycarbonyl-Ala + 2-naphthol
-
-
-
-
?
tert-butyloxycarbonyl-Ala-4-nitrophenyl ester + H2O
tert-butyloxycarbonyl-Ala + 4-nitrophenol
tert-butyloxycarbonyl-Val-4-nitrophenyl ester + H2O
tert-butyloxycarbonyl-Val + 4-nitrophenol
-
-
-
-
?
tissue inhibitor of metalloprotease-1 + H2O
tissue inhibitor of metalloprotease-1 peptide fragments
-
i.e. TIMP-1, neutrophil elastase degrades TIMP-1 and cleaves between Val69-Cys70
-
-
?
VAPGVGVAPGV + H2O
VAPGVGV + APGV + VAPGV + GVAPGV
-
human elastin exon 24-derived peptide substrate, hydrolysis by the enzyme occurs when its active site is fully occupied by the substrate, cleavage at Val-Ala and at Gly-Val bonds, the latter to a lesser extent
-
-
?
annexin 1 + H2O
?
-
annexin 1 is externalized and truncated upon adhesion of polymorphonuclear leukocytes to endothelial cells, annexin 1 participates in regulating leukocyte emigration into inflamed tissue through N-terminal peptides generated at inflammatory sites, overview
-
-
?
annexin 1 + H2O
?
-
cleavage of N-terminal peptides, recombinant substrate
-
-
?
antithrombin + H2O
?
-
catalyzes the inactivation of antithrombin by a specific and limited proteinolytic cleavage
-
-
?
antithrombin + H2O
?
-
leukocyte elastase inactivates antithrombin by a specific and limited proteolytic cleavage
-
-
?
corticosteroid-binding globulin + H2O
?
-
cleavage by neutrophil elastase destroys ligand binding capacity and supposedly liberates cortisol at sites of inflammation. Enzyme activity on wild-type and mutant CBG serpin recombinantly produced by 293-EBNA cells, overview. CBG mutant G335V is more sensitive for elastase cleavage, while CBG mutant T342A is more resistant to elastase cleavage
-
-
?
corticosteroid-binding globulin + H2O
?
-
a serpin family of serine protease inhibitor secreted by the liver
-
-
?
elafin + H2O
?
-
elafin is cleaved by its cognate enzyme neutrophil elastase, neutrophil elastase-mediated cleavage of elafin abolishes the capacity of the inhibitor to cross-link to fibronectin by transglutamination, neutrophil elastase-mediated cleavages of elafin at Val5-Lys-6 and Val9-Ser10 peptide bonds only occur with 2x excess of neutrophil elastase, a partial cleavage of the inhibitor is identified at the scissile peptide bond Ala24-Met25
-
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
-
647546, 647548, 647552, 663596, 663821, 663914, 664635, 664846, 664848, 665158, 665458, 665911, 666151, 666152, 696403, 696938, 697329, 697826, 698394, 717369, 717904, 718421, 731106, 731124, 731591, 731788, 731991, 732294, 732438, 732564, 732600, 732758, 732907, 754758
-
-
?
Elastin + H2O
?
-
the enzyme cleaves elastin selectively near the cross-linking desmosine residues
-
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells also might be damaged, involved in the onset of emphysema and rheumatoid arthritis
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, enzyme is assumed to play a key role in the gradual decrease of lung function during cystic fibrosis
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the onset of emphysema, acute respiratory distress syndrome, and rheumatoid arthritis
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
generation of soluble peptides by limited proteolysis, elastin-derived peptides play roles in cell migration, differentiation, proliferation, chemotaxis, tumor progression, and up-regulation of metalloproteinases, the sequence GXXPG is required within the enzyme to stimulate the cellular effects, overview
-
-
?
Elastin + H2O
?
-
human substrate, generation of soluble peptides by limited proteolysis
-
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, could participate in neutrophil migration
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the onset of emphysema and rheumatoid arthritis
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
G-CSF receptor + H2O
?
-
neutrophil elastase proteolytically cleaves the G-CSF receptor, G-CSFR, a transmembrane protein, in its extracellular region on neutrophils and blocks G-CSFR-mediated granulopoiesis in vitro, and growth of neutrophils and monocytes, CFU-GM, overview
-
-
?
G-CSF receptor + H2O
?
-
neutrophil elastase proteolytically cleaves the G-CSF receptor, G-CSFR, a transmembrane protein, in its extracellular region on neutrophils and blocks G-CSFR-mediated granulopoiesis in vitro, and growth of neutrophils and monocytes, CFU-GM
-
-
?
human SP-D protein + H2O
SP-D protein peptide fragments
-
-
cleavage product identification by N-terminal sequencing, overview
-
?
human SP-D protein + H2O
SP-D protein peptide fragments
-
cleavage in the lungs of the cystic fibrosis human host, but not in helathy human hosts
cleavage product identification by N-terminal sequencing, overview
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-methylcoumarin 7-amide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 7-amino-4-methylcoumarin
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-methylcoumarin 7-amide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 7-amino-4-methylcoumarin
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
mucin + H2O
?
-
proteolysis of mucin is suggested to be involved in cell damaging processes during chronic infection and inflammation of the respiratory tract
-
-
?
N-methoxy-succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxy-succinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
N-methoxy-succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxy-succinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
663987, 683043, 683056, 683536, 683810, 683956, 697329, 698394, 698834, 699427, 699737, 700570, 701184, 707673, 707710, 707735, 707913, 708387, 708691, 709357, 709363, 709472, 709493, 709989, 717334, 717895, 717904, 718423
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
specific neutrophil elastase substrate
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
highly specific synthetic substrate for neutrophil elastase
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
a fluorogenic enzyme-specific substrate
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
highly specific synthetic substrate
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Val 4-nitroanilide + H2O
N-succinyl-Ala-Ala-Val + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Val 4-nitroanilide + H2O
N-succinyl-Ala-Ala-Val + 4-nitroaniline
-
-
-
-
?
oxidized B chain of insulin + H2O
?
-
most susceptible bonds are Val12-Glu13, Val18-Cys(O3H)-19. Other bonds hydrolyzed are Ala14-Leu15, Ser9-His10 and Cys(O3H)7-Gly8
-
-
-
oxidized B chain of insulin + H2O
?
-
initial cleavage sites for proteinase 2A and 2B are the Ala14-Leu15 and Val18-Cys19 bonds. Cleavage of the Val12-Glu13 bond is a secondary event resulting from the further cleavage of the primary peptide Phe1-Ala14
-
-
-
protein C + H2O
small peptides
-
the enzyme splits protein C in vitro, and also in vivo degradation of protein C may take place
-
?
protein C + H2O
small peptides
-
the enzyme splits protein C in vitro and also in vivo degradation of protein C may take place
-
?
secretory leucoprotease inhibitor + H2O
?
-
i.e. SLPI, SLPI is cleaved and inactivated by neutrophil elastase in cystic fibrosis lungs
-
-
?
secretory leucoprotease inhibitor + H2O
?
-
i.e. SLPI, recombinant human, a neutrophil serine protease inhibitor, neutrophil elastase cleaves the protein at two sites in the NH2-terminal region and abrogate its ability to bind lipopolysaccharides and NF-kappaB consensus binding sites but not its ability to inhibit activity of the serine protease cathepsin G
-
-
?
SP-D protein + H2O
SP-D protein peptide fragments
-
-
cleavage product identification by N-terminal sequencing, overview
-
?
SP-D protein + H2O
SP-D protein peptide fragments
-
no activity in healthy lungs, but in 50% of cystic fibrosis patient lungs
cleavage product identification by N-terminal sequencing, overview
-
?
succinyl-Ala-Ala-NH-4-nitroanilide + H2O
succinyl-Ala-Ala-NH2 + 4-nitroaniline
-
-
-
-
?
succinyl-Ala-Ala-NH-4-nitroanilide + H2O
succinyl-Ala-Ala-NH2 + 4-nitroaniline
-
-
-
-
?
tert-butyloxycarbonyl-Ala-4-nitrophenyl ester + H2O
tert-butyloxycarbonyl-Ala + 4-nitrophenol
-
-
-
-
-
tert-butyloxycarbonyl-Ala-4-nitrophenyl ester + H2O
tert-butyloxycarbonyl-Ala + 4-nitrophenol
-
-
-
-
?
H2 heavy chain of inter-alpha-trypsin inhibitor + H2O
additional information
-
-
-
early cleavage products consists of heavy chain H1 linked to the light chain, known as bikunin
?
additional information
?
-
-
neutrophil elastase cleaves vascular endothelial growth factor, VEGF, to generate a VEGF fragment with altered activity. Recombinant human VEGF165 is a substrate for the enzyme. The neutrophil elastase-generated VEGF fragment shows significantly reduced binding to VEGF receptor 2 and heparin, yet retains the ability to bind to VEGF receptor 1. The VEGF fragment shows altered signaling in pulmonary artery endothelial cells compared with intact VEGF165, detailed overview. Substrate and product analysis by mass spectrometry. PDGF is also a substrate of neutrophil elastase, while TNFalpha and FGF2 are not
-
-
-
additional information
?
-
-
development of an ELISA for equine neutrophil elastase measurement in EDTA-plasma samples, method development, evaluation, and validation, overview
-
-
-
additional information
?
-
-
catalyzes the inactivation of antithrombin by a specific and limited proteinolytic cleavage
-
-
-
additional information
?
-
-
elastase in contrast to human elastase, may play a minor role in mediating tissue damage and organ failure
-
-
-
additional information
?
-
-
the enzyme may contribute to the intracellular degradation of phagocytized material, its release from activated polymorphonuclear leukocytes into extracellular spaces. The enzyme has been implicated in the pathogenesis of various diseases and is thought to be responsible for tissue damage
-
-
-
additional information
?
-
-
proteolysis of connective tissue by enzymes such as PMN-elastase is a crucial step during inflammation and metastasis
-
-
-
additional information
?
-
-
imbalance between elastase and its endogenous inhibitors may result in several pathophysiological states such as chronic obstructive pulmonary disease, asthma, emphysema, cystic fibrosis and chronic inflammatory diseases
-
-
-
additional information
?
-
-
neutrophil elastase is a key component of the body‘s inflammatory defenses, assisting the neutrophil in its migration to the site of inflammation and participating in the proteolytic degradation of invading microorganisms. In addition the enzyme is involved in tissue remodeling and wound healing. Under homeostatic conditions, the destructive effects of the enzyme are limited to the microenvironment immediately surrounding the neutrophil by endogenous proteinase inhibitors such as alpha1-proteinase inhibitor. As a consequence of chronic inflammation, however, the balance between the enzyme and alpha1-antitrypsin can be shifted in favor of the enzyme, resulting in uncontrolled tissue destruction. The enzyme has been implicated in the promotion or exacerbation of a number of diseases including pancreatitis acute respiratory distress syndrome, rheumatoid arthritis, atherosclerosis, pulmonary emphysema and cystic fibrosis
-
-
-
additional information
?
-
-
the enzyme may be involved in a number of important disease states. Including the pulmonary emphysema associated with a hereditary deficiency of alpha1-proteinase inhibitor
-
-
-
additional information
?
-
-
leukocyte elastase induces keratinocyte proliferation by epidermal growth factor receptor activation
-
-
-
additional information
?
-
-
neutrophil elastase induces MUC5AC mucin production in human airway epithelial cells via a cascade involving protein kinase C, reactive oxygen species, and TNF-alpha-converting enzyme
-
-
-
additional information
?
-
-
release of leukocyte elastase and cathepsin G from neutrophils specifically down-regulates the responsiveness of neutrophils to C5a. Elastase and cathepsin play an important role in the down-regulation of acute inflammation
-
-
-
additional information
?
-
-
a massive release of PMN-elastase from neutrophils occurs during surgical procedures, effects on the enzyme of cholecystectomy via laparoscopic or open surgical operation of patients with gallbladder cholethiasis, overview
-
-
-
additional information
?
-
-
inflammatory lung secretions inhibit dendritic cell maturation and function via neutrophil elastase, neutrophil elastase downregulated the expression of CD40, CD80, and CD86, but of not major histocompatibility complex II, on dendritic cells and inhibited LPS-induced dendritic cell maturation, and the the antigen-presenting ability of muring dendritic cells, overview
-
-
-
additional information
?
-
-
neutrophil elastase converts human immature dendritic cells into transforming growth factor-beta1-secreting cells and reduces allostimulatory ability, elastase induces IkappaBalpha degradation in dendritic cells, overview
-
-
-
additional information
?
-
-
neutrophil elastase, a component of the innate host defense system, is bactericidal for Gram-negative bacteria and degrades bacterial virulence factors, resistance of Pseudomonas aeruginosa to the bactericidal effect of neutrophil elastase, as well as this organism’s ability to sense this enzyme’s presence and downregulate the synthesis of a pathogen-associated molecular pattern, may be the key factors in allowing Pseudomonas aeruginosa to colonize the lungs, overview
-
-
-
additional information
?
-
the enzyme digests microbes after phagocytosis in polymorphonuclear neutrophil primary granules, which fuse with neutrophil phagolysosomes, and also acts extracellularly at sites of inflammation, overview, mutations in the human neutrophil elastase gene cause cyclic and congenital neutropenia leading to an immunodeficiency characterized by decreased or oscillating levels of neutrophils in the blood
-
-
-
additional information
?
-
-
product determination by mass spectrometry, overview, no activity with elastin exon 24-derived peptide VGVAPGV
-
-
-
additional information
?
-
structure-function relationships, overview
-
-
-
additional information
?
-
-
human neutrophil elastase induces interleukin-8 release from HUVEC cells
-
-
-
additional information
?
-
-
neutrophil elastase possesses potent microbicidal activity, and is speculated to assist with phagocytosis of pathogens by activated neutrophils, moreover, neutrophil elastase can indirectly help the host eradication of pathogens by upregulating the expression of potent antiprotease/antimicrobial agents such as elafin, secretory leukocyte protease inhibitor, and human beta defensin-2
-
-
-
additional information
?
-
-
neutrophil elastase reduces secretion of secretory leukoproteinase inhibitor by lung epithelial cells
-
-
-
additional information
?
-
-
does not cleave N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
-
-
additional information
?
-
-
leukocyte elastase induces binding activity of NF-kappaB to lung epithelial cells, and induces phosphorylation of p53 on Ser46 and alters its localization. And leukocyte elastase induces expression of PUMA, a p53-upregulated modulator of apoptosis
-
-
-
additional information
?
-
-
neutrophil elastase does not cleave the N-terminal domains and does not disarm either PAR-1 or PAR-2
-
-
-
additional information
?
-
-
neutrophil elastase induces NF-kappaB activation by p65 in airway smooth muscle, which leads to induction of TGF-beta1. Neutrophil elastase suppresses NF-kappaB response gene IL-8/CXCL8 release and mRNA expression in airway smooth muscle cells at the transcription level mediated by induction of NF-kappaB repressing factor, NRF. In A549 and Beas-2B cells, neutrophil elastase only stimulates NF-kappaB activation by p65 and IL-8/CXCL8 induction, but not NRF, overview
-
-
-
additional information
?
-
-
neutrophil elastase interacts with phosphonoformate immunoassociated protein 5, i.e. PFAAP5 or N4BP2L2, with potential participation in a feedback circuit in which neutrophil elastase regulates its own transcription
-
-
-
additional information
?
-
-
nano-LC tandem mass spectrometry neutrophil elastase cleavage site identification, overview
-
-
-
additional information
?
-
-
histone H3 is not degraded by neutrophil elastase
-
-
-
additional information
?
-
-
high concentrations of neutrophil elastase inhibit nuclear decondensation. This autoinhibition can be caused by neutrophil elastase autodegradation
-
-
-
additional information
?
-
-
substrates with a hydrophobic side chain at P1 are efficiently cleaved and P1-valine is preferred over an alanine or a phenylalanine
-
-
-
additional information
?
-
-
the enzyme prefers L-Val in the P1 position but also cleaves substrates with L-Ile relatively efficiently and does not cleave after aromatic amino acids
-
-
-
additional information
?
-
-
no activity with succiny-Ala-Ala-Pro-Phe-4-nitroanilide, succiny-Leu-Leu-Val-Tyr-4-nitroanilide, succiny-Ala-Ala-Pro-Leu-4-nitroanilide, succiny-Val-Leu-Gly-Arg-4-nitroanilide, Z-Gly-Pro-Arg-4-nitroanilide, acetyl-Tyr-Val-Ala-Asp-4-nitroanilide, acetyl-Val-Glu-Ile-Asp-4-nitroanilide, and acetyl-Ile-Glu-Pro-Asp-4-nitroanilide
-
-
-
additional information
?
-
-
neutrophil elastase influences the proliferation and differentiation of primary early myeloid cells expressing low levels of PML-retioic acid receptor alpha
-
-
-
additional information
?
-
-
involvement of neutrophil elastase in leukotriene B4-induced neutrophil transmigration in vivo, specific NE inhibitor suppresses neutrophil migration through IL-1beta-stimulated cremasteric venules at the level of the basement membrane
-
-
-
additional information
?
-
-
the enzyme digests microbes after phagocytosis in polymorphonuclear neutrophils, as well as extracellularly, but causes tissue damage and inflammation in the latter case, serine protease inhibitor 6-deficient Spi6 KO mice have increased neutrophil immunity to Pseudomonas aeruginosa, enzyme inhibitor Spi6 protects the cells from self-inflicted damage, the enzyme protects against Pseudomonas aeruginosa infection, overview
-
-
-
additional information
?
-
-
neutrophil elastase is required for maximal intracellular killing of Pseudomonas aeruginosa by neutrophils
-
-
-
additional information
?
-
-
neutrophil elastase cleaves vascular endothelial growth factor, VEGF, to generate a VEGF fragment with altered activity. Recombinant human VEGF165 is a substrate for the enzyme. The neutrophil elastase-generated VEGF fragment, VEGFf, and the wild-type VEGF both activate Akt, and VEGFf appears to be more effective. Substrate and product analysis by mass spectrometry
-
-
-
additional information
?
-
-
the enzyme digests microbes after phagocytosis in polymorphonuclear neutrophils, as well as extracellularly, but causes tissue damage and inflammation in the latter case, serine protease inhibitor 6-deficient Spi6 KO mice have increased neutrophil immunity to Pseudomonas aeruginosa, enzyme inhibitor Spi6 protects the cells from self-inflicted damage, the enzyme protects against Pseudomonas aeruginosa infection, overview
-
-
-
additional information
?
-
-
neutrophils and the elastase thereof play a role in the progression of gut barrier dysfunction during acut alveolar hypoxia, inhibition of neutrophil elastase attenuates gut mucosal injury evoked by acute alveolar hypoxia in rabbits, overview
-
-
-
additional information
?
-
-
elastase in contrast to human elastase, may play a minor role in mediating tissue damage and organ failure
-
-
-
additional information
?
-
-
neutrophil elastase cleaves vascular endothelial growth factor, VEGF, to generate a VEGF fragment with altered activity. Recombinant human VEGF165 is a substrate for the enzyme. The neutrophil elastase-generated VEGF fragment shows significantly reduced binding to VEGF receptor 2 and heparin, yet retains the ability to bind to VEGF receptor 1. Substrate and product analysis by mass spectrometry
-
-
-
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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
alpha1-PI + H2O
?
-
important antiprotease of the lung, enzyme reduces the lungs’ primary protection against proteolysis
-
-
?
annexin 1 + H2O
?
-
annexin 1 is externalized and truncated upon adhesion of polymorphonuclear leukocytes to endothelial cells, annexin 1 participates in regulating leukocyte emigration into inflamed tissue through N-terminal peptides generated at inflammatory sites, overview
-
-
?
BP180/type XVII collagen + H2O
peptide p561 + peptide p506
-
neutrophil elastase degrades recombinant mouse BP180 within the immunodominant extracellular domain at amino acid positions 506 and 561
-
-
?
corticosteroid-binding globulin + H2O
?
-
cleavage by neutrophil elastase destroys ligand binding capacity and supposedly liberates cortisol at sites of inflammation. Enzyme activity on wild-type and mutant CBG serpin recombinantly produced by 293-EBNA cells, overview. CBG mutant G335V is more sensitive for elastase cleavage, while CBG mutant T342A is more resistant to elastase cleavage
-
-
?
Factor VIIIa + H2O
?
-
neutrophil elastase inactivates factor VIIIa. The enzyme proteolyses the heavy chain of factor VIIIa into two terminal products, A11-358 and A2375-708, by limited proteolysis at Val358, Val374, and Val708
-
-
?
G-CSF receptor + H2O
?
-
neutrophil elastase proteolytically cleaves the G-CSF receptor, G-CSFR, a transmembrane protein, in its extracellular region on neutrophils and blocks G-CSFR-mediated granulopoiesis in vitro, and growth of neutrophils and monocytes, CFU-GM, overview
-
-
?
human SP-D protein + H2O
SP-D protein peptide fragments
-
cleavage in the lungs of the cystic fibrosis human host, but not in helathy human hosts
cleavage product identification by N-terminal sequencing, overview
-
?
IgA + H2O
?
-
involved in the regulation of inflammation by a feedback mechanism, elastase treated IgA preparations are unable to induce oxidative burst of polymorphonuclear leukocytes
protein cleaved in the hinge region
-
?
IgG + H2O
?
-
involved in the regulation of inflammation by a feedback mechanism, elastase treated IgG preparations are unable to induce oxidative burst of polymorphonuclear leukocytes
protein cleaved in the hinge region
-
?
interleukin-36 receptor antagonist + H2O
activated interleukin-36 receptor antagonist V2 + ?
-
the enzyme cleaves 9 amino acids upstream of the A-X-D consensus of interleukin-36 receptor antagonist
-
-
?
IpaB protein + H2O
?
-
neutrophil elastase cleaves IpaB protein after alanine, valine, isoleucine, or threonine residues
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Va + 4-nitroanilide
-
-
-
-
?
mucin + H2O
?
-
proteolysis of mucin is suggested to be involved in cell damaging processes during chronic infection and inflammation of the respiratory tract
-
-
?
oxytalan fibre + H2O
?
-
the elastase degrades the interfibrillar substances in the periodontal ligament and exposed individual collagen fibrils but not the collagen fibers of the transverse sections of rat mandibular first molars
-
-
?
procarboxypeptidase R + H2O
carboxypeptidase R + ?
-
generation of activated carboxypeptidase R from procarboxypeptidase R by elastase from activated neutrophils at the site of inflammation should contribute to the suppression of excessive inflammation and any abnormality in this mechanism can induce serious hyper-inflammation such as seen in multiple organ failure
-
-
?
protein C + H2O
small peptides
-
the enzyme splits protein C in vitro and also in vivo degradation of protein C may take place
-
?
proteinase-activated receptor 2 N-terminus + H2O
GPNSKGRSLIGRLDTPPPITGKGAPVEPGFSVDEFSAS + VLTGKLTTVFLP
-
-
-
-
?
secretory leucoprotease inhibitor + H2O
?
-
i.e. SLPI, SLPI is cleaved and inactivated by neutrophil elastase in cystic fibrosis lungs
-
-
?
SLPI + H2O
?
-
important antiprotease of the lung, enzyme reduces the lungs’ primary protection against proteolysis
-
-
?
SP-D protein + H2O
SP-D protein peptide fragments
-
no activity in healthy lungs, but in 50% of cystic fibrosis patient lungs
cleavage product identification by N-terminal sequencing, overview
-
?
elafin + H2O
?
-
elafin is cleaved by its cognate enzyme neutrophil elastase, neutrophil elastase-mediated cleavage of elafin abolishes the capacity of the inhibitor to cross-link to fibronectin by transglutamination, neutrophil elastase-mediated cleavages of elafin at Val5-Lys-6 and Val9-Ser10 peptide bonds only occur with 2x excess of neutrophil elastase, a partial cleavage of the inhibitor is identified at the scissile peptide bond Ala24-Met25
-
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
-
697329, 697826, 698394, 717369, 717904, 718421, 731106, 731124, 731591, 731788, 731991, 732294, 732438, 732564, 732600, 732758, 732907, 754758
-
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells also might be damaged, involved in the onset of emphysema and rheumatoid arthritis
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, enzyme is assumed to play a key role in the gradual decrease of lung function during cystic fibrosis
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the onset of emphysema, acute respiratory distress syndrome, and rheumatoid arthritis
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
generation of soluble peptides by limited proteolysis, elastin-derived peptides play roles in cell migration, differentiation, proliferation, chemotaxis, tumor progression, and up-regulation of metalloproteinases, the sequence GXXPG is required within the enzyme to stimulate the cellular effects, overview
-
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, could participate in neutrophil migration
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the onset of emphysema and rheumatoid arthritis
protein cleaved at at least one location
-
?
Elastin + H2O
?
-
involved in lung defense against bacterial infection, due to the ability of the enzyme to cleave cell surface proteins, body cells might also be damaged, involved in the etiology of emphysema, rheumatoid arthritis, psoriasis, and adult respiratory distress syndrome
protein cleaved at at least one location
-
?
additional information
?
-
-
catalyzes the inactivation of antithrombin by a specific and limited proteinolytic cleavage
-
-
-
additional information
?
-
-
elastase in contrast to human elastase, may play a minor role in mediating tissue damage and organ failure
-
-
-
additional information
?
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the enzyme may contribute to the intracellular degradation of phagocytized material, its release from activated polymorphonuclear leukocytes into extracellular spaces. The enzyme has been implicated in the pathogenesis of various diseases and is thought to be responsible for tissue damage
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additional information
?
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proteolysis of connective tissue by enzymes such as PMN-elastase is a crucial step during inflammation and metastasis
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additional information
?
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imbalance between elastase and its endogenous inhibitors may result in several pathophysiological states such as chronic obstructive pulmonary disease, asthma, emphysema, cystic fibrosis and chronic inflammatory diseases
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additional information
?
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neutrophil elastase is a key component of the body‘s inflammatory defenses, assisting the neutrophil in its migration to the site of inflammation and participating in the proteolytic degradation of invading microorganisms. In addition the enzyme is involved in tissue remodeling and wound healing. Under homeostatic conditions, the destructive effects of the enzyme are limited to the microenvironment immediately surrounding the neutrophil by endogenous proteinase inhibitors such as alpha1-proteinase inhibitor. As a consequence of chronic inflammation, however, the balance between the enzyme and alpha1-antitrypsin can be shifted in favor of the enzyme, resulting in uncontrolled tissue destruction. The enzyme has been implicated in the promotion or exacerbation of a number of diseases including pancreatitis acute respiratory distress syndrome, rheumatoid arthritis, atherosclerosis, pulmonary emphysema and cystic fibrosis
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additional information
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the enzyme may be involved in a number of important disease states. Including the pulmonary emphysema associated with a hereditary deficiency of alpha1-proteinase inhibitor
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additional information
?
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leukocyte elastase induces keratinocyte proliferation by epidermal growth factor receptor activation
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additional information
?
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neutrophil elastase induces MUC5AC mucin production in human airway epithelial cells via a cascade involving protein kinase C, reactive oxygen species, and TNF-alpha-converting enzyme
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additional information
?
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-
release of leukocyte elastase and cathepsin G from neutrophils specifically down-regulates the responsiveness of neutrophils to C5a. Elastase and cathepsin play an important role in the down-regulation of acute inflammation
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additional information
?
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a massive release of PMN-elastase from neutrophils occurs during surgical procedures, effects on the enzyme of cholecystectomy via laparoscopic or open surgical operation of patients with gallbladder cholethiasis, overview
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additional information
?
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inflammatory lung secretions inhibit dendritic cell maturation and function via neutrophil elastase, neutrophil elastase downregulated the expression of CD40, CD80, and CD86, but of not major histocompatibility complex II, on dendritic cells and inhibited LPS-induced dendritic cell maturation, and the the antigen-presenting ability of muring dendritic cells, overview
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-
-
additional information
?
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-
neutrophil elastase converts human immature dendritic cells into transforming growth factor-beta1-secreting cells and reduces allostimulatory ability, elastase induces IkappaBalpha degradation in dendritic cells, overview
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additional information
?
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-
neutrophil elastase, a component of the innate host defense system, is bactericidal for Gram-negative bacteria and degrades bacterial virulence factors, resistance of Pseudomonas aeruginosa to the bactericidal effect of neutrophil elastase, as well as this organism’s ability to sense this enzyme’s presence and downregulate the synthesis of a pathogen-associated molecular pattern, may be the key factors in allowing Pseudomonas aeruginosa to colonize the lungs, overview
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additional information
?
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the enzyme digests microbes after phagocytosis in polymorphonuclear neutrophil primary granules, which fuse with neutrophil phagolysosomes, and also acts extracellularly at sites of inflammation, overview, mutations in the human neutrophil elastase gene cause cyclic and congenital neutropenia leading to an immunodeficiency characterized by decreased or oscillating levels of neutrophils in the blood
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additional information
?
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human neutrophil elastase induces interleukin-8 release from HUVEC cells
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additional information
?
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neutrophil elastase possesses potent microbicidal activity, and is speculated to assist with phagocytosis of pathogens by activated neutrophils, moreover, neutrophil elastase can indirectly help the host eradication of pathogens by upregulating the expression of potent antiprotease/antimicrobial agents such as elafin, secretory leukocyte protease inhibitor, and human beta defensin-2
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-
additional information
?
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-
neutrophil elastase reduces secretion of secretory leukoproteinase inhibitor by lung epithelial cells
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-
-
additional information
?
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-
leukocyte elastase induces binding activity of NF-kappaB to lung epithelial cells, and induces phosphorylation of p53 on Ser46 and alters its localization. And leukocyte elastase induces expression of PUMA, a p53-upregulated modulator of apoptosis
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additional information
?
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neutrophil elastase does not cleave the N-terminal domains and does not disarm either PAR-1 or PAR-2
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additional information
?
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neutrophil elastase induces NF-kappaB activation by p65 in airway smooth muscle, which leads to induction of TGF-beta1. Neutrophil elastase suppresses NF-kappaB response gene IL-8/CXCL8 release and mRNA expression in airway smooth muscle cells at the transcription level mediated by induction of NF-kappaB repressing factor, NRF. In A549 and Beas-2B cells, neutrophil elastase only stimulates NF-kappaB activation by p65 and IL-8/CXCL8 induction, but not NRF, overview
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additional information
?
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neutrophil elastase interacts with phosphonoformate immunoassociated protein 5, i.e. PFAAP5 or N4BP2L2, with potential participation in a feedback circuit in which neutrophil elastase regulates its own transcription
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additional information
?
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histone H3 is not degraded by neutrophil elastase
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additional information
?
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the enzyme prefers L-Val in the P1 position but also cleaves substrates with L-Ile relatively efficiently and does not cleave after aromatic amino acids
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additional information
?
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neutrophil elastase influences the proliferation and differentiation of primary early myeloid cells expressing low levels of PML-retioic acid receptor alpha
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additional information
?
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involvement of neutrophil elastase in leukotriene B4-induced neutrophil transmigration in vivo, specific NE inhibitor suppresses neutrophil migration through IL-1beta-stimulated cremasteric venules at the level of the basement membrane
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additional information
?
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the enzyme digests microbes after phagocytosis in polymorphonuclear neutrophils, as well as extracellularly, but causes tissue damage and inflammation in the latter case, serine protease inhibitor 6-deficient Spi6 KO mice have increased neutrophil immunity to Pseudomonas aeruginosa, enzyme inhibitor Spi6 protects the cells from self-inflicted damage, the enzyme protects against Pseudomonas aeruginosa infection, overview
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additional information
?
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neutrophil elastase is required for maximal intracellular killing of Pseudomonas aeruginosa by neutrophils
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additional information
?
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the enzyme digests microbes after phagocytosis in polymorphonuclear neutrophils, as well as extracellularly, but causes tissue damage and inflammation in the latter case, serine protease inhibitor 6-deficient Spi6 KO mice have increased neutrophil immunity to Pseudomonas aeruginosa, enzyme inhibitor Spi6 protects the cells from self-inflicted damage, the enzyme protects against Pseudomonas aeruginosa infection, overview
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-
additional information
?
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neutrophils and the elastase thereof play a role in the progression of gut barrier dysfunction during acut alveolar hypoxia, inhibition of neutrophil elastase attenuates gut mucosal injury evoked by acute alveolar hypoxia in rabbits, overview
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additional information
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elastase in contrast to human elastase, may play a minor role in mediating tissue damage and organ failure
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Na+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
((6R,7S)-2-{[(2S)-2-(dihydroxymethyl)pyrrolidin-1-yl]carbonyl}-7-methoxy-5,5-dioxido-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-en-3-yl)methyl acetate
-
-
(1-{1-Methyl-2-oxo-2-[2-(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidin-1-yl]-ethylcarbamoyl}-ethyl)-carbamic acid benzyl ester
-
-
(1-{2-[1-(4,5-Dihydro-oxazole-2-carbonyl)-2-methyl-propylcarbamoyl]-pyrrolidine-1-carbonyl}-2-methyl-propyl)-carbamic acid benzyl ester
-
(
(1-{2-[1-(Benzooxazol-2-yl-hydroxy-methyl)-2-methyl-propylcarbamoyl]-pyrrolidine-1-carbonyl}-2-methyl-propyl)-carbamic acid benzyl ester
-
-
(1-{2-[1-(Benzooxazole-2-carbonyl)-2-methyl-propylcarbamoyl]-pyrrolidine-1-carbonyl}-2-methyl-propyl)-carbamic acid benzyl ester
-
-
(1-{2-[2-(3,3-Difluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidin-1-yl]-1-methyl-2-oxo-ethylcarbamoyl}-ethyl)-carbamic acid benzyl ester
-
-
(1-{[1-(2-tert-Butoxycarbonylamino-3-methyl-butyryl)-pyrrolidine-2-carbonyl]-amino}-2-methyl-propyl)-phosphonic acid diphenyl ester
-
-
(2-(3,5-bis-trifluoromethyl-phenyl)-6-oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(2-(3,5-difluoro-phenyl)-6-oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(2-(4-amino-phenyl)-6-oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(2-(4-chloro-phenyl)-6-oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(2-(4-formylamino-phenyl)-6-oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(2-(4-methoxy-phenyl)-6-oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(2-(4-nitro-phenyl)-6-oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(2-cyclohexyl-6-oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(2-isopropyl-6-oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(2S)-1-({(6R,7S)-3-[(acetyloxy)methyl]-7-methoxy-5,5-dioxido-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-en-2-yl}carbonyl)pyrrolidine-2-carboxylic acid
-
-
(3beta,5alpha,8alpha,22E)-ergosta-6,22-diene-3-ol-5,8-peroxide 3-O-beta-D-glucoside
-
-
(3R)-1-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-3-carboxylic acid
-
-
(3S)-1-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-3-carboxylic acid
-
-
(4-tert-butyl-1,1-dioxido-3-oxo-1,2-benzisothiazol-2(3H)-yl)methyl 2,6-dichlorobenzoate
-
-
(5-Benzyloxycarbonylamino-1-{2-methyl-1-[2-(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidine-1-carbonyl]-propylcarbamoyl}-pentyl)-carbamic acid benzyl ester
-
-
(6-oxo-2-(4-fluorophenyl)-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(6-oxo-2-phenyl-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(6-oxo-2-pyridin-3-yl-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(6-oxo-2-thiophen-2-yl-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(6-oxo-2-[4-(2,2,2-trifluoro-acetylamino)-phenyl]-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-1,6-dihydro-pyrimidin-5-yl)-carbamic acid benzyl ester
-
-
(6R,7S)-3-[(acetyloxy)methyl]-7-methoxy-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid 5,5-dioxide
-
-
(E)-3-(3-(3,7-dimethylocta-2,6-dienyl)-2,4-dihydroxyphenyl)-3,5,7-trihydroxy-chroman-4-one
-
competitive inhibitor
-
(E)-6-O-p-coumaroyl scandoside methyl ester
-
an iridoid glycoside isolated from the methanolic extract of Hedyotis diffusa, usage of air-dried whole plant
(E)-6-O-p-feruloyl scandoside methyl ester
-
an iridoid glycoside isolated from the methanolic extract of Hedyotis diffusa, usage of air-dried whole plant
(E)-6-O-p-methoxycinnamoyl scandoside methyl ester
-
an iridoid glycoside isolated from the methanolic extract of Hedyotis diffusa, usage of air-dried whole plant. Molecular docking simulation and structural model for the inhibition of human neutrophil elastase, overview
(R)-3-phenyl-2-(1,1,3-trioxo-1,3-dihydro-1lambda6-1,2-benzisothiazol-2-yl-methanesulfonylamino)-propionic acid methyl ester
-
-
(S)-1-[(S)-2-(4-methoxybenzamido)-3-methylbutyryl]-N-[(S)-2-methyl-1-(trifluoroacetyl)propyl]pyrrolidine-2-carboxamide
-
-
(S)-3-phenyl-2-(1,1,3-trioxo-1,3-dihydro-1lambda6-1,2-benzisothiazol-2-yl-methanesulfonylamino)-propionic acid methyl ester
-
-
(Z)-6-O-p-coumaroyl scandoside methyl ester
-
an iridoid glycoside isolated from the methanolic extract of Hedyotis diffusa, usage of air-dried whole plant
(Z)-6-O-p-methoxycinnamoyl scandoside methyl ester
-
an iridoid glycoside isolated from the methanolic extract of Hedyotis diffusa, usage of air-dried whole plant
1(6H)-Pyrimidineacetamide, 2-(4-aminophenyl)-5-[(methylsulfonyl)amino]-6-oxo-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
1(6H)-Pyrimidineacetamide, 2-(4-fluorophenyl)-5-(methylamino)-6-oxo-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
1(6H)-Pyrimidineacetamide, 5-(ethylamino)-6-oxo-2-(2-thienyl)-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
1(6H)-Pyrimidineacetamide, 5-(formylamino)-6-oxo-2-(2-thienyl)-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
1(6H)-Pyrimidineacetamide, 5-amino-2-(4-fluorophenyl)-N-[2-methyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)propyl]-6-oxo-
-
-
1(6H)-Pyrimidineacetamide, 5-amino-N-[2-methyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)propyl]-6-oxo-2-(2-thienyl)-
-
-
1(6H)-Pyrimidineacetamide, 5-[[(cyclohexylamino)sulfonyl]amino]-2-(4-fluorophenyl)-N-[2-methyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)propyl]-6-oxo-
-
-
1(6H)-Pyrimidineacetamide, 6-oxo-2-phenyl-5-[(trifluoroacetyl)amino]-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
the inhibitor causes rapid, time-dependent, irreversible loss of enzymatic activity
1-(2-((1-methyl-1H-imidazol-2-ylthio)methyl)phenyl)-3,3-diethylazetidine-2,4-dione
-
-
1-(2-((5-phenyl-1,3,4-oxadiazol-2-ylthio)methyl)phenyl)-3,3-diethylazetidine-2,4-dione
-
-
1-(2-((benzo[d]oxazol-2-ylthio)methyl)phenyl)-3,3-diethylazetidine-2,4-dione
-
-
1-(2-((benzo[d]thiazol-2-ylthio)methyl)phenyl)-3,3-diethylazetidine-2,4-dione
-
-
1-(2-Acetylamino-propionyl)-pyrrolidine-2-carboxylic acid (3-chloro-1-methyl-2-oxo-propyl)-amide
-
-
1-(4-((5-phenyl-1,3,4-oxadiazol-2-ylthio)methyl)phenyl)-3,3-diethylazetidine-2,4-dione
-
-
1-(4-((benzo[d]oxazol-2-ylthio)methyl)phenyl)-3,3-diethylazetidine-2,4-dione
-
-
1-(4-((benzo[d]thiazol-2-ylthio)methyl)phenyl)-3,3-diethylazetidine-2,4-dione
-
-
1-(6-((benzo[d]thiazol-2-ylthio)methyl)pyridin-3-yl)-3,3-diethylazetidine-2,4-dione
-
-
1-[2-(2-Acetylamino-propionylamino)-propionyl]-pyrrolidine-2-carboxylic acid (3-chloro-1-isopropyl-2-oxo-propyl)-amide
-
-
1-[2-(2-Acetylamino-propionylamino)-propionyl]-pyrrolidine-2-carboxylic acid (3-chloro-1-methyl-2-oxo-propyl)-amide
-
-
1-[2-(4-Benzenesulfonylaminocarbonyl-benzoylamino)-3-methyl-butyryl]-pyrrolidine-2-carboxylic acid (3,3-difluoro-1-isopropyl-2-oxo-3-phenethylcarbamoyl-propyl)-amide
-
-
1-[3-(5-cyclobutyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
-
-
1-[3-(5-cyclopropyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
-
-
1-[3-(5-ethyl-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
-
-
1-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
-
-
1-[3-(5-methyl-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
-
-
1-[3-(7-methoxy-4-oxo-5-propyl-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
-
-
1-[3-[7-methoxy-4-oxo-5-(propan-2-yl)-4H-3,1-benzoxazin-2-yl]pyridin-2-yl]piperidine-4-carboxylic acid
-
-
1-{2-[4-(4-Bromo-benzenesulfonylaminocarbonyl)-benzoylamino]-3-methyl-butyryl}-pyrrolidine-2-carboxylic acid (3,3,3-trifluoro-1-isopropyl-2-oxo-propyl)-amide
-
-
1-{2-[4-(4-Chloro-benzenesulfonylaminocarbonyl)-benzoylamino]-3-methyl-butyryl}-pyrrolidine-2-carboxylic acid (1-isopropyl-2,3-dioxo-heptyl)-amide
-
-
1-{2-[4-(4-Chloro-benzenesulfonylaminocarbonyl)-benzoylamino]-3-methyl-butyryl}-pyrrolidine-2-carboxylic acid (3,3,3-trifluoro-1-isopropyl-2-oxo-propyl)-amide
-
-
1-{3-Methyl-2-[(naphthalene-2-carbonyl)-amino]-butyryl}-pyrrolidine-2-carboxylic acid (1-isopropyl-2,3-dioxo-heptyl)-amide
-
-
1-{[({2-[3-(trifluoromethyl)phenyl]ethyl}amino)carbonyl]oxy}pyrrolidine-2,5-dione
-
-
2,2,2-trifluoroethyl 1-[(3-methoxyphenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
2,2-Dimethyl-propionic acid 4-[2-(2,2-dihydroxy-ethylcarbamoyl)-benzenesulfonylamino]-phenyl ester
-
-
2,2-Dimethyl-propionic acid 4-[4-(2,2-dimethyl-propionyloxy)-benzoyl]-phenyl ester
-
-
2,3-dihydro-6-[3-(2-hydroxymethyl)-phenyl-2-propenyl]5-benzofuranol
-
the synthetic inhibitor may provide a new and useful therapeutic for the treatment of diseases characterized by polymorphonuclear elastase involvement
2-(2-[4-[2-(dimethylamino)ethyl]piperazin-1-yl]pyridin-3-yl)-5-ethyl-7-methoxy-4H-3,1-benzoxazin-4-one
-
-
2-(2-[[2-(dimethylamino)ethyl](methyl)amino]pyridin-3-yl)-5-methyl-4H-3,1-benzoxazin-4-one
-
-
2-(2-[[2-(dimethylamino)ethyl]amino]pyridin-3-yl)-5-methyl-4H-3,1-benzoxazin-4-one
-
-
2-(3,3,3-Trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidine-1-carboxylic acid benzyl ester
-
-
2-(4-(3,3-diethyl-2,4-dioxoazetidin-1-yl)benzylthio)benzo[d ]-oxazole-6-carboxylic acid
-
-
2-(4-Chloro-benzenesulfonylamino)-5,5-dihydroxy-pentanoic acid (2-isopropylamino-5-methyl-4-oxo-4H-benzo[d][1,3]oxazin-7-yl)-amide
-
-
2-(4-Dihydroxymethyl-phenoxy)-3,3-diethyl-4-oxo-azetidine-1-carboxylic acid 4-methyl-benzylamide
-
-
2-(5-amino-6-oxo-2-thien-2-ylpyrimidin-1(6H)-yl)-N-(3,3,3-trifluoro-1-isopropyl-2-oxopropyl)acetamide
-
-
2-(thiophen-2-ylcarbonylthio)-N-(2-oxo-2,3,4,5-tetrahydrothiophen-3-yl)propionamide
-
reversible, slow-binding, fully competitive
2-Acetylamino-N-[1-(3-chloro-1-methyl-2-oxo-propylcarbamoyl)-ethyl]-propionamide
-
-
2-Acetylamino-N-[2-(2-{2-[(2-chloro-acetyl)-isopropyl-amino]-acetyl}-pyrrolidin-1-yl)-1-methyl-2-oxo-ethyl]-propionamide
-
-
2-Acetylamino-N-{1-[1-(3-chloro-1-methyl-2-oxo-propylcarbamoyl)-ethylcarbamoyl]-ethyl}-propionamide
-
-
2-hydroxyethyl (4R)-4-[4-cyanophenyl-6-methyl-2-oxo-1-[3-(trifluoromethyl)phenyl]]-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
-
2-[2-(4-butylpiperazin-1-yl)pyridin-3-yl]-5-ethyl-7-methoxy-4H-3,1-benzoxazin-4-one
-
-
2-[2-(4-cyclopentylpiperazin-1-yl)pyridin-3-yl]-5-ethyl-7-methoxy-4H-3,1-benzoxazin-4-one
-
-
2-[2-(4-fluorophenyl)-6-oxo-5-[(cyclohexylsulfamoyl)-amino]-1,6-dihydro-1-pyrimidinyl]-N-(3,3,3-trifluoro-1-isopropyl-2-oxopropyl)acetamide
-
-
2-[2-[4-(cyclopropylmethyl)piperazin-1-yl]pyridin-3-yl]-5-ethyl-7-methoxy-4H-3,1-benzoxazin-4-one
-
-
2-[4-(2,2-Dihydroxy-ethyl)-phenoxy]-3,3-diethyl-4-oxo-azetidine-1-carboxylic acid (1-benzo[1,3]dioxol-5-yl-butyl)-amide
-
-
2-[4-(2,2-Dihydroxy-ethyl)-phenoxy]-3,3-diethyl-4-oxo-azetidine-1-carboxylic acid (1-p-tolyl-butyl)-amide
-
-
2-[4-(2,2-Dihydroxy-ethyl)-phenoxy]-3,3-diethyl-4-oxo-azetidine-1-carboxylic acid 4-methyl-benzylamide
-
-
2-[5-amino-2-(3,5-difluorophenyl)-6-oxopyrimidin-1(6H)-yl]-N-(3,3,3-trifluoro-1-isopropyl-2-oxopropyl)acetamide
-
-
2-[5-amino-6-oxo-2-(2-thienyl)-1,6-dihydro-1-pyrimidinyl]-N-(3,3,3-trifluoro-1-isopropyl-2-oxopropyl)acetamide
-
-
2-[5-amino-6-oxo-2-(4-fluorophenyl)-1,6-dihydro-1-pyrimidinyl]-N-[2-methyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)propyl]acetamide
-
-
2-[5-[(benzyloxycarbonyl)amino]-6-oxo-2-(2-thienyl)-1,6-dihydro-1-pyrimidinyl]-N-(3,3,3-trifluoro-1-isopropyl-2-oxopropyl)acetamide
-
-
3-acetoxymethyl-7-[S]-methoxy-8-oxo-5-thia-1-aza-6[R]-bicyclo[4.2.0]oct-2-ene-2-(2-(S)-carboxypyrrolidine-carboxamide)-5,5-dioxide
-
L-658,758, cephalosporin-based anti-elastase
3-[(1-{2-[2-(3-Methoxycarbonyl-propionylamino)-propionylamino]-propionyl}-pyrrolidine-2-carbonyl)-amino]-4-methyl-2-oxo-pentanoic acid methyl ester
-
-
3-[2-(2-Benzyloxycarbonylamino-propionylamino)-propionylamino]-2-oxo-pentanoic acid benzyl ester
-
-
3-[4-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperazin-1-yl]propanenitrile
-
-
3-{[1-(2-Benzyloxycarbonylamino-3-methyl-butyryl)-pyrrolidine-2-carbonyl]-amino}-4-methyl-2-oxo-pentanoic acid ethyl ester
-
-
4-((1-(((1-(R)-(5-benzofuranyl)butyl)amino)carbonyl)-3,3-diethyl-4-oxo-2-(S)-azetidinyl)oxy)benzene acetic acid
-
the synthetic inhibitor may provide a new and useful therapeutic for the treatment of diseases characterized by polymorphonuclear elastase involvement
4-(4-bromophenylsulfonylcarbamoyl)benzoyl-L-valyl-L-proline 1 (RS)-(1-trifluoroacetyl-2-methylpropyl)amide
-
ICI 200,355, reversible, tight, and potent inhibitor, prevents the ongoing destruction of insoluble elastin by elastase, IC50: 16 nM, 4fold excess of inhibitor over enzyme causes 83% inhibition
4-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperazine-1-carboxylic acid
-
-
4-{5-(Adamantane-1-sulfonylamino)-6-oxo-6-[2-(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidin-1-yl]-hexylcarbamoyl}-butyric acid methyl ester
-
-
5-(2-Chloro-benzyl)-2-(2,2-dimethyl-propionyloxy)-5-hydroxy-5,6-dihydro-thieno[3,2-c]pyridin-5-ium; chloride
-
-
5-(4-Chloro-benzenesulfonylamino)-5-(2-isopropylamino-5-methyl-4-oxo-4H-benzo[d][1,3]oxazin-7-ylcarbamoyl)-pentyl-ammonium; chloride
-
-
5-cyclobutyl-7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-cyclobutyl-7-methoxy-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-cyclopropyl-7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-cyclopropyl-7-methoxy-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-ethyl-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-ethyl-2-[2-[4-(2-hydroxyethyl)piperazin-1-yl]pyridin-3-yl]-7-methoxy-4H-3,1-benzoxazin-4-one
-
-
5-ethyl-7-methoxy-2-(2-[4-[2-(morpholin-4-yl)ethyl]piperazin-1-yl]pyridin-3-yl)-4H-3,1-benzoxazin-4-one
-
-
5-ethyl-7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-ethyl-7-methoxy-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-ethyl-7-methoxy-2-[2-[4-(2-methoxyethyl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-ethyl-7-methoxy-2-[2-[4-(2-methylpropyl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-methyl-2-(2-phenoxy-pyridin-3-yl)-benzo[d][1,3]oxazin-4-one
-
development and synthesis, overview
5-methyl-2-(2-[[2-(morpholin-4-yl)ethyl]amino]pyridin-3-yl)-4H-3,1-benzoxazin-4-one
-
-
5-methyl-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
5-tert-butyl-7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
6-({1-[2-(2-Benzyloxycarbonylamino-propionylamino)-propionyl]-pyrrolidine-2-carbonyl}-amino)-4,4-difluoro-5-oxo-heptanoic acid methyl ester
-
-
6-amino-2-(2,2,2-trifluoro-acetylamino)-hexanoic acid [1-(4-trifluoromethyl-phenylcarbamoyl)-ethyl]-amide
-
-
7-(4-chlorophenylsulfonyl-L-glutamyl)amino-5-methyl-2-iso-propylamino-4H-3,1-benzoxazin-4-one
7-(4-chlorophenylsulfonyl-L-lysyl)amino-5-methyl-2-iso-propylamino-4H-3,1-benzoxazin-4-one
7-(dimethylamino)-5-ethyl-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
7-(dimethylamino)-5-ethyl-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
-
-
7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-5-(propan-2-yl)-4H-3,1-benzoxazin-4-one
-
-
7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-5-propyl-4H-3,1-benzoxazin-4-one
-
-
7-methoxy-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-5-(propan-2-yl)-4H-3,1-benzoxazin-4-one
-
-
7-methoxy-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-5-propyl-4H-3,1-benzoxazin-4-one
-
-
Ala15-reactive site variant of aprotinin
-
good inhibitor for proteinase 2B and weak inhibitor of proteinase 2A
-
alginate
-
weak inhibition, elastase molecule interacts with 19 uronic acid units of alginate
alpha-aminobutyric acid15-reactive site variant of aprotinin
-
good inhibitor for proteinase 2B and weak inhibitor of proteinase 2A
-
alpha-aminovaleric acid15-reactive site variant of aprotinin
-
good inhibitor for proteinase 2B and weak inhibitor of proteinase 2A
-
bis(2,3,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(2,3-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(2-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(3,4,5-trimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(3,4-dimethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-methylpropyl)phosphonate
-
-
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-methylpropyl)phosphonate
-
-
bis(4-methylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-methylpropyl)phosphonate
-
-
bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis[3-(methylsulfanyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-2-methylpropyl)phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]butyl)phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]propyl)phosphonate
-
-
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]pentyl)phosphonate
-
-
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]propyl)phosphonate
-
-
Butyric acid 3-(3-bromomethylene-6-isopropyl-5-oxo-[1,4]dioxan-2-yl)-pyrrolidin-1-yl ester
-
-
Ca2+
-
inhibition of human SP-D protein cleavage at physiological concentrations
Carbamic acid, [1,6-dihydro-6-oxo-1-[2-oxo-2-[[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]amino]ethyl]-2-(2-thienyl)-5-pyrimidinyl]-, 1-methylethyl ester
-
-
Carbamic acid, [1,6-dihydro-6-oxo-1-[2-oxo-2-[[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]amino]ethyl]-2-(2-thienyl)-5-pyrimidinyl]-, 2,2,2-trifluoroethyl ester
-
-
Carbamic acid, [1,6-dihydro-6-oxo-1-[2-oxo-2-[[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]amino]ethyl]-2-(2-thienyl)-5-pyrimidinyl]-, methyl ester
-
-
Carbamic acid, [1,6-dihydro-6-oxo-1-[2-oxo-2-[[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]amino]ethyl]-2-phenyl-5-pyrimidinyl]-, 2,2,2-trifluoroethyl ester
-
-
Carbamic acid, [2-(4-fluorophenyl)-1,6-dihydro-1-[2-[[2-methyl-1-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)propyl]amino]-2-oxoethyl]-6-oxo-5-pyrimidinyl]-, (3,5-dimethyl-4-pyridinyl)methyl ester
-
-
Carbamic acid, [2-(4-fluorophenyl)-1,6-dihydro-6-oxo-1-[2-oxo-2-[[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]amino]ethyl]-5-pyrimidinyl]-, 2-pyridinylmethyl ester
-
-
Carbamic acid, [2-(4-fluorophenyl)-1,6-dihydro-6-oxo-1-[2-oxo-2-[[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]amino]ethyl]-5-pyrimidinyl]-, 4-pyridinylmethyl ester
-
-
Carbamothioic acid, [1,6-dihydro-6-oxo-1-[2-oxo-2-[[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]amino]ethyl]-2-phenyl-5-pyrimidinyl]-, S-methyl ester
-
-
Carbamothioic acid, [2-(4-fluorophenyl)-1,6-dihydro-6-oxo-1-[2-oxo-2-[[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]amino]ethyl]-5-pyrimidinyl]-, S-methyl ester
-
-
clitocybin D
-
4-(4,6-dihydroxy-3-methoxy-3Hisoindol-1-yl)-benzoic acid, isolated from mycelia culture broth of Clitocybe aurantiaca, structure determination by NMR and mass spectroscopy
dimethyl 3,3'-[[(1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphoryl]bis(oxy)]dibenzoate
-
-
dimethyl 4,4'-[[(1-[[(benzyloxy)carbonyl]amino]-2-methylpropyl)phosphoryl]bis(oxy)]dibenzenesulfinate
-
-
dimethyl 4,4'-[[(1-[[(benzyloxy)carbonyl]amino]-2-methylpropyl)phosphoryl]bis(oxy)]dibenzoate
-
-
dimethyl 4,4'-[[(1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphoryl]bis(oxy)]dibenzoate
-
-
dimethyl 4,4'-[[(1-[[(benzyloxy)carbonyl]amino]butyl)phosphoryl]bis(oxy)]dibenzoate
-
-
dimethyl 4,4'-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)phosphoryl]bis(oxy)]dibenzoate
-
-
dimethyl 4,4'-[[(1-[[(benzyloxy)carbonyl]amino]pentyl)phosphoryl]bis(oxy)]dibenzoate
-
-
dimethyl 4,4'-[[(1-[[(benzyloxy)carbonyl]amino]propyl)phosphoryl]bis(oxy)]dibenzoate
-
-
ethyl (2S,3R)-2-[(2,2-dihydroxyethyl)sulfonyl]-3-ethyl-4-oxoazetidine-1-carboxylate
-
-
Formic acid 2-(3-{1-[2-(N'-benzyloxycarbonyl-N'-propyl-hydrazinocarbonyl)-pyrrolidine-1-carbonyl]-2-methyl-propyl}-ureido)-4-methyl-pentyl ester
-
-
Formic acid 4-methyl-2-(3-{2-methyl-1-[2-(N'-phenoxycarbonyl-N'-propyl-hydrazinocarbonyl)-pyrrolidine-1-carbonyl]-propyl}-ureido)-pentyl ester
-
-
GW447631
-
i.e. (3S,3aS,6aR)-4-(5-cyclopropylaminomethyl-pyrazine-2-carbonyl)-3-isopropyl-1-methanesulfonyl-hexahydropyrrolo[3,2-b]pyrrol-2-one hydrochloride
GW469002
-
i.e. (3S,3aS,6R)-4-[1-(2,2-dimethyl-propyl)azetidine-3-carbonyl]-3-isopropyl-1-methanesulfonyl-hexahydro-pyrrolo-[3,2-b]pyrrol-2-one
human pancreatic secretory trypsin inhibitor
-
variants optimized with respect to the affinity and specificity for human leukocyte elastase relative to trypsin, and in particular chymotrypsin
-
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1R)-3,3-difluoro-1-(1-methylethyl)-2,4-dioxo-4-[(2-pyridinylmethyl)amino]butyl]-
-
-
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-3,3-difluoro-1-(1-methylethyl)-2,4-dioxo-4-[(2-pyridinylmethyl)amino]butyl]-
-
-
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-3,3-difluoro-1-(1-methylethyl)-2-oxo-4-[(phenylmethyl)amino]butyl]-
-
-
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-3,3-difluoro-4-(methylamino)-1-(1-methylethyl)-2,4-dioxobutyl]-
-
-
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-4-(benzoylamino)-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-4-amino-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-4-[[(1,1-dimethylethoxy)carbonyl]amino]-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
L-Prolinamide, N-(phenoxycarbonyl)-L-valyl-N-[(1S)-3,3-difluoro-1-(1-methylethyl)-2,4-dioxo-4-[(2-pyridinylmethyl)amino]butyl]-
-
-
L-Prolinamide, N-(phenoxycarbonyl)-L-valyl-N-[(1S)-3,3-difluoro-4-(methylamino)-1-(1-methylethyl)-2,4-dioxobutyl]-
-
-
L-Prolinamide, N-(phenoxycarbonyl)-L-valyl-N-[(1S)-4-[[(1,1-dimethylethoxy)carbonyl]amino]-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
L-Prolinamide, N-(phenoxycarbonyl)-L-valyl-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-3,3-difluoro-1-(1-methylethyl)-2-oxo-4-[(phenylmethyl)amino]butyl]-
-
-
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-3,3-difluoro-4-(methylamino)-1-(1-methylethyl)-2,4-dioxobutyl]-
-
-
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-4-amino-3,3-difluoro-1-(1-methylethyl)-2,4-dioxobutyl]-
-
-
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-4-amino-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-4-[[(1,1-dimethylethoxy)carbonyl]amino]-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
matrix metalloproteinase-7
-
human leukocyte elastase cleaves matrix metalloproteinase-7 resulting in loss of enzymatic activity
-
MeOSuc-Ala-Ala-Pro-Val-chloromethylketone
-
neutrophil elastase-specific inhibitor
methoxysuccinyl-Ala-Ala-Pro-(isobutyl-4,4,5,5-tetramethyl-1,3,2-dioxaborolane)amide
-
-
N'-{1-[2-(2-Acetylamino-propionylamino)-propionyl]-pyrrolidine-2-carbonyl}-N-methyl-hydrazinecarboxylic acid 1-benzylcarbamoyl-ethyl ester
-
-
N'-{1-[2-(2-Acetylamino-propionylamino)-propionyl]-pyrrolidine-2-carbonyl}-N-methyl-hydrazinecarboxylic acid 1-carbamoyl-ethyl ester
-
-
N-(1-(1-[1-(4-benzoyl-phenylcarbamoyl)-2-methyl-propylcarbamoyl]-3-methyl-butylcarbamoyl)-2-(4-hydroxy-phenyl)-ethyl)-succinamic acid
-
-
N-(1-{1-Methyl-2-oxo-2-[2-(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidin-1-yl]-ethylcarbamoyl}-ethyl)-succinamic acid methyl ester
-
-
N-(1-{2-[2-(3-Chloro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidin-1-yl]-1-methyl-2-oxo-ethylcarbamoyl}-ethyl)-succinamic acid methyl ester
-
-
N-(1-{2-[2-(4-Ethoxy-3,3-difluoro-1-isopropyl-2-oxo-butylcarbamoyl)-pyrrolidin-1-yl]-1-methyl-2-oxo-ethylcarbamoyl}-ethyl)-succinamic acid methyl ester
-
-
N-(2,2-diphenyl-ethyl)-1-(1,1,3-trioxo-1,3-dihydro-1lambda6-1,2-benzisothiazol-2-yl)-methanesulfonamide
-
-
N-(5-(adamantane-1-sulfonylamino)-5-[1-(1-formyl-2-methyl-propylcarbamoyl)-ethylcarbamoyl]-pentyl)-succinamic acid
-
-
N-(5-(adamantane-1-sulfonylamino)-5-[1-(1-formyl-2-methyl-propylcarbamoyl)-ethylcarbamoyl]-pentyl)-terephthalamic acid
-
-
N-(5-benzyloxycarbonylamino-1-(1-[2-(1-formyl-2-methyl-propylcarbamoyl)-pyrrolidine-1-carbonyl]-2-methyl-propylcarbamoyl)-pentyl)-succinamic acid
-
-
N-([3-(carboxymethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]acetyl)-L-valyl-N-[(3R,S)1,1,1-trifluoro-4-methyl-2-oxopentan-3-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]acetyl)-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]acetyl)-L-valyl-N-[(3S)-1-methoxy-4-methyl-1,2-dioxopentan-3-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2,4-dioxoimidazolidin-1-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2,5-dioxoimidazolidin-1-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2,6-dioxotetrahydropyrimidin-1(2H)-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2-oxoimidazolidin-1-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2-oxoimidazolidin-1-yl]acetyl)-L-valyl-N-[(3R)-1,1,1-trifluoro-4-methyl-2-oxopentan-3-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-2-oxoimidazolidin-1-yl]acetyl)-L-valyl-N-[(3S)-1,1,1-trifluoro-4-methyl-2-oxopentan-3-yl]-L-prolinamide
-
i.e. AE-3763, it effects in lipopolysaccharide-induced lung injury model of lung edema and leukocyte infiltration, overveiw
N-([3-(carboxymethyl)-4,4-dimethyl-2,5-dioxoimidazolidin-1-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-5,5-dimethyl-2,4-dioxoimidazolidin-1-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([3-(carboxymethyl)-5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([4-(carboxymethoxy)phenoxy]acetyl)-L-valyl-N-[(benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([4-(carboxymethyl)-2,3-dioxopiperazin-1-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
-
-
N-([4-(carboxymethyl)-2,3-dioxopiperazin-1-yl]acetyl)-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-prolinamide
-
-
N-([4-(carboxymethyl)-2,3-dioxopiperazin-1-yl]acetyl)-L-valyl-N-[(3S)-1-methoxy-4-methyl-1,2-dioxopentan-3-yl]-L-prolinamide
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N-([4-(carboxymethyl)-2,5-dioxopiperazin-1-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
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N-([4-(carboxymethyl)-3,5-dioxo-4,5-dihydro-1,2,4-triazin-2(3H)-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
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N-([4-(carboxymethyl)-6-methyl-3,5-dioxo-4,5-dihydro-1,2,4-triazin-2(3H)-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
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N-([4-(carboxymethyl)piperazin-1-yl]acetyl)-L-valyl-N-[(2S)-1-(1,3-benzoxazol-2-yl)-3-methyl-1-oxobutan-2-yl]-L-prolinamide
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N-benzyl-1-(1,1,3-trioxo-1,3-dihydro-1lambda6-1,2-benzisothiazol-2-yl)-methanesulfonamide
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N-galloyl-4-alkyliden-beta-lactam
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a beta-lactam with an N-linked galloyl moiety, specific noncompetitive inhibition of the enzyme, but not affecting chemotactic response and viability of polymorphonuclear leukocytes, synthesis and structure, overview
N-methoxysuccinyl-Ala-Ala-Pro-Val-chloromethyl ketone
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neutrophil elastase-specific inhibitor
N-phenethyl-1-(1,1,3-trioxo-1,3-dihydro-1lambda6-1,2-benzisothiazol-2-yl)-methanesulfonamide
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N-[(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)acetyl]-L-valyl-N-[(3R,S)-1,1,1-trifluoro-4-methyl-2-oxopentan-3-yl]-L-prolinamide
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N-{1-[2-(2-{2-[(2-Chloro-acetyl)-isopropyl-amino]-acetyl}-pyrrolidin-1-yl)-1-methyl-2-oxo-ethylcarbamoyl]-ethyl}-succinamic acid
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N-{1-[2-(2-{2-[(2-Chloro-acetyl)-isopropyl-amino]-acetyl}-pyrrolidin-1-yl)-1-methyl-2-oxo-ethylcarbamoyl]-ethyl}-succinamic acid methyl ester
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N-{1-[2-(2-{2-[Isopropyl-(4-nitro-phenoxycarbonyl)-amino]-acetyl}-pyrrolidin-1-yl)-1-methyl-2-oxo-ethylcarbamoyl]-ethyl}-succinamic acid methyl ester
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N-{5-(Adamantane-1-sulfonylamino)-5-[1-(1-formyl-2-methyl-propylcarbamoyl)-ethylcarbamoyl]-pentyl}-4-dihydroxymethyl-benzamide
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N2-[4-[(Z)-(2,4-dioxo-1,3-thiazolidin-5-ylidene)methyl]benzoyl]-N-(2-propylphenyl)-L-leucinamide
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pancreatic secretory trypsin inhibitor
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variants of human secretory trypsin inhibitor are constructed with the aim of producing inhibitors specific for human leukocyte elastase. Models of the human pancreatic secretory trypsin inhibitor/human leukocytic elastase and human pancreatic secretory trypsin inhibitor/chymotrypsin complexes are generated by computer aided protein design and used to plan better human leukocyte elastase inhibitors. The native human pancreatic secretory trypsin inhibitor with Lys in position P1 (amino acid 18) is a highly potent inhibitor for trypsin and completely inactive towards chymotrypsin and elastase like proteinases. Replacing the Lys in P1 by Leu (pancreatic secretory trypsin inhibitor 7) causes a drastic change of the specificity : this variant no longer inhibits trypsin-like enzymes but is an excellent inhibitor of chymotrypsin and human leukocytic elastase
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prolastin
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i.e. alpha1-antitrypsin, acts similar to monocyte/neutrophil elastase inhibitor, MNEI
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propolis
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IC50: 0.002 mg dry weight per ml for ethyl acetate extract of propolis
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secretory leukoproteinase inhibitor
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important inhibitor of neutrophil elastase
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semisynthetic glucan sulfates
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with pullulan as basic polysaccharide: PulS1, PulS2, PulS3 (IC50: 0.0000181 mM), PulS4, PulS5, PulS6 and PulS7, with glucuronoxylan as basic polysaccharide: PPS, and with phycarine as basic polysaccharide: PS3
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tert-butyl (6R,7S)-3-[(acetyloxy)methyl]-7-chloro-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate 5,5-dioxide
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tert-butyl (6R,7S)-3-[(acetyloxy)methyl]-7-methoxy-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate 5,5-dioxide
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