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Information on EC 3.4.21.37 - leukocyte elastase and Organism(s) Homo sapiens and UniProt Accession P08246

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.37 leukocyte elastase
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P08246 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Hydrolysis of proteins, including elastin. Preferential cleavage Val-/- > Ala-/-
Synonyms
neutrophil elastase, leukocyte elastase, granulocyte elastase, pmn elastase, elane, pmn-elastase, polymorphonuclear leukocyte elastase, polymorphonuclear neutrophil elastase, neutrophil-elastase, lysosomal elastase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
leukocyte elastase
-
neutrophil elastase
-
neutrophil-released elastase
-
bone marrow serine protease
-
-
-
-
ELA2
-
-
elastase
-
-
-
-
elaszym
-
-
-
-
granulocyte elastase
lysosomal elastase
-
-
-
-
N-elastase
-
-
NE
-
-
-
-
neutrophil elastase
neutrophil-elastase
-
-
PMN elastase
PMN-elastase
-
-
polymorphonuclear leukocyte elastase
-
-
polymorphonuclear neutrophil elastase
-
-
serine elastase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9004-06-2
eastase
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid + H2O
?
show the reaction diagram
-
-
-
?
Antithrombin III + H2O
?
show the reaction diagram
degradation
-
-
?
Collagen + H2O
?
show the reaction diagram
degradation
-
-
?
Elastin + H2O
?
show the reaction diagram
degradation
-
-
?
Fibrin + H2O
?
show the reaction diagram
degradation
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
degradation
-
-
?
GW475151 + H2O
?
show the reaction diagram
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-(4-(4-morpholinylcarbonyl)benzoyl)-Val-Pro-Ile + H2O
?
show the reaction diagram
-
-
-
?
OMTKY3a + H2O
?
show the reaction diagram
-
-
-
?
Proteoglycan + H2O
?
show the reaction diagram
degradation
-
-
?
secretory leukocyte protease inhibitor + H2O
?
show the reaction diagram
-
-
-
?
(VGVAPG)2V + H2O
VGVAPGVGV + APGV + VGVAPG + VGVAPGV
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
ir
2-(chloroacetyl)-3-naphthoic acid o-toluidide + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-APEEIMDQQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-APEEI + MDQQ-N-(2,4-dinitrophenyl)ethylenediamine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
kcat/Km is 45times greater for neutrophil elastase than for proteinase 3
-
-
?
acetyl-Ala-Ala-Ala-p-nitroanilide + H2O
?
show the reaction diagram
acetyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-L-Phe-2-naphthyl ester + H2O
acetyl-L-Phe + 2-naphthol
show the reaction diagram
-
-
-
-
?
alpha1-PI + H2O
?
show the reaction diagram
-
important antiprotease of the lung, enzyme reduces the lungs’ primary protection against proteolysis
-
-
?
annexin 1 + H2O
?
show the reaction diagram
antithrombin + H2O
?
show the reaction diagram
-
catalyzes the inactivation of antithrombin by a specific and limited proteinolytic cleavage
-
-
?
APG(VGVAPG)2 + H2O
APGVGV + APGVAPGV + APGVGVAPGVGV + APGVGVAPG + APGV + VGVAPGV
show the reaction diagram
-
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
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-3-hydroxy-5-phenylpyrrole + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-4-nitrophenol + H2O
benzyloxycarbonyl-Ala + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Ala 2-naphthyl ester + H2O
benzyloxycarbonyl-Ala + 2-naphthol
show the reaction diagram
-
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
Cartilage proteoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
CD2 + H2O
?
show the reaction diagram
-
CD2 on peripheral blood T lymphocytes
-
-
?
CD4 + H2O
?
show the reaction diagram
-
CD4 on peripheral blood T lymphocytes
-
-
?
CD8 + H2O
?
show the reaction diagram
-
CD8 on peripheral blood T lymphocytes
-
-
?
coagulation factor V + H2O
?
show the reaction diagram
-
-
-
-
?
coagulation factor VIII + H2O
?
show the reaction diagram
-
-
-
-
?
coagulation factor XI + H2O
?
show the reaction diagram
-
-
-
-
?
coagulation factor XIII + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
Collagen type I + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type II + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type III + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagenase + H2O
?
show the reaction diagram
-
-
-
-
?
complement factor C3 + H2O
?
show the reaction diagram
-
-
-
-
?
complement factor C5 + H2O
?
show the reaction diagram
-
-
-
-
?
complement receptor + H2O
?
show the reaction diagram
-
-
-
-
?
corticosteroid-binding globulin + H2O
?
show the reaction diagram
Cut homeobox 1 + H2O
?
show the reaction diagram
-
-
-
-
?
elafin + H2O
?
show the reaction diagram
Elastin + H2O
?
show the reaction diagram
EMILIN1 + H2O
?
show the reaction diagram
-
-
-
-
?
Factor VIIIa + H2O
?
show the reaction diagram
-
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
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
G-CSF receptor + H2O
?
show the reaction diagram
Gelatinase + H2O
?
show the reaction diagram
-
-
-
-
?
gp120 protein + H2O
?
show the reaction diagram
-
-
-
-
?
GRGGAGGRG + H2O
GRGGA + GGRG
show the reaction diagram
-
-
-
-
?
GRGGFGGRG + H2O
GRGGF + GGRG
show the reaction diagram
-
-
-
-
?
GRGGLGGRG + H2O
GRGGL + GGRG
show the reaction diagram
-
-
-
-
?
GRGGRGGRG + H2O
GRGGR + GGRG
show the reaction diagram
-
-
-
-
?
GRGGVGGRG + H2O
GRGGV + GGRG
show the reaction diagram
-
-
-
-
?
heparin-antithrombin complex + H2O
?
show the reaction diagram
-
-
-
-
?
histone H1 + H2O
?
show the reaction diagram
-
-
-
-
?
histone H4 + H2O
?
show the reaction diagram
-
-
-
-
?
human IgG3 + H2O
?
show the reaction diagram
-
-
-
-
?
IgA + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
-
?
immunoglobulin A + H2O
?
show the reaction diagram
-
-
-
-
?
immunoglobulin G + H2O
?
show the reaction diagram
-
-
-
-
?
immunoglobulin M + H2O
?
show the reaction diagram
-
-
-
-
?
intercellular adhesion molecule-1 + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-2 + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-36 receptor antagonist + H2O
activated interleukin-36 receptor antagonist V2 + ?
show the reaction diagram
-
the enzyme cleaves 9 amino acids upstream of the A-X-D consensus of interleukin-36 receptor antagonist
-
-
?
interleukin-6 + H2O
?
show the reaction diagram
-
-
-
-
?
IpaB protein + H2O
?
show the reaction diagram
-
neutrophil elastase cleaves IpaB protein after alanine, valine, isoleucine, or threonine residues
-
-
?
kininogen + H2O
?
show the reaction diagram
-
-
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
lung surfactant + H2O
?
show the reaction diagram
-
-
-
-
?
MAAPV-p-nitroanilide + H2O
MAAPV + p-nitroaniline
show the reaction diagram
-
-
-
-
?
matrix metalloprotease 9 + H2O
matrix metalloprotease 9 peptide fragments
show the reaction diagram
-
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
?
show the reaction diagram
-
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-Ala-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Ala-thiobenzyl ester
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-alpha-aminobutyryl-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-methylcoumarin 7-amide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 7-amino-4-methylcoumarin
show the reaction diagram
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroanilide
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-7-amido-4-methylcoumarin + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-thiobenzyl ester
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ile-Pro-Met-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Pro-Ala-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Pro-Ala-thiobenzyl ester
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Pro-Val-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Pro-Val-thiobenzyl ester
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Pro-Val-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Pro-Val-thiobenzyl ester
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Val-4-nitroanilide
methoxysuccinyl-Val + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Val-thiobenzyl ester
?
show the reaction diagram
-
-
-
-
?
mucin + H2O
?
show the reaction diagram
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
N-methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroaniline
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-succinyl-Ala-Ala-Val 4-nitroanilide + H2O
N-succinyl-Ala-Ala-Val + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Nalpha-methoxysuccinyl-Nepsilon-2-picolinoyl-L-lysinyl-L-Ala-L-Pro-L-Val 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
native type I collagen + H2O
3/4 length fragments similar in size to those produced by interstitial collagenase
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoic acid-Glu-Ala-Ile-Pro-Met-Ser-Ile-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoic acid-Gly-Ile-Ala-Thr-Phe-Cys-Met-Leu-Met-Pro-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoic acid-Met-Met-Arg-Cys-Ala-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoic acid-Thr-Phe-Cys-Met-Leu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoic acid-Val-Ala-Asp-Cys-Ala-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoic acid-Val-Ala-Glu-Cys-Cys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoic acid-Val-Ser-Ala-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
show the reaction diagram
-
-
-
-
?
oxidized B chain of insulin + H2O
?
show the reaction diagram
oxytalan fibre + H2O
?
show the reaction diagram
-
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
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
-
-
-
?
plasminogen + H2O
miniplasminogen + ?
show the reaction diagram
-
-
-
-
?
plasminogen activator inhibitor type-1 + H2O
?
show the reaction diagram
-
-
-
-
?
platelet IIb/IIIa receptor + H2O
?
show the reaction diagram
-
-
-
-
?
procarboxypeptidase R + H2O
carboxypeptidase R + ?
show the reaction diagram
-
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
-
-
?
progranulin + H2O
?
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
-
enzyme capable of degrading proteins of the lung extracellular matrix in vitro
-
-
?
protein C + H2O
small peptides
show the reaction diagram
proteinase-activated receptor 2 N-terminus + H2O
GPNSKGRSLIGRLDTPPPITGKGAPVEPGFSVDEFSAS + VLTGKLTTVFLP
show the reaction diagram
-
-
-
-
?
Proteoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
secretory leucoprotease inhibitor + H2O
?
show the reaction diagram
SLPI + H2O
?
show the reaction diagram
-
important antiprotease of the lung, enzyme reduces the lungs’ primary protection against proteolysis
-
-
?
SP-D protein + H2O
SP-D protein peptide fragments
show the reaction diagram
succinyl-Ala-Ala-NH-4-nitroanilide + H2O
succinyl-Ala-Ala-NH2 + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Ala-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Ile-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Tyr-Leu-Val-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
syndecan-1 + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Ala-4-nitrophenyl ester + H2O
tert-butyloxycarbonyl-Ala + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Val-4-nitrophenyl ester + H2O
tert-butyloxycarbonyl-Val + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
thrombomodulin + H2O
?
show the reaction diagram
-
-
-
-
?
tissue inhibitor of metalloprotease + H2O
?
show the reaction diagram
-
-
-
-
?
tissue inhibitor of metalloprotease-1 + H2O
tissue inhibitor of metalloprotease-1 peptide fragments
show the reaction diagram
-
i.e. TIMP-1, neutrophil elastase degrades TIMP-1 and cleaves between Val69-Cys70
-
-
?
tissue necrosis factor alpha + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-Ala-3-hydroxy-5-phenylpyrrole + H2O
?
show the reaction diagram
-
-
-
-
?
tosyl-Ala-4-nitrophenol + H2O
tosyl-Ala + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
tropoelastin + H2O
?
show the reaction diagram
-
-
-
-
?
VAPGVGVAPGV + H2O
VAPGVGV + APGV + VAPGV + GVAPGV
show the reaction diagram
-
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
-
-
?
VLLFSEVL + H2O
VLLF + SEVL
show the reaction diagram
-
-
-
-
?
VLLISEVL + H2O
VLLI + SEVL
show the reaction diagram
-
-
-
-
?
VLLVSEVL + H2O
VLLV + SEVL
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Antithrombin III + H2O
?
show the reaction diagram
degradation
-
-
?
Collagen + H2O
?
show the reaction diagram
degradation
-
-
?
Elastin + H2O
?
show the reaction diagram
degradation
-
-
?
Fibrin + H2O
?
show the reaction diagram
degradation
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
degradation
-
-
?
Proteoglycan + H2O
?
show the reaction diagram
degradation
-
-
?
alpha1-PI + H2O
?
show the reaction diagram
-
important antiprotease of the lung, enzyme reduces the lungs’ primary protection against proteolysis
-
-
?
annexin 1 + H2O
?
show the reaction diagram
-
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
-
-
?
coagulation factor V + H2O
?
show the reaction diagram
-
-
-
-
?
coagulation factor VIII + H2O
?
show the reaction diagram
-
-
-
-
?
coagulation factor XI + H2O
?
show the reaction diagram
-
-
-
-
?
coagulation factor XIII + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type I + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type II + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen type III + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagenase + H2O
?
show the reaction diagram
-
-
-
-
?
complement factor C3 + H2O
?
show the reaction diagram
-
-
-
-
?
complement factor C5 + H2O
?
show the reaction diagram
-
-
-
-
?
complement receptor + H2O
?
show the reaction diagram
-
-
-
-
?
corticosteroid-binding globulin + H2O
?
show the reaction diagram
-
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
-
-
?
elafin + H2O
?
show the reaction diagram
Elastin + H2O
?
show the reaction diagram
EMILIN1 + H2O
?
show the reaction diagram
-
-
-
-
?
Factor VIIIa + H2O
?
show the reaction diagram
-
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
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
G-CSF receptor + H2O
?
show the reaction diagram
-
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
-
-
?
Gelatinase + H2O
?
show the reaction diagram
-
-
-
-
?
gp120 protein + H2O
?
show the reaction diagram
-
-
-
-
?
histone H1 + H2O
?
show the reaction diagram
-
-
-
-
?
histone H4 + H2O
?
show the reaction diagram
-
-
-
-
?
IgA + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
-
?
immunoglobulin A + H2O
?
show the reaction diagram
-
-
-
-
?
immunoglobulin G + H2O
?
show the reaction diagram
-
-
-
-
?
immunoglobulin M + H2O
?
show the reaction diagram
-
-
-
-
?
intercellular adhesion molecule-1 + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-2 + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-36 receptor antagonist + H2O
activated interleukin-36 receptor antagonist V2 + ?
show the reaction diagram
-
the enzyme cleaves 9 amino acids upstream of the A-X-D consensus of interleukin-36 receptor antagonist
-
-
?
interleukin-6 + H2O
?
show the reaction diagram
-
-
-
-
?
IpaB protein + H2O
?
show the reaction diagram
-
neutrophil elastase cleaves IpaB protein after alanine, valine, isoleucine, or threonine residues
-
-
?
kininogen + H2O
?
show the reaction diagram
-
-
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
lung surfactant + H2O
?
show the reaction diagram
-
-
-
-
?
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
methoxysuccinyl-Ala-Ala-Pro-Val + 4-nitroanilide
show the reaction diagram
-
-
-
-
?
mucin + H2O
?
show the reaction diagram
-
proteolysis of mucin is suggested to be involved in cell damaging processes during chronic infection and inflammation of the respiratory tract
-
-
?
oxytalan fibre + H2O
?
show the reaction diagram
-
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
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
-
-
-
?
plasminogen + H2O
miniplasminogen + ?
show the reaction diagram
-
-
-
-
?
plasminogen activator inhibitor type-1 + H2O
?
show the reaction diagram
-
-
-
-
?
platelet IIb/IIIa receptor + H2O
?
show the reaction diagram
-
-
-
-
?
procarboxypeptidase R + H2O
carboxypeptidase R + ?
show the reaction diagram
-
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
-
-
?
progranulin + H2O
?
show the reaction diagram
-
-
-
-
?
protein C + H2O
small peptides
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
Proteoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
secretory leucoprotease inhibitor + H2O
?
show the reaction diagram
-
i.e. SLPI, SLPI is cleaved and inactivated by neutrophil elastase in cystic fibrosis lungs
-
-
?
SLPI + H2O
?
show the reaction diagram
-
important antiprotease of the lung, enzyme reduces the lungs’ primary protection against proteolysis
-
-
?
SP-D protein + H2O
SP-D protein peptide fragments
show the reaction diagram
-
no activity in healthy lungs, but in 50% of cystic fibrosis patient lungs
cleavage product identification by N-terminal sequencing, overview
-
?
thrombomodulin + H2O
?
show the reaction diagram
-
-
-
-
?
tissue inhibitor of metalloprotease + H2O
?
show the reaction diagram
-
-
-
-
?
tissue necrosis factor alpha + H2O
?
show the reaction diagram
-
-
-
-
?
tropoelastin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxyethyl (4R)-4-[4-cyanophenyl-6-methyl-2-oxo-1-[3-(trifluoromethyl)phenyl]]-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
GW475151
suicide inhibitor
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
-
MDL101146
suicide inhibitor
MeO-Suc-Ala-Ala-Pro-Ala-CH2Cl
MeO-Suc-Ala-Ala-Pro-Val-CH2Cl
methoxysuccinyl-Ala-Ala-Pro-Val-CH2Cl
-
methoxysuccinyl-Ala-Ala-Pro-Val-chloromethyl ketone
-
N2-[4-[(Z)-(2,4-dioxo-1,3-thiazolidin-5-ylidene)methyl]benzoyl]-N-(2-propylphenyl)-L-leucinamide
-
((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
-
-
(-)-epigallocatechin-3-gallate
-
-
(1,1-dioxido-3-oxo-1,2-benzisothiazol-2(3H)-yl)methyl 2,6-dichlorobenzoate
-
-
(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
-
-
(22E,24R)-ergosta-7,22-dien-2alpha,3alpha,9alpha-triol
-
-
(2R, 3R)-6-methyl-3'-geranyl-2,3-trans-5,7,4'-trihydroxyflavonol
-
-
(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
-
-
(3-methylindazol-1-yl)-m-tolyl-methanone
-
-
(3beta,5alpha,8alpha,22E)-ergosta-6,22-diene-3-ol-5,8-peroxide
-
-
(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
-
-
(5E)-3-benzyl-5-but-2-ynylidenedihydrofuran-2(3H)-one
-
-
(5E)-3-benzyl-5-prop-2-ynylidenedihydrofuran-2(3H)-one
-
-
(5E)-3-butyl-5-prop-2-ynylidenedihydrofuran-2(3H)-one
-
-
(5E)-5-prop-2-ynylidenedihydrofuran-2(3H)-one
-
-
(5Z)-3-benzyl-5-prop-2-ynylidenedihydrofuran-2(3H)-one
-
-
(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
-
-
(6E)-3-benzyl-6-prop-2-ynylidenetetrahydro-2H-pyran-2-one
-
-
(6E)-6-(1-bromoethylidene)-3-isopropyltetrahydro-2H-pyran-2-one
-
-
(6E)-6-(bromomethylene)-3-isopropyltetrahydro-2H-pyran-2-one
-
-
(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
-
-
(6Z)-3-benzyl-6-prop-2-ynylidenetetrahydro-2H-pyran-2-one
-
-
(6Z)-6-(bromomethylene)-3-isopropyltetrahydro-2H-pyran-2-one
-
-
(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-(2-methylbenzoyl)-1H-indazole-3-carboxylic acid phenylamide
-
-
1-(3-aminobenzoyl)-1H-indazole-3-carboxylic acid ethyl ester
-
-
1-(3-aminobenzoyl)-1H-indazole-3-carboxylic acid phenylamide
-
-
1-(3-methoxybenzoyl)-1H-indazole-3-carboxylic acid ethyl ester
-
-
1-(3-methoxybenzoyl)-1H-indazole-3-carboxylic acid methyl ester
-
-
1-(3-methoxybenzoyl)-1H-indazole-3-carboxylic acid phenylamide
-
-
1-(3-methoxybenzoyl)-1H-indazole-3-carboxylic acid propyl ester
-
-
1-(3-methylbenzoyl)-1H-indazole-3-carboxylic acid methyl ester
-
-
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-(4-chlorophenyl)-3,3-diethylazetidine-2,4-dione
-
-
1-(4-chlorophenyl)-3,3-dimethylazetidine-2,4-dione
-
-
1-(4-cyanobenzoyl)-1H-indazole-3-carboxylic acid ethyl ester
-
-
1-(6-((benzo[d]thiazol-2-ylthio)methyl)pyridin-3-yl)-3,3-diethylazetidine-2,4-dione
-
-
1-(pyridine-4-carbonyl)-1H-indazole-3-carboxylic acid phenylamide
-
-
1-(thiophene-3-carbonyl)-1H-indazole-3-carboxylic acid ethyl ester
-
-
1-(thiophene-3-carbonyl)-1H-indazole-3-carboxylic acid methyl ester
-
-
1-(thiophene-3-carbonyl)-1H-indazole-3-carboxylic acid phenylamide
-
-
1-(thiophene-3-carbonyl)-1H-indazole-3-carboxylic acid propyl ester
-
-
1-benzoyl-1H-indazole-3-carboxylic acid methyl ester
-
-
1-benzoyl-1H-indazole-3-carboxylic acid phenylamide
-
-
1-benzyl-3,3-dimethylazetidine-2,4-dione
-
-
1-butyryl-1H-indazole-3-carboxylic acid ethyl ester
-
-
1-cyclopentanecarbonyl-1H-indazole-3-carboxylic acid ethyl ester
-
-
1-methyl-1H-tetrazole-5-thiol
-
-
1-propionyl-1H-indazole-3-carboxylic acid ethyl ester
-
-
1-[(3-chlorophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
-
-
1-[(3-fluorophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
-
-
1-[(3-methylphenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
-
-
1-[(3-nitrophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
-
-
1-[(4-chlorophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
-
-
1-[(4-cyanophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
-
-
1-[(4-fluorophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
-
-
1-[(4-methylphenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
-
-
1-[(methylsulfonyl)oxy]pyrrolidine-2,5-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-[2-(chloromethyl)phenyl]-3,3-difluoroazetidin-2-one
-
-
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
-
-
14alpha-hydroxy-ergosta-4,7,9(11),22-tetraen-3,6-dione
-
-
1H-indazol-1-yl(3-methylphenyl)methanone
-
-
2,2,2-trifluoroethyl 1-(phenylcarbonyl)-1H-indazole-3-carboxylate
-
-
2,2,2-trifluoroethyl 1-(thiophen-3-ylcarbonyl)-1H-indazole-3-carboxylate
-
-
2,2,2-trifluoroethyl 1-[(3-aminophenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
2,2,2-trifluoroethyl 1-[(3-methoxyphenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
2,2,2-trifluoroethyl 1-[(3-methylphenyl)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-dinitrophenyl)-1,2-benzisothiazol-3(2H)-one 1,1-dioxide
-
-
2-(2-ethylbutanoyl)-1,2-benzisothiazol-3(2H)-one
-
-
2-(2-furoyl)-1,2-benzisothiazol-3(2H)-one
-
-
2-(2-furoyl)-1,2-benzisothiazol-3(2H)-one 1,1-dioxide
-
-
2-(2-methoxypyridin-3-yl)-5-methyl-4H-3,1-benzoxazin-4-one
-
-
2-(2-phenoxypyridin-3-yl)-4H-3,1-benzoxazin-4-one
-
-
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-(3-trifluoromethylphenylamino)-4H-thieno[2,3-d][1,3]oxazin-4-one
-
-
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-(chloromethyl)-1,2-benzisothiazol-3(2H)-one 1,1-dioxide
-
-
2-(thiophen-2-ylcarbonylthio)-N-(2-oxo-2,3,4,5-tetrahydrothiophen-3-yl)propionamide
-
reversible, slow-binding, fully competitive
2-(trifluoromethyl)-4H-3,1-benzoxazin-4-one
-
-
2-Acetylamino-N-(1-ethylcarbamoyl-ethyl)-propionamide
-
-
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-amino-4H-3,1-benzoxazin-4-one
-
-
2-amino-5-ethyl-4H-3,1-benzoxazin-4-one
-
-
2-benzoyl-1,2-benzisothiazol-3(2H)-one 1,1-dioxide
-
-
2-CF3CF2C(O)NH-C6H4-SO2-F
-
-
2-CF3SNH-C6H4-SO2-F
-
-
2-chloro-4-(1-hydroxyoctadecyl)benzoic acid
-
SC-39026, reversible non-competitive inhibition at low concentrations (0.0005-0.00125 mM), mixed type inhibition at higher concentrations
2-ethoxy-4H-3,1-benzoxazin-4-one
-
-
2-ethoxy-5-ethyl-4H-3,1-benzoxazin-4-one
-
-
2-methyl-4H-3,1-benzoxazin-4-one
-
-
2-nitrophenylboronic acid
-
-
2-[(Imidazole-1-carbonyl)-amino]-pentanoic acid methyl ester
-
-
2-[2-(1H-imidazol-1-yl)pyridin-3-yl]-5-methyl-4H-3,1-benzoxazin-4-one
-
-
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
-
-
2-[benzyloxycarbonyl-NHCH2-C(O)NH]-C6H4-SO2-F
-
-
3'-geranyl-5,7,2',4'-tetrahydroxyisoflavanone
-
-
3,3-diethyl-1-(4-((phenylthio)methyl)phenyl)azetidine-2,4-dione
-
-
3,3-diethyl-1-(4-methoxyphenyl)azetidine-2,4-dione
-
-
3,3-diethyl-1-(4-methylphenyl)azetidine-2,4-dione
-
-
3,3-diethyl-1-(6-methylpyridin-3-yl)azetidine-2,4-dione
-
-
3,3-diethyl-1-(naphthalen-1-yl)azetidine-2,4-dione
-
-
3,3-diethyl-1-(pyridin-3-yl)azetidine-2,4-dione
-
-
3,3-diethyl-1-o-tolylazetidine-2,4-dione
-
-
3,3-diethyl-1-phenylazetidine-2,4-dione
-
-
3,3-diethyl-1-[4-(naphthalen-2-yloxy)phenyl]azetidine-2,4-dione
-
-
3,3-dimethyl-1-phenylazetidine-2,4-dione
-
-
3,4-dichloro-1H-isochromen-1-one
-
-
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-benzyl-1-(sulfooxy)pyrrolidine-2,5-dione
-
-
3-benzyl-1-[(methylsulfonyl)oxy]pyrrolidine-2,5-dione
-
-
3-benzyl-1-{[(4-vinylphenyl)sulfonyl]oxy}pyrrolidine-2,5-dione
-
-
3-benzyl-3-ethyl-1-phenylazetidine-2,4-dione
-
-
3-benzyl-3-methyl-1-phenylazetidine-2,4-dione
-
-
3-CF3-C6H4-CO-Ala-Ala-4-nitroanilide
-
-
3-chloro-1H-isochromen-1-one
-
-
3-ethyl-3-isobutyl-1-phenylazetidine-2,4-dione
-
-
3-isopropyl-1-[(methylsulfonyl)oxy]pyrrolidine-2,5-dione
-
-
3-isopropyl-1-{[(4-vinylphenyl)sulfonyl]oxy}pyrrolidine-2,5-dione
-
-
3-isopropyl-6-methylenetetrahydro-2H-pyran-2-one
-
-
3-methoxy-1-oxo-1H-isochromen-7-yl nitrite
-
-
3-methoxy-7-nitro-1H-isochromen-1-one
-
-
3-tert-butyl-1-{[(4-vinylphenyl)sulfonyl]oxy}pyrrolidine-2,5-dione
-
-
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
-
-
3beta,5alpha,9alpha-trihydroxy-ergosta-7,22-dien-6-one
-
-
3beta,5alpha-dihydroxy-6beta-methoxyergosta-7,22-diene
-
-
3beta,5alpha-dihydroxy-ergosta-7,22-dien-6-one
-
-
3beta-hydroxy-ergosta-7,22-dien-6-one
-
-
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-(3,3-diethyl-2,4-dioxoazetidin-1-yl)benzonitrile
-
-
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-CH3-C6H4-SO2-F
-
-
4-chloro-3-ethoxy-1H-isochromen-1-one
-
-
4-chloro-3-methoxy-1-oxo-1H-isochromen-7-yl nitrite
-
-
4-chloro-3-methoxy-7-nitro-1H-isochromen-1-one
-
-
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
-
-
5,6-dimethyl-2-(4-nitrophenylamino)-4H-thieno[2,3-d][1,3]thioxazin-4-one
-
-
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-aminopyridin-6-one-containing trifluoromethyl ketones
-
-
-
5-chloro-2-(2-bromophenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
5-chloro-2-(2-chlorophenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
5-chloro-2-(2-fluorophenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
5-chloro-2-(2-methoxyphenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
5-chloro-2-(2-methylphenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
5-chloro-2-(2-phenoxypyridin-3-yl)-4H-3,1-benzoxazin-4-one
-
-
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-(isopropylamino)-4H-3,1-benzoxazin-4-one
-
-
5-ethyl-2-methyl-4H-3,1-benzoxazin-4-one
-
-
5-ethyl-2-[2-(4-methylpiperazin-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-methoxy-2-(2-phenoxypyridin-3-yl)-4H-3,1-benzoxazin-4-one
-
-
5-methyl-2-(2-methylpyridin-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-phenoxyphenyl)-4H-3,1-benzoxazin-4-one
-
-
5-methyl-2-(2-phenoxypyridin-3-yl)-4H-3,1-benzoxazin-4-one
-
-
5-methyl-2-(2-[[2-(morpholin-4-yl)ethyl]amino]pyridin-3-yl)-4H-3,1-benzoxazin-4-one
-
-
5-methyl-2-(6-methylpyridin-3-yl)-4H-3,1-benzoxazin-4-one
-
-
5-methyl-2-(pyridin-3-yl)-4H-3,1-benzoxazin-4-one
-
-
5-methyl-2-(trifluoromethyl)-4H-3,1-benzoxazin-4-one
-
-
5-methyl-2-[2-(4-methylpiperazin-1-yl)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
-
-
5alpha,6alpha,8alpha,9alpha-diepoxy-ergost-22-en-3beta,7alpha-diol
-
-
5alpha,6alpha-epoxy-ergosta-8(14),22-diene-3beta,7alpha-diol
-
-
5alpha,6alpha-epoxy-ergosta-8(9),22-dien-7-one-3beta-ol
-
-
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
-
TEI-5624, strong, highly specific inhibitor, prevents degradation of insoluble elastin by elastase
7-(4-chlorophenylsulfonyl-L-lysyl)amino-5-methyl-2-iso-propylamino-4H-3,1-benzoxazin-4-one
-
TEI-6344, strong, highly specific inhibitor, prevents degradation of insoluble elastin by elastase
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-amino-3-methoxy-1H-isochromen-1-one
-
-
7-amino-4-chloro-3-methoxy-1H-isochromen-1-one
-
-
7-chloro-2-(2-bromophenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
7-chloro-2-(2-chlorophenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
7-chloro-2-(2-fluorophenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
7-chloro-2-(2-methoxyphenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
7-chloro-2-(2-methylphenyl)-4H-benzo[d][1,3]oxazin-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
-
-
8-chloro-2-(2-bromophenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
8-chloro-2-(2-chlorophenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
8-chloro-2-(2-fluorophenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
8-chloro-2-(2-methoxyphenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
8-chloro-2-(2-methylphenyl)-4H-benzo[d][1,3]oxazin-4-one
-
-
Ac-Pro-Ala-Pro-NH2CH(CH3)CH2OH
-
-
Ac-Pro-Ala-Pro-NH2CH(CH3)CHO
-
-
Ac-Pro-Ala-Pro-NH2CH(CH3)CONH2
-
-
acetyl-Ala-Ala-Ala-Ala-CH2Cl
-
-
acetyl-Ala-Ala-Pro-Ala-CH2Cl
-
-
acetyl-Ala-Ala-Pro-Ile-CH2Cl
-
-
acetyl-Ala-Ala-Pro-Val-CH2Cl
-
-
Ala-Ala-Pro-Ala
-
-
alginate
-
weak inhibition, elastase molecule interacts with 19 uronic acid units of alginate
alpha-1-antichymotrypsin
-
-
-
alpha-1-antitrypsin
-
alpha-1-protease inhibitor
-
also called alpha-1-antitrypsin
-
alpha-ketobenzoxazoles
-
-
-
alpha1-antitrypsin
-
Alpha1-proteinase inhibitor
-
-
-
alpha2-Macroglobulin
-
-
-
antipain
-
-
Aprotinin
-
-
astragaloside IV
-
-
benzyl 3,3,3-trifluoro-1-isopropyl-2-oxopropylcarbamate
-
-
betulinic acid
-
-
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(3-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]propyl)phosphonate
-
-
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]pentyl)phosphonate
-
-
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]propyl)phosphonate
-
-
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-methylpropyl)phosphonate
-
-
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]butyl)phosphonate
-
-
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
-
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]propyl)phosphonate
-
-
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]-2-methylpropyl)phosphonate
-
-
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]pentyl)phosphonate
-
-
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]propyl)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(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
-
bis(4-tert-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]pentyl)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]ethyl)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
-
-
Boc-Ala-Pro-isobutyl-boronic acid amide
-
-
Butyric acid 3-(3-bromomethylene-6-isopropyl-5-oxo-[1,4]dioxan-2-yl)-pyrrolidin-1-yl 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]-, 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
-
-
CBZ-Ala-(isobutyl-difluoro-boron)amide
-
-
CBZ-Ala-isobutyl-boronic acid amide
-
-
ceftazidime
-
slight inhibition of purified elastase
cephalotin
-
IC50: 0.00025 mg/ml
CF3-CO-Ala-Ala-4-nitroanilide
-
-
CF3-CO-Ala-Ala-Ala-OH
-
-
chymostatin
-
-
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
cucurbitacin B
-
-
difluoro-beta-ketoamides
-
-
-
difluoromethyleneamines
-
-
-
diisopropyl phosphorofluoridate
-
-
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
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-methylbutyl)phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]butyl)phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]pentyl)phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]propyl)phosphonate
-
-
Eglin c
eglin-c
-
-
elafin
-
elasnin
-
-
elastase inhibitor III
-
-
-
Elastatinal
-
-
EPI-hNE-4
-
potent and specific inhibitor of neutrohil elastase
-
EPI-hNE4 (depelstat)
-
-
-
epigallocatechin gallate
-
-
ergosta-4,7,22-trien-3,6-dione
-
-
ergosta-7,22-dien-2beta,3alpha,9alpha-triol
-
-
ergosta-7,22-dien-3beta,5alpha,6beta,9alpha-tetraol
-
-
ergosterol
-
-
erythromycin
-
acts as an alternate substrate neutrophil elastase inhibitor
ethyl (2S,3R)-2-[(2,2-dihydroxyethyl)sulfonyl]-3-ethyl-4-oxoazetidine-1-carboxylate
-
-
ethyl 1-(1,3-benzodioxol-5-ylcarbonyl)-1H-indazole-3-carboxylate
-
-
ethyl 1-(phenylcarbonyl)-1H-indazole-3-carboxylate
-
-
ethyl 1-acetyl-1H-indazole-3-carboxylate
-
-
ethyl 1-[(2-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
ethyl 1-[(3-chlorophenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
ethyl 1-[(3-fluorophenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
ethyl 1-[(3-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
ethyl 1-[(4-chlorophenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
ethyl 1-[(4-fluorophenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
ethyl 1-[(4-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
ethyl [4-(3,3-diethyl-2,4-dioxoazetidin-1-yl)phenyl]acetate
-
-
flurythromycin
-
inactivator of neutrophil elastase
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
-
-
gentamycin
-
slight inhibition of purified elastase
ginsenoside Re
-
-
glutaryl-Ala-Ala-Pro-NH-C3H7
-
-
glycyrrhetinic acid
-
-
glycyrrhizin
-
-
gold thiomalate
-
inhibition is abolished by 1.0 M KCl
greglin
-
fast-acting and tight-binding inhibitor of neutrophil elastase
-
GW311616
-
-
GW311616A
-
-
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
GW475151
-
i.e. (3S,3aS,6aR)-3-isopropyl-1-methanesulfonyl-4-(2-pyrrolidin-1-ylmethyl-oxazole-4-carbonyl)hexahydro-pyrrolo-[3,2-b]pyrrol-2-one hydrochloride
heparin
horse leukocyte elastase inhibitor
-
protein with a molecular weight of 35200 Da that forms sodium dodecylsulfate-stable equimolar complexes with elastase
-
human monocyte/neutrophil elastase inhibitor
-
effective inhibition
-
ICI 200,355
-
-
ICI 219,680
-
-
insulapeptolide A
-
-
insulapeptolide B
-
-
insulapeptolide C
-
-
insulapeptolide D
-
-
insulapeptolide E
-
-
insulapeptolide F
-
-
insulapeptolide G
-
-
insulapeptolide H
-
-
Kunitz inhibitor
-
-
-
L-658758
-
-
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]-
-
-
leukocyte elastase inhibitor
-
leupeptin
-
-
long-chain fatty acids
-
-
lupeol
-
-
m-CF3-C6H4-CO-Ala-Ala-4-nitroanilide
-
-
matrix metalloproteinase-7
-
human leukocyte elastase cleaves matrix metalloproteinase-7 resulting in loss of enzymatic activity
-
MCoTI-II K10A
-
a MCoTI-II exchange analogue
MCoTI-II K10F
-
a MCoTI-II exchange analogue
MCoTI-II K10V
-
a MCoTI-II exchange analogue
MeOSuc-Ala-Ala-Pro-Val-chloromethylketone
-
neutrophil elastase-specific inhibitor
methoxsuccinyl-Ala-Ala-Pro-Ile-boronic acid
-
-
methoxysuccinyl-Ala-Ala-Pro-(isobutyl-4,4,5,5-tetramethyl-1,3,2-dioxaborolane)amide
-
-
methoxysuccinyl-Ala-Ala-Pro-isobutyl-boronic acid amide
-
-
methoxysuccinyl-Ala-Ala-Pro-phenylethylboronic acid
-
-
methoxysuccinyl-Ala-Ala-Pro-Val chloromethyl ketone
-
specific inhibitor
methoxysuccinyl-Ala-Ala-Pro-Val-CH2Cl
-
-
methoxysuccinyl-Ala-Ala-Pro-Val-chloromethylketone
-
-
monocyte/neutrophil elastase inhibitor
-
i.e. MNEI, a 42 kDA serpin protein
-
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-(2-phenylethyl)-1H-imidazole-1-carboxamide
-
-
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-(methoxysuccinyl)-Ala-Ala-Pro-Val-chloromethyl ketone
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
N-benzyl-1-(1,1,3-trioxo-1,3-dihydro-1lambda6-1,2-benzisothiazol-2-yl)-methanesulfonamide
-
-
N-galloyl-4-alkyliden-beta-lactam
-
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-Ala chloromethylketone
-
irreversible inhibitor
-
N-methoxysuccinyl-Ala-Ala-Pro-Val chloromethyl ketone
-
-
N-phenethyl-1-(1,1,3-trioxo-1,3-dihydro-1lambda6-1,2-benzisothiazol-2-yl)-methanesulfonamide
-
-
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
-
-
N-{1-[2-(2-{2-[(2-Chloro-acetyl)-isopropyl-amino]-acetyl}-pyrrolidin-1-yl)-1-methyl-2-oxo-ethylcarbamoyl]-ethyl}-succinamic acid
-
-
N-{1-[2-(2-{2-[(2-Chloro-acetyl)-isopropyl-amino]-acetyl}-pyrrolidin-1-yl)-1-methyl-2-oxo-ethylcarbamoyl]-ethyl}-succinamic acid methyl ester
-
-
N-{1-[2-(2-{2-[Isopropyl-(4-nitro-phenoxycarbonyl)-amino]-acetyl}-pyrrolidin-1-yl)-1-methyl-2-oxo-ethylcarbamoyl]-ethyl}-succinamic acid methyl ester
-
-
N-{2-[3-(trifluoromethyl)phenyl]ethyl}-1H-imidazole-1-carboxamide
-
-
N-{5-(Adamantane-1-sulfonylamino)-5-[1-(1-formyl-2-methyl-propylcarbamoyl)-ethylcarbamoyl]-pentyl}-4-dihydroxymethyl-benzamide
-
-
NaCl
-
1.0 M, 50% inhibition
nigranoic acid
-
significant inhibitory activity
oleanolic acid
-
-
oleic acid
-
-
oleoyl-Ala-Ala-Pro-Ala
-
-
oleoyl-Ala-Ala-Pro-Val
-
-
ONO-5046
-
-
ovomucoid
-
pancreatic secretory trypsin inhibitor
-
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
-
pefabloc
-
-
phenylboronic acid
-
-
phenylmethylsulfonyl fluoride
-
-
piefeltarraenin IA
-
-
polysaccharide sulfates
-
-
-
propan-2-yl 1-(phenylcarbonyl)-1H-indazole-3-carboxylate
-
-
propan-2-yl 1-(thiophen-3-ylcarbonyl)-1H-indazole-3-carboxylate
-
-
propan-2-yl 1-[(3-aminophenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
propan-2-yl 1-[(3-methoxyphenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
propan-2-yl 1-[(3-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
propolis
-
IC50: 0.002 mg dry weight per ml for ethyl acetate extract of propolis
-
propyl 1-(phenylcarbonyl)-1H-indazole-3-carboxylate
-
-
propyl 1-[(3-aminophenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
propyl 1-[(3-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
-
-
secretory leukocyte protease inhibitor
-
-
-
secretory leukoprotease inhibitor
-
-
-
secretory leukoproteinase inhibitor
-
important inhibitor of neutrophil elastase
-
semisynthetic glucan sulfates
-
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
-
serpin B1
-
-
-
serum leukocyte protease inhibitor
-
-
-
shionone
-
-
sivelestat
sivelestat sodium
-
neutrophil elastase specific inhibitor
sivelestat sodium hydrate
SSR69071
-
i.e. 2-(9-(2-piperidinoethoxy)-4-oxo-4H-pyrido[1,2-a]pyrimidin-2-yloxymethyl)-4-(1-methylethyl)-6-methoxy-1,2-benzisothiazol-3-one-1,1-dioxide, a selective, orally active, and potent inhibitor of leukocyte elastase with good penetration in respiratory tissues
succinyl-Ala-Ala-Pro-Val-CH2Cl
-
-
succinyl-Tyr-D-Leu-D-Val-4-nitroanilide
-
-
tert-butoxycarbonyl-Val-Val-Val-NH-(CH2)11-CH3
-
-
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
-
-
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
-
-
thieno[2,3-d]-1,3-oxazin-4-ones
-
-
thieno[2,3-d]-1,3-thioxazin-4-ones
-
-
thieno[3,2-d]-1,3-oxazin-4-ones
-
-
thieno[3,2-d]-1,3-thioxazin-4-ones
-
-
tobramycin
-
slight inhibition of purified elastase
toosendanin
-
-
tosyl-Lys-CH2Cl
-
weak
trappin-2
-
-
-
trifluoromethylketones
-
-
Trypsin inhibitor
-
ursolic acid
valinal
-
-
ZD0892
-
synthetic neutrophil elastase inhibitor
ZD8321
-
-
ZnSO4
-
-
[(4S)-5-benzyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-(4-benzoylphenyl)propanoate
-
-
[(4S)-5-benzyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-(4-phenoxyphenyl)propanoate
-
-
[(4S)-5-benzyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-(acetyloxy)benzoate
-
-
[(4S)-5-benzyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-hydroxybenzoate
-
-
[(4S)-5-benzyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-[4-(propan-2-yl)phenyl]propanoate
-
-
[(4S)-5-benzyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 3-phenylpropanoate
-
-
[(4S)-5-benzyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl phenylacetate
-
-
[(4S)-5-benzyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl [2-[(2,6-dichlorophenyl)amino]phenyl]acetate
-
-
[(4S)-5-methyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-(4-benzoylphenyl)propanoate
-
-
[(4S)-5-methyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-(4-phenoxyphenyl)propanoate
-
-
[(4S)-5-methyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-(acetyloxy)benzoate
-
-
[(4S)-5-methyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-hydroxybenzoate
-
-
[(4S)-5-methyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 2-[4-(propan-2-yl)phenyl]propanoate
-
-
[(4S)-5-methyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl 3-phenylpropanoate
-
-
[(4S)-5-methyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl phenylacetate
-
-
[(4S)-5-methyl-4-(2-methylpropyl)-1,1-dioxido-3-oxo-1,2,5-thiadiazolidin-2-yl]methyl [2-[(2,6-dichlorophenyl)amino]phenyl]acetate
-
-
[({(2R,3S)-3-ethyl-1-[(4-methylphenyl)sulfonyl]-4-oxoazetidin-2-yl}carbonyl)oxy]acetic acid
-
-
[6-Oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-2-(4-trifluoromethyl-phenyl)-1,6-dihydro-pyrimidin-5-yl]-carbamic acid benzyl ester
-
-
{(6R,7S)-2-[(tert-butylamino)carbonyl]-7-methoxy-5,5-dioxido-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-en-3-yl}methyl acetate
-
-
{1-[2-(1-Acetyl-2-methyl-propylcarbamoyl)-pyrrolidine-1-carbonyl]-2-methyl-propyl}-carbamic acid benzyl ester
-
-
{1-[2-(1-Aminooxalyl-2-methyl-propylcarbamoyl)-pyrrolidine-1-carbonyl]-2-methyl-propyl}-carbamic acid benzyl ester
-
-
{1-[2-(1-Formyl-2-methyl-propylcarbamoyl)-pyrrolidine-1-carbonyl]-2-methyl-propyl}-carbamic acid benzyl ester
-
-
{1-[2-(1-Isopropyl-2,3-dioxo-heptylcarbamoyl)-pyrrolidine-1-carbonyl]-2-methyl-propyl}-carbamic acid benzyl ester
-
-
{1-[2-(3,3-Difluoro-1-isopropyl-2,4-dioxo-7-phenyl-heptylcarbamoyl)-pyrrolidine-1-carbonyl]-2-methyl-propyl}-carbamic acid benzyl ester
-
-
{1-[2-(3-Benzylcarbamoyl-3,3-difluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidine-1-carbonyl]-2-methyl-propyl}-carbamic acid benzyl ester
-
-
{2-Methyl-1-[(R)-2-(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidine-1-carbonyl]-propyl}-carbamic acid benzyl ester
-
-
{2-Methyl-1-[(S)-2-(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidine-1-carbonyl]-propyl}-carbamic acid benzyl ester
-
-
{2-Methyl-1-[2-(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-pyrrolidine-1-carbonyl]-propyl}-carbamic acid benzyl ester
-
-
{2-Methyl-1-[2-(3,3,3-trifluoro-2-hydroxy-1-isopropyl-propylcarbamoyl)-pyrrolidine-1-carbonyl]-propyl}-carbamic acid benzyl ester
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
C5a
-
-
-
colistin
-
significant stimulation of purified elastase and elastase activity in sputum samples, able to reverse inhibition by heparin
erythromycin
-
significant stimulation of purified elastase
fMLP peptide
-
a tripeptide derived from bacterial wall
-
interleukin-8
-
-
-
lipopolysaccharide
-
-
N-Formyl-Met-Leu-Phe
-
a chemotactic peptide, stimulates the enzyme and its release from primary granules of PMN
tumour necrosis factor alpha
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31
acetyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 7.4, 37°C
0.016 - 0.022
benzyloxycarbonyl-Ala-3-hydroxy-5-phenylpyrrole
0.046 - 0.065
benzyloxycarbonyl-Ala-4-nitrophenol
0.001
heparin-antithrombin complex
-
pH 7.5, 37°C
-
0.833
methoxysuccinyl-Ala-Ala-Pro-Ala-4-nitroanilide
-
pH 7.4, 25°C
0.013
methoxysuccinyl-Ala-Ala-Pro-Ala-thiobenzyl ester
-
pH 7.4, 25°C
2.4
methoxysuccinyl-Ala-Ala-Pro-Met-4-nitroanilide
0.05 - 0.21
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
0.0023
methoxysuccinyl-Ala-Ala-Pro-Val-thiobenzyl ester
-
pH 7.4, 25°C
1.7
methoxysuccinyl-Ala-Ile-Pro-Met-4-nitroanilide
-
pH 7.4, 37°C
1.5
methoxysuccinyl-Ala-Pro-Ala-4-nitroanilide
-
pH 7.4, 25°C
0.012
methoxysuccinyl-Ala-Pro-Ala-thiobenzyl ester
-
pH 7.4, 25°C
0.189
methoxysuccinyl-Ala-Pro-Val-4-nitroanilide
-
pH 7.4, 25°C
0.0023
methoxysuccinyl-Ala-Pro-Val-thiobenzyl ester
-
pH 7.4, 25°C
0.696
methoxysuccinyl-Pro-Val-4-nitroanilide
-
pH 7.4, 25°C
0.012
methoxysuccinyl-Pro-Val-thiobenzyl ester
-
pH 7.4, 25°C
0.788
methoxysuccinyl-Val-4-nitroanilide
-
pH 7.4, 25°C
0.015
methoxysuccinyl-Val-thiobenzyl ester
-
pH 7.4, 25°C
0.06 - 5.02
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
1.1 - 3.7
N-succinyl-Ala-Ala-Ala 4-nitroanilide
0.0184
o-aminobenzoic acid-Ala-Pro-Glu-Glu-Ile-Met-Asp-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.0086
o-aminobenzoic acid-Val-Ala-Asp-Cys-Ala-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
-
0.016 - 0.08
tosyl-Ala-3-hydroxy-5-phenylpyrrole
0.028 - 0.035
tosyl-Ala-4-nitrophenol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.1
acetyl-Ala-Ala-Pro-Val-4-nitroanilide
-
pH 7.4, 37°C
16 - 20
benzyloxycarbonyl-Ala-3-hydroxy-5-phenylpyrrole
28 - 46
benzyloxycarbonyl-Ala-4-nitrophenol
3.33
heparin-antithrombin complex
-
pH 7.5, 37°C
-
22
methoxysuccinyl-Ala-Ala-Pro-Ala-4-nitroanilide
-
pH 7.4, 25°C
52
methoxysuccinyl-Ala-Ala-Pro-Ala-thiobenzyl ester
-
pH 7.4, 25°C
21
methoxysuccinyl-Ala-Ala-Pro-alpha-aminobutyryl-4-nitroanilide
-
pH 7.4, 25°C
0.72
methoxysuccinyl-Ala-Ala-Pro-Met-4-nitroanilide
10 - 23
methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
13
methoxysuccinyl-Ala-Ala-Pro-Val-thiobenzyl ester
-
pH 7.4, 25°C
6.8
methoxysuccinyl-Ala-Ile-Pro-Met-4-nitroanilide
-
pH 7.4, 37°C
7
methoxysuccinyl-Ala-Pro-Ala-4-nitroanilide
-
pH 7.4, 25°C
46
methoxysuccinyl-Ala-Pro-Ala-thiobenzyl ester
-
pH 7.4, 25°C
10
methoxysuccinyl-Ala-Pro-Val-4-nitroanilide
-
pH 7.4, 25°C
13
methoxysuccinyl-Ala-Pro-Val-thiobenzyl ester
-
pH 7.4, 25°C
0.04
methoxysuccinyl-Pro-Val-4-nitroanilide
-
pH 7.4, 25°C
10
methoxysuccinyl-Pro-Val-thiobenzyl ester
-
pH 7.4, 25°C
0.06
methoxysuccinyl-Val-4-nitroanilide
-
pH 7.4, 25°C
11
methoxysuccinyl-Val-thiobenzyl ester
-
pH 7.4, 25°C
2.42 - 63.11
N-methoxysuccinyl-Ala-Ala-Pro-Val-4-nitroanilide
0.7 - 2.1
N-succinyl-Ala-Ala-Ala 4-nitroanilide
3.1
N-succinyl-Ala-Ala-Val 4-nitroanilide
-
pH 7.5, 25°C, proteinase 2A
96 - 4800
tosyl-Ala-3-hydroxy-5-phenylpyrrole
120
tosyl-Ala-4-nitrophenol
-
pH 7.0 and pH 8.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000072
(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
-
-
0.00002
(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
-
-
0.0000036
(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
-
-
0.000018
(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
-
-
0.000009 - 0.000101
(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
0.0000081
(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
-
-
0.000017
(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
-
-
0.000057
(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
-
-
0.00017
(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
-
-
0.0000082
(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
-
-
0.0000066
(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
-
-
0.000033
(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
-
-
0.000043
(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
-
-
0.01634
(E)-3-(3-(3,7-dimethylocta-2,6-dienyl)-2,4-dihydroxyphenyl)-3,5,7-trihydroxy-chroman-4-one
-
at pH 8.0, temperature not specified in the publication
0.0000067
(S)-1-[(S)-2-(4-methoxybenzamido)-3-methylbutyryl]-N-[(S)-2-methyl-1-(trifluoroacetyl)propyl]pyrrolidine-2-carboxamide
-
-
0.000015
1(6H)-Pyrimidineacetamide, 2-(4-aminophenyl)-5-[(methylsulfonyl)amino]-6-oxo-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
0.000046
1(6H)-Pyrimidineacetamide, 2-(4-fluorophenyl)-5-(methylamino)-6-oxo-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
0.000026
1(6H)-Pyrimidineacetamide, 5-(ethylamino)-6-oxo-2-(2-thienyl)-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
0.0001
1(6H)-Pyrimidineacetamide, 5-(formylamino)-6-oxo-2-(2-thienyl)-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
0.0000049
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)-
-
-
0.0000016 - 0.0000077
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-
0.000094
1(6H)-Pyrimidineacetamide, 6-oxo-2-phenyl-5-[(trifluoroacetyl)amino]-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
0.00000574
1,2,5-thiadiazolidin-3-one 1,1-dioxide
-
-
0.000004
1-methyl-1H-tetrazole-5-thiol
-
-
0.00052
2-(5-amino-6-oxo-2-thien-2-ylpyrimidin-1(6H)-yl)-N-(3,3,3-trifluoro-1-isopropyl-2-oxopropyl)acetamide
-
-
0.000127 - 0.00138
2-(thiophen-2-ylcarbonylthio)-N-(2-oxo-2,3,4,5-tetrahydrothiophen-3-yl)propionamide
0.0015
2-chloro-4-(1-hydroxyoctadecyl)benzoic acid
-
pH 8.0, 30°C
0.0000016
2-[2-(4-fluorophenyl)-6-oxo-5-[(cyclohexylsulfamoyl)-amino]-1,6-dihydro-1-pyrimidinyl]-N-(3,3,3-trifluoro-1-isopropyl-2-oxopropyl)acetamide
-
pH 7.4
0.00027
2-[5-amino-2-(3,5-difluorophenyl)-6-oxopyrimidin-1(6H)-yl]-N-(3,3,3-trifluoro-1-isopropyl-2-oxopropyl)acetamide
-
-
0.0000062 - 0.000052
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
0.000011
2-[5-[(benzyloxycarbonyl)amino]-6-oxo-2-(2-thienyl)-1,6-dihydro-1-pyrimidinyl]-N-(3,3,3-trifluoro-1-isopropyl-2-oxopropyl)acetamide
-
pH 7.4
0.0000006
4-(4-bromophenylsulfonylcarbamoyl)benzoyl-L-valyl-L-proline 1 (RS)-(1-trifluoroacetyl-2-methylpropyl)amide
-
-
0.000025
6-amino-2-(2,2,2-trifluoro-acetylamino)-hexanoic acid [1-(4-trifluoromethyl-phenylcarbamoyl)-ethyl]-amide
-
-
0.000007
7-(4-chlorophenylsulfonyl-L-glutamyl)amino-5-methyl-2-iso-propylamino-4H-3,1-benzoxazin-4-one
-
pH 7.5, 37°C
0.000016
7-(4-chlorophenylsulfonyl-L-lysyl)amino-5-methyl-2-iso-propylamino-4H-3,1-benzoxazin-4-one
-
pH 7.5, 37°C
0.0000018
Ala15-reactive site variant of aprotinin
-
pH 7.4, 25°C
-
0.0000002 - 0.00037
alpha-aminobutyric acid15-reactive site variant of aprotinin
-
0.0000002 - 0.00022
alpha-aminovaleric acid15-reactive site variant of aprotinin
-
0.000027
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
-
-
0.000043
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
-
-
0.000042
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
-
-
0.00004
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
-
-
0.00000096
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
-
-
0.000022
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
-
-
0.000023
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
-
-
0.000016
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
-
-
0.000023
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
-
-
0.025
CF3-CO-Ala-Ala-4-nitroanilide
-
-
0.17
CF3-CO-Ala-Ala-Ala
-
-
0.000000075
Eglin c
-
pH 7.3, 37°C
0.00000008 - 0.0000067
elafin
-
0.4
glutaryl-Ala-Ala-Pro-NH-C3H7
-
-
0.00000031
GW311616
-
pH 7.4, 30°C
0.000000014
GW447631
-
pH 7.4, 30°C
0.00000173
GW469002
-
pH 7.4, 30°C
0.00000016
GW475151
-
pH 7.4, 30°C
1.8
H-Ala-Ala-Pro-Ala-OH
-
-
0.00003 - 0.00015
heparin
-
low molecular weight and semi-synthetic heparin samples, inhibition kinetics
0.000036
insulapeptolide D
-
in 50 mM sodium phosphate buffer (100 mM NaCl, pH 7.8), at 25°C
0.000058
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1R)-3,3-difluoro-1-(1-methylethyl)-2,4-dioxo-4-[(2-pyridinylmethyl)amino]butyl]-
-
-
0.0000031
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-3,3-difluoro-1-(1-methylethyl)-2,4-dioxo-4-[(2-pyridinylmethyl)amino]butyl]-
-
-
0.00000035
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-3,3-difluoro-1-(1-methylethyl)-2-oxo-4-[(phenylmethyl)amino]butyl]-
-
-
0.0000038
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-3,3-difluoro-4-(methylamino)-1-(1-methylethyl)-2,4-dioxobutyl]-
-
-
0.0000064
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-4-(benzoylamino)-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
0.000015
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-4-amino-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
0.0000034
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[(1S)-4-[[(1,1-dimethylethoxy)carbonyl]amino]-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
0.0000033
L-Prolinamide, N-(4-methoxybenzoyl)-L-valyl-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
0.0000017
L-Prolinamide, N-(phenoxycarbonyl)-L-valyl-N-[(1S)-3,3-difluoro-1-(1-methylethyl)-2,4-dioxo-4-[(2-pyridinylmethyl)amino]butyl]-
-
-
0.00000085
L-Prolinamide, N-(phenoxycarbonyl)-L-valyl-N-[(1S)-3,3-difluoro-4-(methylamino)-1-(1-methylethyl)-2,4-dioxobutyl]-
-
-
0.00000035
L-Prolinamide, N-(phenoxycarbonyl)-L-valyl-N-[(1S)-4-[[(1,1-dimethylethoxy)carbonyl]amino]-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
0.0000015
L-Prolinamide, N-(phenoxycarbonyl)-L-valyl-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
0.0000016
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-3,3-difluoro-1-(1-methylethyl)-2-oxo-4-[(phenylmethyl)amino]butyl]-
-
-
0.000003
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-3,3-difluoro-4-(methylamino)-1-(1-methylethyl)-2,4-dioxobutyl]-
-
-
0.00000038
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-4-amino-3,3-difluoro-1-(1-methylethyl)-2,4-dioxobutyl]-
-
-
0.00013
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-4-amino-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
0.0000011
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[(1S)-4-[[(1,1-dimethylethoxy)carbonyl]amino]-3,3-difluoro-1-(1-methylethyl)-2-oxobutyl]-
-
-
0.0000026
L-Prolinamide, N-[(phenylmethoxy)carbonyl]-L-valyl-N-[3,3,3-trifluoro-1-(1-methylethyl)-2-oxopropyl]-
-
-
0.004
m-CF3-C6H4-CO-Ala-Ala-4-nitroanilide
-
-
0.000032
MCoTI-II K10A
-
pH not specified in the publication, temperature not specified in the publication
0.0075
MCoTI-II K10F
-
pH not specified in the publication, temperature not specified in the publication
0.000021
MCoTI-II K10V
-
pH not specified in the publication, temperature not specified in the publication
0.06
N-(1-(1-[1-(4-benzoyl-phenylcarbamoyl)-2-methyl-propylcarbamoyl]-3-methyl-butylcarbamoyl)-2-(4-hydroxy-phenyl)-ethyl)-succinamic acid
-
-
0.00011
N-(5-(adamantane-1-sulfonylamino)-5-[1-(1-formyl-2-methyl-propylcarbamoyl)-ethylcarbamoyl]-pentyl)-succinamic acid
-
-
0.00006
N-(5-(adamantane-1-sulfonylamino)-5-[1-(1-formyl-2-methyl-propylcarbamoyl)-ethylcarbamoyl]-pentyl)-terephthalamic acid
-
-
0.000035
N-(5-benzyloxycarbonylamino-1-(1-[2-(1-formyl-2-methyl-propylcarbamoyl)-pyrrolidine-1-carbonyl]-2-methyl-propylcarbamoyl)-pentyl)-succinamic acid
-
-
0.0007
N-galloyl-4-alkyliden-beta-lactam
-
-
0.009
oleic acid
-
-
0.00007 - 0.0058
oleoyl-Ala-Ala-Pro-Ala
0.004
oleoyl-Ala-Ala-Pro-Val
-
-
0.00000027
Pro44-eglin c
-
-
-
0.000058
semisynthetic glucan sulfate LMWH
-
37°C
-
0.0000185
semisynthetic glucan sulfate PPS
-
37°C
-
0.0000132
semisynthetic glucan sulfate PS3
-
37°C
-
0.000012
semisynthetic glucan sulfate PulS1
-
37°C
-
0.0000215
semisynthetic glucan sulfate PulS2
-
37°C
-
0.000036
semisynthetic glucan sulfate PulS3
-
37°C
-
0.000044
semisynthetic glucan sulfate PulS4
-
37°C
-
0.0000034
semisynthetic glucan sulfate PulS5
-
37°C
-
0.000001
semisynthetic glucan sulfate PulS6
-
37°C
-
0.0000008
semisynthetic glucan sulfate PulS7
-
37°C
-
0.0000056
semisynthetic glucan sulfate UFH
-
37°C
-
0.0000000168
SSR69071
-
pH 7.8
0.12
succinyl-Tyr-D-Leu-D-Val-4-nitroanilide
-
-
0.0000022
synthetic trihexacontapeptide corresponding to the sequence 8-70 of eglin c
-
-
-
0.00021
tert-butoxycarbonyl-Val-Val-Val-NH-(CH2)11-CH3
-
-
0.00000003
trappin-2
-
neutrophil elastase
-
0.0000003
Val15-aminobutyric acid15-reactive site variant of aprotinin
-
pH 7.4, 25°C
-
0.000004 - 0.00012
Val15-reactive site variant of aprotinin
-
0.000005571
ZD8321
-
pH 7.8
0.000042
[6-Oxo-1-[(3,3,3-trifluoro-1-isopropyl-2-oxo-propylcarbamoyl)-methyl]-2-(4-trifluoromethyl-phenyl)-1,6-dihydro-pyrimidin-5-yl]-carbamic acid benzyl ester
-
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0128
(-)-epigallocatechin-3-gallate
Homo sapiens
-
pH 7.5, 37°C
0.1
(22E,24R)-ergosta-7,22-dien-2alpha,3alpha,9alpha-triol
Homo sapiens
-
IC50 above 0.1 mM, pH 7.5, 37°C
0.0179
(2R, 3R)-6-methyl-3'-geranyl-2,3-trans-5,7,4'-trihydroxyflavonol
Homo sapiens
-
at pH 8.0, temperature not specified in the publication
0.022
(3-methylindazol-1-yl)-m-tolyl-methanone
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.1
(3beta,5alpha,8alpha,22E)-ergosta-6,22-diene-3-ol-5,8-peroxide
Homo sapiens
-
IC50 above 0.1 mM, pH 7.5, 37°C
0.1
(3beta,5alpha,8alpha,22E)-ergosta-6,22-diene-3-ol-5,8-peroxide 3-O-beta-D-glucoside
Homo sapiens
-
IC50 above 0.1 mM, pH 7.5, 37°C
0.000025
(3R)-1-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-3-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.000019
(3S)-1-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-3-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.0085
(E)-3-(3-(3,7-dimethylocta-2,6-dienyl)-2,4-dihydroxyphenyl)-3,5,7-trihydroxy-chroman-4-one
Homo sapiens
-
at pH 8.0, temperature not specified in the publication
0.1
(E)-6-O-p-coumaroyl scandoside methyl ester
Homo sapiens
-
pH 7.5, 37°C, above
0.1
(E)-6-O-p-feruloyl scandoside methyl ester
Homo sapiens
-
pH 7.5, 37°C, above
0.018
(E)-6-O-p-methoxycinnamoyl scandoside methyl ester
Homo sapiens
-
pH 7.5, 37°C
0.1
(Z)-6-O-p-coumaroyl scandoside methyl ester
Homo sapiens
-
pH 7.5, 37°C, above
0.1
(Z)-6-O-p-methoxycinnamoyl scandoside methyl ester
Homo sapiens
-
pH 7.5, 37°C, above
0.034
1-(2-methylbenzoyl)-1H-indazole-3-carboxylic acid phenylamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0016
1-(3-aminobenzoyl)-1H-indazole-3-carboxylic acid ethyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0031
1-(3-aminobenzoyl)-1H-indazole-3-carboxylic acid phenylamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0008
1-(3-methoxybenzoyl)-1H-indazole-3-carboxylic acid ethyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00055
1-(3-methoxybenzoyl)-1H-indazole-3-carboxylic acid methyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0018
1-(3-methoxybenzoyl)-1H-indazole-3-carboxylic acid phenylamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0019
1-(3-methoxybenzoyl)-1H-indazole-3-carboxylic acid propyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00013
1-(3-methylbenzoyl)-1H-indazole-3-carboxylic acid methyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.038
1-(4-cyanobenzoyl)-1H-indazole-3-carboxylic acid ethyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00093
1-(thiophene-3-carbonyl)-1H-indazole-3-carboxylic acid ethyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00031
1-(thiophene-3-carbonyl)-1H-indazole-3-carboxylic acid methyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0031
1-(thiophene-3-carbonyl)-1H-indazole-3-carboxylic acid phenylamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0019
1-(thiophene-3-carbonyl)-1H-indazole-3-carboxylic acid propyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.000089
1-benzoyl-1H-indazole-3-carboxylic acid methyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00042
1-benzoyl-1H-indazole-3-carboxylic acid phenylamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00018
1-butyryl-1H-indazole-3-carboxylic acid ethyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00048
1-cyclopentanecarbonyl-1H-indazole-3-carboxylic acid ethyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0004
1-propionyl-1H-indazole-3-carboxylic acid ethyl ester
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0039
1-[(3-chlorophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0059
1-[(3-fluorophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0093
1-[(3-methylphenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.011
1-[(3-nitrophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0061
1-[(4-chlorophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.038
1-[(4-cyanophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0081
1-[(4-fluorophenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.029
1-[(4-methylphenyl)carbonyl]-N-phenyl-1H-indazole-3-carboxamide
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0013
1-[3-(5-cyclobutyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.00014
1-[3-(5-cyclopropyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.0407
1-[3-(5-ethyl-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.000028
1-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.000079
1-[3-(5-methyl-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.00018
1-[3-(7-methoxy-4-oxo-5-propyl-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperidine-4-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.00033
1-[3-[7-methoxy-4-oxo-5-(propan-2-yl)-4H-3,1-benzoxazin-2-yl]pyridin-2-yl]piperidine-4-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.0205
14alpha-hydroxy-ergosta-4,7,9(11),22-tetraen-3,6-dione
Homo sapiens
-
pH 7.5, 37°C
0.01
1H-indazol-1-yl(3-methylphenyl)methanone
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00026
2,2,2-trifluoroethyl 1-(phenylcarbonyl)-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00051
2,2,2-trifluoroethyl 1-(thiophen-3-ylcarbonyl)-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00034
2,2,2-trifluoroethyl 1-[(3-aminophenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00089
2,2,2-trifluoroethyl 1-[(3-methoxyphenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00046
2,2,2-trifluoroethyl 1-[(3-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.000085
2-(2-methoxypyridin-3-yl)-5-methyl-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.0093
2-(2-phenoxypyridin-3-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000021
2-(2-[4-[2-(dimethylamino)ethyl]piperazin-1-yl]pyridin-3-yl)-5-ethyl-7-methoxy-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00011
2-(2-[[2-(dimethylamino)ethyl](methyl)amino]pyridin-3-yl)-5-methyl-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.0081
2-(2-[[2-(dimethylamino)ethyl]amino]pyridin-3-yl)-5-methyl-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000064
2-[2-(1H-imidazol-1-yl)pyridin-3-yl]-5-methyl-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000027
2-[2-(4-butylpiperazin-1-yl)pyridin-3-yl]-5-ethyl-7-methoxy-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000034
2-[2-(4-cyclopentylpiperazin-1-yl)pyridin-3-yl]-5-ethyl-7-methoxy-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000028
2-[2-[4-(cyclopropylmethyl)piperazin-1-yl]pyridin-3-yl]-5-ethyl-7-methoxy-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.0308
3'-geranyl-5,7,2',4'-tetrahydroxyisoflavanone
Homo sapiens
-
at pH 8.0, temperature not specified in the publication
0.000024
3-[4-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperazin-1-yl]propanenitrile
Homo sapiens
-
pH 7.4, 22°C
0.1
3beta,5alpha,9alpha-trihydroxy-ergosta-7,22-dien-6-one
Homo sapiens
-
IC50 above 0.1 mM, pH 7.5, 37°C
0.0146
3beta,5alpha-dihydroxy-6beta-methoxyergosta-7,22-diene
Homo sapiens
-
pH 7.5, 37°C
0.1
3beta,5alpha-dihydroxy-ergosta-7,22-dien-6-one
Homo sapiens
-
IC50 above 0.1 mM, pH 7.5, 37°C
0.1
3beta-hydroxy-ergosta-7,22-dien-6-one
Homo sapiens
-
IC50 above 0.1 mM, pH 7.5, 37°C
0.000016
4-(4-bromophenylsulfonylcarbamoyl)benzoyl-L-valyl-L-proline 1 (RS)-(1-trifluoroacetyl-2-methylpropyl)amide
Homo sapiens
-
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
0.000023
4-[3-(5-ethyl-7-methoxy-4-oxo-4H-3,1-benzoxazin-2-yl)pyridin-2-yl]piperazine-1-carboxylic acid
Homo sapiens
-
pH 7.4, 22°C
0.0234
5-chloro-2-(2-chlorophenyl)-4H-benzo[d][1,3]oxazin-4-one
Homo sapiens
-
pH 7.4, 25°C
0.00121
5-chloro-2-(2-fluorophenyl)-4H-benzo[d][1,3]oxazin-4-one
Homo sapiens
-
pH 7.4, 25°C
0.00648
5-chloro-2-(2-methoxyphenyl)-4H-benzo[d][1,3]oxazin-4-one
Homo sapiens
-
pH 7.4, 25°C
0.00016
5-chloro-2-(2-phenoxypyridin-3-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00015
5-cyclobutyl-7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00085
5-cyclobutyl-7-methoxy-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00012
5-cyclopropyl-7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00011
5-cyclopropyl-7-methoxy-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.04055
5-ethyl-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.04067
5-ethyl-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000016
5-ethyl-2-[2-[4-(2-hydroxyethyl)piperazin-1-yl]pyridin-3-yl]-7-methoxy-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000022
5-ethyl-7-methoxy-2-(2-[4-[2-(morpholin-4-yl)ethyl]piperazin-1-yl]pyridin-3-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00002
5-ethyl-7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000028
5-ethyl-7-methoxy-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000016
5-ethyl-7-methoxy-2-[2-[4-(2-methoxyethyl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000021
5-ethyl-7-methoxy-2-[2-[4-(2-methylpropyl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00039
5-methoxy-2-(2-phenoxypyridin-3-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000087
5-methyl-2-(2-methylpyridin-3-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00017
5-methyl-2-(2-phenoxyphenyl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000061
5-methyl-2-(2-phenoxypyridin-3-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.006
5-methyl-2-(2-[[2-(morpholin-4-yl)ethyl]amino]pyridin-3-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00071
5-methyl-2-(6-methylpyridin-3-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.0009
5-methyl-2-(pyridin-3-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00093
5-methyl-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000074
5-methyl-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.000015
5-tert-butyl-7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.0352
5alpha,6alpha,8alpha,9alpha-diepoxy-ergost-22-en-3beta,7alpha-diol
Homo sapiens
-
pH 7.5, 37°C
0.0282
5alpha,6alpha-epoxy-ergosta-8(14),22-diene-3beta,7alpha-diol
Homo sapiens
-
pH 7.5, 37°C
0.0751
5alpha,6alpha-epoxy-ergosta-8(9),22-dien-7-one-3beta-ol
Homo sapiens
-
pH 7.5, 37°C
0.0053
7-(dimethylamino)-5-ethyl-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.0026
7-(dimethylamino)-5-ethyl-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.002
7-chloro-2-(2-bromophenyl)-4H-benzo[d][1,3]oxazin-4-one
Homo sapiens
-
pH 7.4, 25°C
0.00268
7-chloro-2-(2-chlorophenyl)-4H-benzo[d][1,3]oxazin-4-one
Homo sapiens
-
pH 7.4, 25°C
0.00138
7-chloro-2-(2-fluorophenyl)-4H-benzo[d][1,3]oxazin-4-one
Homo sapiens
-
pH 7.4, 25°C
0.00021
7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-5-(propan-2-yl)-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00025
7-methoxy-2-[2-(4-methylpiperazin-1-yl)pyridin-3-yl]-5-propyl-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.00014
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
Homo sapiens
-
pH 7.4, 22°C
0.000071
7-methoxy-2-[2-[4-(1-methylpiperidin-4-yl)piperazin-1-yl]pyridin-3-yl]-5-propyl-4H-3,1-benzoxazin-4-one
Homo sapiens
-
pH 7.4, 22°C
0.0178
clitocybin D
Homo sapiens
-
pH 7.5, 37°C
0.0552
ergosta-4,7,22-trien-3,6-dione
Homo sapiens
-
pH 7.5, 37°C
0.1
ergosta-7,22-dien-2beta,3alpha,9alpha-triol
Homo sapiens
-
IC50 above 0.1 mM, pH 7.5, 37°C
0.0775
ergosta-7,22-dien-3beta,5alpha,6beta,9alpha-tetraol
Homo sapiens
-
pH 7.5, 37°C
0.0645
ergosterol
Homo sapiens
-
pH 7.5, 37°C
0.028
ethyl 1-(1,3-benzodioxol-5-ylcarbonyl)-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0004
ethyl 1-(phenylcarbonyl)-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0048
ethyl 1-acetyl-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.052
ethyl 1-[(2-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0017
ethyl 1-[(3-chlorophenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0017
ethyl 1-[(3-fluorophenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00041
ethyl 1-[(3-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.019
ethyl 1-[(4-chlorophenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0057
ethyl 1-[(4-fluorophenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.036
ethyl 1-[(4-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00014
insulapeptolide A
Homo sapiens
-
in 50 mM sodium phosphate buffer (100 mM NaCl, pH 7.8), at 25°C
0.0001
insulapeptolide B
Homo sapiens
-
in 50 mM sodium phosphate buffer (100 mM NaCl, pH 7.8), at 25°C
0.00009
insulapeptolide C
Homo sapiens
-
in 50 mM sodium phosphate buffer (100 mM NaCl, pH 7.8), at 25°C
0.000085
insulapeptolide D
Homo sapiens
-
in 50 mM sodium phosphate buffer (100 mM NaCl, pH 7.8), at 25°C
0.0032
insulapeptolide E
Homo sapiens
-
in 50 mM sodium phosphate buffer (100 mM NaCl, pH 7.8), at 25°C
0.0016
insulapeptolide F
Homo sapiens
-
in 50 mM sodium phosphate buffer (100 mM NaCl, pH 7.8), at 25°C
0.0035
insulapeptolide G
Homo sapiens
-
in 50 mM sodium phosphate buffer (100 mM NaCl, pH 7.8), at 25°C
0.0027
insulapeptolide H
Homo sapiens
-
in 50 mM sodium phosphate buffer (100 mM NaCl, pH 7.8), at 25°C
0.001 - 0.002
N-galloyl-4-alkyliden-beta-lactam
Homo sapiens
-
-
0.00377
nigranoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.02168
oleanolic acid
Homo sapiens
-
at pH 8.0, temperature not specified in the publication
0.00024
propan-2-yl 1-(phenylcarbonyl)-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00069
propan-2-yl 1-(thiophen-3-ylcarbonyl)-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00051
propan-2-yl 1-[(3-aminophenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00076
propan-2-yl 1-[(3-methoxyphenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00065
propan-2-yl 1-[(3-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0004
propyl 1-(phenylcarbonyl)-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0007
propyl 1-[(3-aminophenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.00078
propyl 1-[(3-methylphenyl)carbonyl]-1H-indazole-3-carboxylate
Homo sapiens
-
in 200 mM Tris-HCl, pH 7.5, at 25°C
0.0000181
semisynthetic glucan sulfates
Homo sapiens
-
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
-
0.00551 - 0.0337
ursolic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1804
-
-
875
-
substrate N-succinyl-Ala-Ala-Ala-4-nitroanilide
additional information
-
enzyme activity in crevicular fluid before tooth extraction and after early and later type-I loading of implants, diverse samples, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7.6
-
assay at
8
-
assay at
8.2 - 9.2
-
hydrolysis of azocasein or benzyloxycarbonyl-L-Ala 2-naphthyl ester
8.6
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH 6.0: about 50% of maximal activity, pH 9.0: about 95% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
23
-
assay at
25
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
-
isoelectric focusing, leukocyte elastase
8.77 - 9.15
-
-
9.3
-
isoelectric focusing, leukocyte elastase in complex with Pro44-eglin c
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
primary lung cancer
Manually annotated by BRENDA team
-
neutrophil elastase exists in high concentrations (0.001-0.02 mM) in airway secretions of patiens with chronic inflammatory airway diseases and induces overproduction of MUC5AC mucin
Manually annotated by BRENDA team
-
small amounts of the enzyme are expressed by T-lymphocytes
Manually annotated by BRENDA team
-
leukocyte elastase-alpha1 protease inhibitor complex, quantitative determination, overview
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
of activated neutrophils
Manually annotated by BRENDA team
-
predominantly
Manually annotated by BRENDA team
-
of polymorphonuclear neutrophils, mechanism of binding, inhibited by trypsin, chondroitinase ABC, and heparitinases, but not other glycanases, and purified chondroitin sulfates, heparan sulfate, and other sulfated molecules, but not with non-sulfated glycans, overview
Manually annotated by BRENDA team
-
neutrophil granule
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
human neutrophil elastase plays an important role in cell signaling and represents an regulator of the inflammatory response
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ELNE_HUMAN
267
1
28518
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28520
unprocessed precursor consists of 267 amino acid residues
30000
x * 30000
24000
-
SDS-PAGE
29000
-
x * 29000, SDS-PAGE
30000
-
x * 30000, SDS-PAGE
34400
-
x * 34400, SDS-PAGE
34970
-
x * 34970, calculation from amino acid composition
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, 2.3 A crystal structure of leukocyte elastase in a complex with methoxysuccinyl-Ala-Ala-Pro-Val-chloromethyl ketone
complex of the enzyme with methoxysuccinyl-Ala-Ala-Pro-Ala chloromethyl ketone. The asymmetric distribution of positively charged residues on the surface of the enzyme suggests a mechanism for the specific incorporation of the enzyme into primary granules in the neutrophil
in complex with 1a, sitting drop vapor diffusion method, using 20% (w/v) PEG MME 5000, 0.2 M sodium sulfate
in complex with dihydropyrimidone inhibitor, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M ammonium citrate (pH 5.0) or uncomplexed enzyme, sitting drop vapor diffusion method, using 1.9 M ammonium sulfate, 5% (w/v) PEG 400, 0.1 M 4-morpholine ethanesulfonic acid/NaOH (pH 6.5), and 20% (v/v) glycerol
X-ray crystal structure of the complex of human leukocyte elastase and the third domain of the turkey ovomucoid inhibitor
crystallized in complex with Pro44-eglin c, hanging drop vapour diffusion method using polyethylene glycol 4000 as the precipitating agent
-
hanging drop vapour diffusion method
-
hanging drop vapour diffusion method, using 0.1 M HEPES (pH 7.5) and 20% PEG8000 or in 0.1 M HEPES (pH 7.5) and 35% PEG8000 containing 10 mM N-methoxysuccinyl-Ala-Ala-Pro-Val chloromethyl ketone inhibitor
-
in complex with the recombinant C-terminal domain of secretory leukocyte protease inhibitor (Arg58Ala107), sitting drop vapour diffusion method, using 2.0 M Na-formate at pH 4.5
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A127P
a naturally occuring disease causing mutation, the mutation increase beta-aggregation propensity in the enzyme
A57T
a naturally occuring disease causing mutation, the mutation causes loss of stability and affects enzyme stability
C151S
a naturally occuring disease causing mutation, the mutation causes loss of stability
C151Y
a naturally occuring disease causing mutation, the mutation causes loss of stability
C71R
a naturally occuring disease causing mutation, the mutation causes loss of stability
C71S
a naturally occuring disease causing mutation, the mutation causes loss of stability
G210V
a naturally occuring disease causing mutation, the mutation increase beta-aggregation propensity in the enzyme
G214R
a naturally occuring disease causing mutation, the mutation affects enzyme stability
G85E
a naturally occuring disease causing mutation, the mutation causes loss of stability
H53L
a naturally occuring disease causing mutation, the mutation increase beta-aggregation propensity in the enzyme
I60T
a naturally occuring disease causing mutation, the mutation causes loss of stability
L121P
a naturally occuring disease causing mutation, the mutation causes loss of stability and affects enzyme stability
L152P
a naturally occuring disease causing mutation, the mutation causes loss of stability and affects enzyme stability
L47P
a naturally occuring disease causing mutation, the mutation causes loss of stability and affects enzyme stability
L84P
a naturally occuring disease causing mutation, the mutation causes loss of stability
P205R
a naturally occuring disease causing mutation, the mutation causes loss of stability
P42L
a naturally occuring disease causing mutation, the mutation increase beta-aggregation propensity in the enzyme
R220Q
a naturally occuring disease causing mutation, the mutation causes loss of stability
R81P
a naturally occuring disease causing mutation, the mutation causes loss of stability and affects enzyme stability
S46F
a naturally occuring disease causing mutation, the mutation causes loss of stability and affects enzyme stability, and the mutation increase beta-aggregation propensity in the enzyme
V101M
a naturally occuring disease causing mutation, the mutation affects enzyme stability
V82M
a naturally occuring disease causing mutation, the mutation causes loss of stability and affects enzyme stability
A213V
-
the mutant shows increased kcat and Km values compared to the wild type enzyme
down
-
severe congenital neutropenia is a heterogeneous disorder of myelopoiesis, which follows an autosomal dominant or autosomal recessive pattern of inheritance, and leads to suppression of neutrophil elastase and reduced enzyme protein levels in plasma
F192A
-
the mutant shows increased kcat and Km values compared to the wild type enzyme
F192K
-
the mutant shows increased kcat and Km values compared to the wild type enzyme
F215A
-
very low activity, the mutant shows decreased kcat and increased Km values compared to the wild type enzyme
F215Y
-
the mutant shows decreased kcat and Km values compared to the wild type enzyme
G185R
N95A/N144A
-
the neutrophil elastase glycosylation variant is located in the nucleus
N98T
-
the mutant shows increased kcat and Km values compared to the wild type enzyme
S97L
-
the mutation is associated with cyclic neutropenia
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
-
90 min, denaturation in presence of 1% SDS, 0.04 M dithiothreitol, 0.001 M EDTA
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DMSO
-
1% (v/v) DMSO has no effect on enzyme activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.5 M pyridine acetate buffer, pH 5.3, stable for years
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chromatography
-
from pooled sputum
-
further purification of a commercial preparation by affinity chromatography
-
native enzyme from purulent sputum
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpressed with CD63 on COS cells
-
expressed in HEK-293FT cells
-
expressed in NB-4 cells and U-937 cells
-
expressed in RBL-1 cells
-
expression of neutrophil elastase and phosphonoformate immunoassociated protein in the yeast two hybrid system, overall protein interaction analysis, overview. PFAAP5 coimmunoprecipitates with neutrophil elastase and Gfi1 in transfected NIH 3T3 cells expressing the Myc-tagged proteins
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzymatic activity of neutrophil elastase is markedly decreased until four hours after the stimulation with lipopolysaccharide
-
enzyme activity is higher overall in patients with predicted severe acute pancreatitis than in those with predicted mild acute pancreatitis. Patients with respiratory failure have higher enzyme activity than those without
-
esophagectomy with elective lymphadenectomy may induce excessive release of neutrophil elastase
-
urinary trypsin inhibitor, UTI, a member of the inter-alpha trypsin inhibitor family, suppresses neutrophile leastase and granulocyte elastase in vivo
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
neutrophil elastase is a major target for the development of compounds that inhibit the progression of long-term lung function decline in chronic obstructive pulmonary disease patients
diagnostics
drug development
-
suppression of the enzyme reduces the risk of preterm delivery and improved neonatal outcomes and is therefore a target for inhibitor development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Braun, N.J.; Bodmer, J.L.; Virca, G.D.; Metz-Virca, G.; Maschler, R.; Bieth, J.G.; Schnebli, H.P.
Kinetic studies on the interaction of eglin c with human leukocyte elastase and cathepsin G
Biol. Chem. Hoppe-Seyler
368
299-308
1987
Homo sapiens
Manually annotated by BRENDA team
Powers, J.C.; Gupton, B.F.; Harley, A.D.; Nishino, N.; Whitley, R.J.
Specificity of porcine pancreatic elastase, human leukocyte elastase and cathepsin G. Inhibition with peptide chloromethyl ketones
Biochim. Biophys. Acta
485
156-166
1977
Homo sapiens
Manually annotated by BRENDA team
Heck, L.W.; Darby, W.L.; Hunter, F.A.; Bhown, A.; Miller, E.J.; Bennett, J.C.
Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil elastase from normal donors
Anal. Biochem.
149
153-162
1985
Homo sapiens
Manually annotated by BRENDA team
Starkey, P.M.; Barrett, A.J.
Human lysosomal elastase. Catalytic and immunological properties
Biochem. J.
155
265-271
1976
Homo sapiens
Manually annotated by BRENDA team
Feinstein, G.; Janoff, A.
A rapid method of purification of human granulocyte cationic neutral proteases: purification and further characterization of human granulocyte elastase
Biochim. Biophys. Acta
403
493-505
1975
Homo sapiens
Manually annotated by BRENDA team
Ohlsson, K.; Olsson, I.
The neutral proteases of human granulocytes. Isolation and partial characterization of granulocyte elastases
Eur. J. Biochem.
42
519-527
1974
Homo sapiens
Manually annotated by BRENDA team
Nakajima, K.; Powers, J.C.; Ashe, B.M.; Zimmerman, M.
Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site
J. Biol. Chem.
254
4027-4032
1979
Homo sapiens
Manually annotated by BRENDA team
Blow, A.M.J.
Action of human lysosomal elastase on the oxidized B chain of insulin
Biochem. J.
161
13-16
1977
Homo sapiens
Manually annotated by BRENDA team
Pacholok, S.G.; Davies, P.; Dorn, C.; Finke, P.; Hanlon, W.A.; Mumford, R.A.; Humes, J.L.
Formation of polymorphonuclear leukocyte elastase:alpha1 proteinase inhibitor complex and Aalpha(1-21) fibrinopeptide in human blood stimulated with the calcium ionophore A23187. A model to characterize inhibitors of polymorphonuclear leukocyte elastase
Biochem. Pharmacol.
49
1513-1520
1995
Homo sapiens
Manually annotated by BRENDA team
Barrett, A.J.
Leukocyte elastase
Methods Enzymol.
80
581-588
1981
Canis lupus familiaris, Oryctolagus cuniculus, Equus caballus, Homo sapiens, Sus scrofa
-
Manually annotated by BRENDA team
Junger, W.G.; Hallstrm, S.; Liu, F.C.; Redl, H.; Schlag, G.
The enzymatic and release characteristics of sheep neutrophil elastase: a comparison with human neutrophil elastase
Biol. Chem. Hoppe-Seyler
373
691-698
1992
Ovis aries, Homo sapiens
Manually annotated by BRENDA team
Weale, C.A.; Bernstein, P.R.; Bryant, C.; Ceccarelli, C.; Damewood, J.R.; Earlay, R.; Feeney, S.W.; Gomes, B.; Kosmider, B.J.; Steelman, G.B.; Thomas, R.M.; Vacek, E.P.; Williams, J.C.; Wolanin, D.J.; Woolson, S.
Nonpeptidic inhibitors of human leukocyte elastase. 5. Design, synthesis, and X-ray crystallography of a series of orally active 5-aminopyrimidin-6-one-containing trifluoromethyl ketones
J. Med. Chem.
38
98-108
1995
Homo sapiens
Manually annotated by BRENDA team
Dubin, A.; Potempa, J.; Travis, J.
Structural and functional characterization of elastases from horse neutrophils
Biochem. J.
300
401-406
1994
Equus caballus, Homo sapiens
Manually annotated by BRENDA team
Korkmaz, B.; Attucci, S.; Hazouard, E.; Ferrandiere, M.; Jourdan, M.L.; Brillard-Bourdet, M.; Juliano, L.; Gauthier, F.
Discriminating between the activities of human neutrophil elastase and proteinase 3 using serpin-derived fluorogenic substrates
J. Biol. Chem.
277
39074-39081
2002
Homo sapiens
Manually annotated by BRENDA team
Jordan, R.E.; Nelson, R.M.; Kilpatrick, J.; Newgren, J.O.; Esmon, P.C.; Fournel, M.A.
Inactivation of human antithrombin by neutrophil elastase. Kinetics of the heparin-dependent reaction
J. Biol. Chem.
264
10493-10500
1989
Homo sapiens
Manually annotated by BRENDA team
Baici, A.
Interaction of human leukocyte elastase with soluble and insoluble protein substrates. A practical kinetic approach
Biochim. Biophys. Acta
1040
355-364
1990
Homo sapiens
Manually annotated by BRENDA team
Becker, M.; Franz, G.; Alban, S.
Inhibition of PMN-elastase activity by semisynthetic glucan sulfates
Thromb. Haemost.
89
915-925
2003
Homo sapiens
Manually annotated by BRENDA team
Kafienah, W.; Buttle, D.J.; Burnett, D.; Hollander, A.P.
Cleavage of native type I collagen by human neutrophil elastase
Biochem. J.
330
897-902
1998
Homo sapiens
Manually annotated by BRENDA team
Macdonald, S.J.; Dowle, M.D.; Harrison, L.A.; Clarke, G.D.; Inglis, G.G.; Johnson, M.R.; Shah, P.; Smith, R.A.; Amour, A.; Fleetwood, G.; Humphreys, D.C.; Molloy, C.R.; Dixon, M.; Godward, R.E.; Wonacott, A.J.; Singh, O.M.; Hodgson, S.T.; Hardy, G.W.
Discovery of further pyrrolidine trans-lactams as inhibitors of human neutrophil elastase (HNE) with potential as development candidates and the crystal structure of HNE complexed with an inhibitor (GW475151)
J. Med. Chem.
45
3878-3890
2002
Homo sapiens
Manually annotated by BRENDA team
Kapui, Z.; Varga, M.; Urban-Szabo, K.; Mikus, E.; Szabo, T.; Szeredi, J.; Batori, S.; Finance, O.; Aranyi, P.
Biochemical and pharmacological characterization of 2-(9-(2-piperidinoethoxy)-4-oxo-4H-pyrido[1,2-a]pyrimidin-2-yloxymethyl)-4 -(1-methylethyl)-6-methoxy-1,2-benzisothiazol-3(2H)-one-1,1-dioxide (SSR69071), a novel, orally active elastase inhibitor
J. Pharmacol. Exp. Ther.
305
451-459
2003
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kawamura, T.; Okada, N.; Okada, H.
Elastase from activated human neutrophils activates procarboxypeptidase R
Microbiol. Immunol.
46
225-230
2002
Homo sapiens
Manually annotated by BRENDA team
Edwards, P.D.; Bernstein, P.R.
Synthetic inhibitors of elastase
Med. Res. Rev.
14
127-194
1994
Homo sapiens
Manually annotated by BRENDA team
Veale, C.A.; Bernstein, P.R.; Bohnert, C.M.; Brown, F.J.; Bryant, C.; Damewood, J.R., Jr.; Earley, R.; Feeney, S.W.; Edwards, P.D.; Gomes, B.; Hulsizer, J.M.; Kosmider, B.J.; Krell, R.D.; Moore, G.; Salcedo, T.W.; Shaw, A.; Silberstein, D.S.; Steelman, G.B.; Stein, M.; Strimpler, A.; Thomas, R.M.; Vacek, E.P.; Williams, J.C.; Wolanin, D.J.; Woolson, S.
Orally active trifluoromethyl ketone inhibitors of human leukocyte elastase
J. Med. Chem.
40
3173-3181
1997
Homo sapiens
Manually annotated by BRENDA team
Wei, A.Z.; Mayr, I.; Bode, W.
The refined 2.3 A crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor
FEBS Lett.
234
367-373
1988
Homo sapiens (P08246), Homo sapiens
Manually annotated by BRENDA team
Szardenings, M.; Vasel, B.; Hecht, H.J.; Collins, J.; Schomburg, D.
Highly effective protease inhibitors from variants of human pancreatic secretory trypsin inhibitor (hPSTI): an assessment of 3-D structure-based protein design
Protein Eng.
8
45-52
1995
Homo sapiens
Manually annotated by BRENDA team
Jackson, D.S.; Brown, A.D.; Schaeper, R.J.; Powers, J.C.
A kinetic study of the hydrolysis of the N-tosylalanine ester of 3-hydroxy-5-phenylpyrrole and related compounds by human leukocyte elastase
Arch. Biochem. Biophys.
323
108-114
1995
Homo sapiens
Manually annotated by BRENDA team
Balduyck, M.; Piva, F.; Mizon, C.; Maes, P.; Malki, N.; Gressier, B.; Michalski, C.; Mizon, J.
Human leucocyte elastase (HLE) preferentially cleaves the heavy chain H2 of inter-alpha-trypsin inhibitor (ITI)
Biol. Chem. Hoppe-Seyler
374
895-901
1993
Homo sapiens
Manually annotated by BRENDA team
Eckle, I.; Seitz, R.; Egbring, R.; Kolb, G.; Havemann, K.
Protein C degradation in vitro by neutrophil elastase
Biol. Chem. Hoppe-Seyler
372
1007-1013
1991
Homo sapiens
Manually annotated by BRENDA team
Sinha, S.; Watorek, W.; Karr, S.; Giles, J.; Bode, W.; Travis, J.
Primary structure of human neutrophil elastase
Proc. Natl. Acad. Sci. USA
84
2228-2232
1987
Homo sapiens (P08246), Homo sapiens
Manually annotated by BRENDA team
Navia, M.A.; McKeever, B.M.; Springer, J.P.; Lin, T.Y.; Williams, H.R.; Fluder, E.M.; Dorn, C.P.; Hoogsteen, K.
Structure of human neutrophil elastase in complex with a peptide chloromethyl ketone inhibitor at 1.84-A resolution
Proc. Natl. Acad. Sci. USA
86
7-11
1989
Homo sapiens (P08246), Homo sapiens
Manually annotated by BRENDA team
Okada, Y.; Tsuboi, S.; Tsuda, Y.; Nagamatsu, Y.; Yamamoto, J.
Synthesis of a trihexacontapeptide corresponding to the sequence 8-70 of eglin c and studies on the relationship between the structure and the inhibitory activity against human leukocyte elastase, cathepsin G and alpha-chymotrypsin
FEBS Lett.
272
113-116
1990
Homo sapiens
Manually annotated by BRENDA team
Bode, W.; Wei, A.Z.; Huber, R.; Meyer, E.; Travis, J.; Neumann, S.
X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor
EMBO J.
5
2453-2458
1986
Homo sapiens (P08246), Homo sapiens
Manually annotated by BRENDA team
Baici, A.; Pelloso, R.; Horler, D.
The kinetic mechanism of inhibition of human leukocyte elastase by MR889, a new cyclic thiolic compound
Biochem. Pharmacol.
39
919-924
1990
Homo sapiens
Manually annotated by BRENDA team
Stein, R.L.; Strimpler, A.M.; Hori, H.; Powers, J.C.
Catalysis by human leukocyte elastase: mechanistic insights into specificity requirements
Biochemistry
26
1301-1305
1987
Homo sapiens
Manually annotated by BRENDA team
Ying, Q.L.; Simon, S.R.
Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin
Biochemistry
32
1866-1874
1993
Homo sapiens
Manually annotated by BRENDA team
Heinz, D.W.; Liersch, M.; Grutter, M.G.
Crystallization of human leukocyte elastase with its inhibitor Pro44-eglin c
J. Mol. Biol.
207
641-642
1989
Homo sapiens
Manually annotated by BRENDA team
Ying, Q.L.; Kemme, M.; Simon, S.R.
Alginate, the slime exopolysaccharide of Pseudomonas aeruginosa, binds human leukocyte elastase, retards inhibition by alpha 1-proteinase inhibitor, and accelerates inhibition by secretory leukoprotease inhibitor
Am. J. Respir. Cell Mol. Biol.
15
283-291
1996
Homo sapiens
Manually annotated by BRENDA team
Korkmaz, B.; Attucci, S.; Moreau, T.; Godat, E.; Juliano, L.; Gauthier, F.
Design and use of highly specific substrates of neutrophil elastase and proteinase 3
Am. J. Respir. Cell Mol. Biol.
30
801-807
2004
Homo sapiens
Manually annotated by BRENDA team
Nakao, A.; Partis, R.A.; Jung, G.P.; Mueller, R.A.
SC-39026, a specific human neutrophil elastase inhibitor
Biochem. Biophys. Res. Commun.
147
666-674
1987
Cricetulus griseus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Redini, F.; Tixier, J.M.; Petitou, M.; Choay, J.; Robert, L.; Hornebeck, W.
Inhibition of leucocyte elastase by heparin and its derivatives
Biochem. J.
252
515-519
1988
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Sissi, C.; Lucatello, L.; Naggi, A.; Torri, G.; Palumbo, M.
Interactions of low-molecular-weight semi-synthetic sulfated heparins with human leukocyte elastase and human Cathepsin G
Biochem. Pharmacol.
71
287-293
2006
Homo sapiens
Manually annotated by BRENDA team
Doring, G.; Goldstein, W.; Botzenhart, K.; Kharazmi, A.; Schiotz, P.O.; Hoiby, N.; Dasgupta, M.
Elastase from polymorphonuclear leucocytes: a regulatory enzyme in immune complex disease
Clin. Exp. Immunol.
64
597-605
1986
Homo sapiens
Manually annotated by BRENDA team
Zani, M.L.; Nobar, S.M.; Lacour, S.A.; Lemoine, S.; Boudier, C.; Bieth, J.G.; Moreau, T.
Kinetics of the inhibition of neutrophil proteinases by recombinant elafin and pre-elafin (trappin-2) expressed in Pichia pastoris
Eur. J. Biochem.
271
2370-2378
2004
Homo sapiens
Manually annotated by BRENDA team
Sommerhoff, C.P.; Krell, R.D.; Williams, J.L.; Gomes, B.C.; Strimpler, A.M.; Nadel, J.A.
Inhibition of human neutrophil elastase by ICI 200,355
Eur. J. Pharmacol.
193
153-158
1991
Homo sapiens
Manually annotated by BRENDA team
Jones, A.; Elphick, H.; Pettitt, E.; Everard, M.L.; Evans, G.S.
Colistin stimulates the activity of neutrophil elastase and Pseudomonas aeruginosa elastase
Eur. Respir. J.
19
1136-1141
2002
Homo sapiens
Manually annotated by BRENDA team
Tralau, T.; Meyer-Hoffert, U.; Schroeder, J.M.; Wiedow, O.
Human leukocyte elastase and cathepsin G are specific inhibitors of C5a-dependent neutrophil enzyme release and chemotaxis
Exp. Dermatol.
13
316-325
2004
Homo sapiens
Manually annotated by BRENDA team
Poncz, L.; Jentoft, N.; Ho, M.C.; Dearborn, D.G.
Kinetics of proteolysis of hog gastric mucin by human neutrophil elastase and by Pseudomonas aeruginosa elastase
Infect. Immun.
56
703-704
1988
Homo sapiens
Manually annotated by BRENDA team
Potempa, J.; Dubin, A.; Watorek, W.; Travis, J.
An elastase inhibitor from equine leukocyte cytosol belongs to the serpin superfamily. Further characterization and amino acid sequence of the reactive center
J. Biol. Chem.
263
7364-7369
1988
Equus caballus, Homo sapiens
Manually annotated by BRENDA team
Doring, G.; Frank, F.; Boudier, C.; Herbert, S.; Fleischer, B.; Bellon, G.
Cleavage of lymphocyte surface antigens CD2, CD4, and CD8 by polymorphonuclear leukocyte elastase and cathepsin G in patients with cystic fibrosis
J. Immunol.
154
4842-4850
1995
Homo sapiens
Manually annotated by BRENDA team
Uejima, Y.; Kokubo, M.; Oshida, J.; Kawabata, H.; Kato, Y.; Fujii, K.
5-Methyl-4H-3,1-benzoxazin-4-one derivatives: specific inhibitors of human leukocyte elastase
J. Pharmacol. Exp. Ther.
265
516-523
1993
Cricetulus griseus, Homo sapiens
Manually annotated by BRENDA team
Rees, D.D.; Brain, J.D.; Wohl, M.E.; Humes, J.L.; Mumford, R.A.
Inhibition of neutrophil elastase in CF sputum by L-658,758
J. Pharmacol. Exp. Ther.
283
1201-1206
1997
Homo sapiens
Manually annotated by BRENDA team
Wei, L.; Lai, Z.; Gan, X.; Alliston, K.R.; Zhong, J.; Epp, J.B.; Tu, J.; Perera, A.B.; Van Stipdonk, M.; Groutas, W.C.
Mechanism-based inactivation of human leukocyte elastase via an enzyme-induced sulfonamide fragmentation process
Arch. Biochem. Biophys.
429
60-70
2004
Homo sapiens
Manually annotated by BRENDA team
Beyer, G.; Melzig, M.F.
Effects of propolis on hypoxanthine-xanthine oxidase-induced toxicity in cultivated human cells and on neutrophil elastase activity
Biol. Pharm. Bull.
28
1183-1186
2005
Homo sapiens
Manually annotated by BRENDA team
Shao, M.X.; Nadel, J.A.
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
J. Immunol.
175
4009-4016
2005
Homo sapiens
Manually annotated by BRENDA team
Meyer-Hoffert, U.; Wingertszahn, J.; Wiedow, O.
Human leukocyte elastase induces keratinocyte proliferation by epidermal growth factor receptor activation
J. Invest. Dermatol.
123
338-345
2004
Homo sapiens
Manually annotated by BRENDA team
Maffia, P.C.; Zittermann, S.E.; Scimone, M.L.; Tateosian, N.; Amiano, N.; Guerrieri, D.; Lutzky, V.; Rosso, D.; Romeo, H.E.; Garcia, V.E.; Issekutz, A.C.; Chuluyan, H.E.
Neutrophil elastase converts human immature dendritic cells into transforming growth factor-beta1-secreting cells and reduces allostimulatory ability
Am. J. Pathol.
171
928-937
2007
Homo sapiens
Manually annotated by BRENDA team
Roghanian, A.; Drost, E.M.; MacNee, W.; Howie, S.E.; Sallenave, J.M.
Inflammatory lung secretions inhibit dendritic cell maturation and function via neutrophil elastase
Am. J. Respir. Crit. Care Med.
174
1189-1198
2006
Homo sapiens
Manually annotated by BRENDA team
Rescher, U.; Goebeler, V.; Wilbers, A.; Gerke, V.
Proteolytic cleavage of annexin 1 by human leukocyte elastase
Biochim. Biophys. Acta
1763
1320-1324
2006
Homo sapiens
Manually annotated by BRENDA team
Lombard, C.; Arzel, L.; Bouchu, D.; Wallach, J.; Saulnier, J.
Human leukocyte elastase hydrolysis of peptides derived from human elastin exon 24
Biochimie
88
1915-1921
2006
Homo sapiens
Manually annotated by BRENDA team
Schietroma, M.; Carlei, F.; Cappelli, S.; Pescosolido, A.; Lygidakis, N.J.; Amicucci, G.
Effects of cholecystectomy (laparoscopic versus open) on PMN-elastase
Hepatogastroenterology
54
342-345
2007
Homo sapiens
Manually annotated by BRENDA team
Thusberg, J.; Vihinen, M.
Bioinformatic analysis of protein structure-function relationships: case study of leukocyte elastase (ELA2) missense mutations
Hum. Mutat.
27
1230-1243
2006
Homo sapiens (P08246), Homo sapiens
Manually annotated by BRENDA team
Sonawane, A.; Jyot, J.; During, R.; Ramphal, R.
Neutrophil elastase an innate immunity effector molecule represses flagellin transcription in Pseudomonas aeruginosa
Infect. Immun.
74
6682 - 6689
2006
Homo sapiens
Manually annotated by BRENDA team
Campbell, E.J.; Owen, C.A.
The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G
J. Biol. Chem.
282
14645-14654
2007
Homo sapiens
Manually annotated by BRENDA team
Dell'Aica, I.; Sartor, L.; Galletti, P.; Giacomini, D.; Quintavalla, A.; Calabrese, F.; Giacometti, C.; Brunetta, E.; Piazza, F.; Agostini, C.; Garbisa, S.
Inhibition of leukocyte elastase, polymorphonuclear chemoinvasion, and inflammation-triggered pulmonary fibrosis by a 4-alkyliden-beta-lactam with a galloyl moiety
J. Pharmacol. Exp. Ther.
316
539-546
2006
Homo sapiens
Manually annotated by BRENDA team
Santagati, N.A.; Salerno, L.; Di Giacomo, C.; Vanella, L.; Ronsisvalle, S.
Inhibition of human leukocyte elastase by novel thieno-1,3-oxazin-4-ones and thieno-1,3-thioxazin-4-ones
Lett. Drug Des. Discov.
4
386-393
2007
Homo sapiens
-
Manually annotated by BRENDA team
Woods, D.E.; Cantin, A.; Cooley, J.; Kenney, D.M.; Remold-O'Donnell, E.
Aerosol treatment with MNEI suppresses bacterial proliferation in a model of chronic Pseudomonas aeruginosa lung infection
Pediatr. Pulmonol.
39
141-149
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Attucci, S.; Gauthier, A.; Korkmaz, B.; Delepine, P.; Martino, M.F.; Saudubray, F.; Diot, P.; Gauthier, F.
EPI-hNE4, a proteolysis-resistant inhibitor of human neutrophil elastase and potential anti-inflammatory drug for treating cystic fibrosis
J. Pharmacol. Exp. Ther.
318
803-809
2006
Homo sapiens
Manually annotated by BRENDA team
Chan, S.C.; Leung, V.O.; Ip, M.S.; Shum, D.K.
Shed syndecan-1 restricts neutrophil elastase from alpha1-antitrypsin in neutrophilic airway inflammation
Am. J. Respir. Cell Mol. Biol.
41
620-628
2009
Homo sapiens
Manually annotated by BRENDA team
Padron-Barthe, L.; Courta, J.; Lepretre, C.; Nagbou, A.; Torriglia, A.
Leukocyte Elastase Inhibitor, the precursor of L-DNase II, inhibits apoptosis by interfering with caspase-8 activation
Biochim. Biophys. Acta
1783
1755-1766
2008
Homo sapiens
Manually annotated by BRENDA team
Kaellquist, L.; Hansson, M.; Persson, A.M.; Janssen, H.; Calafat, J.; Tapper, H.; Olsson, I.
The tetraspanin CD63 is involved in granule targeting of neutrophil elastase
Blood
112
3444-3454
2008
Homo sapiens
Manually annotated by BRENDA team
Alla, V.; Kashyap, A.; Gregor, S.; Theobald, M.; Heid, H.; Galle, P.R.; Strand, D.; Strand, S.
Human leukocyte elastase counteracts matrix metalloproteinase-7 induced apoptosis resistance of tumor cells
Cancer Lett.
268
331-339
2008
Homo sapiens
Manually annotated by BRENDA team
Mehner, C.; Mueller, D.; Kehraus, S.; Hautmann, S.; Guetschow, M.; Koenig, G.M.
New peptolides from the cyanobacterium Nostoc insulare as selective and potent inhibitors of human leukocyte elastase
ChemBioChem
9
2692-2703
2008
Homo sapiens
Manually annotated by BRENDA team
de Lange, T.E.; Simsek, S.; Kramer, M.H.; Nanayakkara, P.W.
A case of cocaine-induced panhypopituitarism with human neutrophil elastase-specific anti-neutrophil cytoplasmic antibodies
Eur. J. Endocrinol.
160
499-502
2009
Homo sapiens
Manually annotated by BRENDA team
Kelly, E.; Greene, C.M.; McElvaney, N.G.
Targeting neutrophil elastase in cystic fibrosis
Expert Opin. Ther. Targets
12
145-157
2008
Homo sapiens
Manually annotated by BRENDA team
Henriksen, P.A.; Sallenave, J.M.
Human neutrophil elastase: mediator and therapeutic target in atherosclerosis
Int. J. Biochem. Cell Biol.
40
1095-1100
2008
Homo sapiens
Manually annotated by BRENDA team
Lepretre, C.; Scovassi, A.I.; Shah, G.M.; Torriglia, A.
Regulation of poly(ADP-ribose) polymerase-1 functions by leukocyte elastase inhibitor/LEI-derived DNase II during caspase-independent apoptosis
Int. J. Biochem. Cell Biol.
41
1046-1054
2009
Homo sapiens
Manually annotated by BRENDA team
Roghanian, A.; Sallenave, J.M.
Neutrophil elastase (NE) and NE inhibitors: canonical and noncanonical functions in lung chronic inflammatory diseases (cystic fibrosis and chronic obstructive pulmonary disease)
J. Aerosol Med. Pulm. Drug Deliv.
21
125-144
2008
Homo sapiens
Manually annotated by BRENDA team
Nishiyama, T.
Changes in polymorphonuclear leukocyte elastase concentrations and hemolysis parameters in patients transfused with different blood preparations, and in the blood preparations themselves
J. Anesth.
22
117-124
2008
Homo sapiens
Manually annotated by BRENDA team
Toyama, S.; Hatori, F.; Shimizu, A.; Takagi, T.
A neutrophil elastase inhibitor, sivelestat, improved respiratory and cardiac function in pediatric cardiovascular surgery with cardiopulmonary bypass
J. Anesth.
22
341-346
2008
Homo sapiens
Manually annotated by BRENDA team
Guyot, N.; Butler, M.W.; McNally, P.; Weldon, S.; Greene, C.M.; Levine, R.L.; ONeill, S.J.; Taggart, C.C.; McElvaney, N.G.
Elafin, an elastase-specific inhibitor, is cleaved by its cognate enzyme neutrophil elastase in sputum from individuals with cystic fibrosis
J. Biol. Chem.
283
32377-32385
2008
Homo sapiens
Manually annotated by BRENDA team
Huang, W.; Yamamoto, Y.; Li, Y.; Dou, D.; Alliston, K.R.; Hanzlik, R.P.; Williams, T.D.; Groutas, W.C.
X-ray snapshot of the mechanism of inactivation of human neutrophil elastase by 1,2,5-thiadiazolidin-3-one 1,1-dioxide derivatives
J. Med. Chem.
51
2003-2008
2008
Homo sapiens
Manually annotated by BRENDA team
Averhoff, P.; Kolbe, M.; Zychlinsky, A.; Weinrauch, Y.
Single residue determines the specificity of neutrophil elastase for Shigella virulence factors
J. Mol. Biol.
377
1053-1066
2008
Homo sapiens
Manually annotated by BRENDA team
Ujiie, Y.; Shimada, A.; Komatsu, K.; Gomi, K.; Oida, S.; Arai, T.; Fukae, M.
Degradation of noncollagenous components by neutrophil elastase reduces the mechanical strength of rat periodontal ligament
J. Periodont. Res.
43
22-31
2008
Homo sapiens
Manually annotated by BRENDA team
Koizumi, M.; Fujino, A.; Fukushima, K.; Kamimura, T.; Takimoto-Kamimura, M.
Complex of human neutrophil elastase with 1/2SLPI
J. Synchrotron Radiat.
15
308-311
2008
Homo sapiens
Manually annotated by BRENDA team
Goulet, B.; Markovic, Y.; Leduy, L.; Nepveu, A.
Proteolytic processing of cut homeobox 1 by neutrophil elastase in the MV4;11 myeloid leukemia cell line
Mol. Cancer Res.
6
644-653
2008
Homo sapiens
Manually annotated by BRENDA team
Matsuoka, T.; Jin, E.; Tachihara, A.; Ghazizadeh, M.; Nakajima, A.; Yoshino, S.; Katayama, Y.; Kawanami, O.
Induction of pulmonary thromboembolism by neutrophil elastase in collagen-induced arthritis mice and effect of recombinant human soluble thrombomodulin
Pathobiology
75
295-305
2008
Homo sapiens
Manually annotated by BRENDA team
Ekenaes, C.; Zebrowska, A.; Schuler, B.; Vrede, T.; Andreasen, K.; Backlund, A.; Merfort, I.; Bohlin, L.
Screening for anti-inflammatory activity of 12 Arnica (Asteraceae) species assessed by inhibition of NF-kappaB and release of human neutrophil elastase
Planta Med.
74
1789-1794
2008
Homo sapiens
Manually annotated by BRENDA team
Wang, Z.; Chen, F.; Zhai, R.; Zhang, L.; Su, L.; Lin, X.; Thompson, T.; Christiani, D.C.
Plasma neutrophil elastase and elafin imbalance is associated with acute respiratory distress syndrome (ARDS) development
PLoS ONE
4
e4380
2009
Homo sapiens
Manually annotated by BRENDA team
Sullivan, A.L.; Dafforn, T.; Hiemstra, P.S.; Stockley, R.A.
Neutrophil elastase reduces secretion of secretory leukoproteinase inhibitor (SLPI) by lung epithelial cells: role of charge of the proteinase-inhibitor complex
Respir. Res.
9
60
2008
Homo sapiens
Manually annotated by BRENDA team
Hashimoto, S.; Okayama, Y.; Shime, N.; Kimura, A.; Funakoshi, Y.; Kawabata, K.; Ishizaka, A.; Amaya, F.
Neutrophil elastase activity in acute lung injury and respiratory distress syndrome
Respirology
13
581-584
2008
Homo sapiens
Manually annotated by BRENDA team
Arakawa, N.S.; Schorr, K.; Ambrosio, S.R.; Merfort, I.; Da Costa, F.B.
Further sesquiterpene lactones from Viguiera robusta and the potential anti-inflammatory activity of a heliangolide: inhibition of human neutrophil elastase release
Z. Naturforsch. C
63
533-538
2008
Homo sapiens
Manually annotated by BRENDA team
Suzuki, T.; Yamashita, C.; Zemans, R.L.; Briones, N.; Van Linden, A.; Downey, G.P.
Leukocyte elastase induces lung epithelial apoptosis via a PAR-1-, NF-kappaB-, and p53-dependent pathway
Am. J. Respir. Cell Mol. Biol.
41
742-755
2009
Homo sapiens
Manually annotated by BRENDA team
Lepretre, C.; Sidoli, G.; Scovassi, A.I.; Torriglia, A.
Leukocyte elastase inhibitor: a new regulator of PARP-1
Ann. N. Y. Acad. Sci.
1171
25-31
2009
Homo sapiens
Manually annotated by BRENDA team
Aimetti, A.A.; Tibbitt, M.W.; Anseth, K.S.
Human neutrophil elastase responsive delivery from poly(ethylene glycol) hydrogels
Biomacromolecules
10
1484-1489
2009
Homo sapiens
Manually annotated by BRENDA team
Shreder, K.R.; Cajica, J.; Du, L.; Fraser, A.; Hu, Y.; Kohno, Y.; Lin, E.C.; Liu, S.J.; Okerberg, E.; Pham, L.; Wu, J.; Kozarich, J.W.
Synthesis and optimization of 2-pyridin-3-yl-benzo[d][1,3]oxazin-4-one based inhibitors of human neutrophil elastase
Bioorg. Med. Chem. Lett.
19
4743-4746
2009
Homo sapiens
Manually annotated by BRENDA team
Xu, G.H.; Kim, Y.H.; Chi, S.W.; Choo, S.J.; Ryoo, I.J.; Ahn, J.S.; Yoo, I.D.
Evaluation of human neutrophil elastase inhibitory effect of iridoid glycosides from Hedyotis diffusa
Bioorg. Med. Chem. Lett.
20
513-515
2010
Homo sapiens
Manually annotated by BRENDA team
Inoue, Y.; Omodani, T.; Shiratake, R.; Okazaki, H.; Kuromiya, A.; Kubo, T.; Sato, F.
Development of a highly water-soluble peptide-based human neutrophil elastase inhibitor; AE-3763 for treatment of acute organ injury
Bioorg. Med. Chem.
17
7477-7486
2009
Homo sapiens
Manually annotated by BRENDA team
Skokowa, J.; Fobiwe, J.P.; Dan, L.; Thakur, B.K.; Welte, K.
Neutrophil elastase is severely down-regulated in severe congenital neutropenia independent of ELA2 or HAX1 mutations but dependent on LEF-1
Blood
114
3044-3051
2009
Homo sapiens
Manually annotated by BRENDA team
Gruber, R.; Nadir, J.; Haas, R.
Neutrophil elastase activity and concentrations of interleukin1-beta in crevicular fluid after immediate replacement and immediate loading of implants
Br. J. Oral Maxillofac. Surg.
48
228-231
2010
Homo sapiens
Manually annotated by BRENDA team
Ewen, D.; Clarke, S.L.; Smith, J.R.; Berger, C.; Salmon, G.; Trevethick, M.; Shute, J.K.
The role of protease-activated receptors PAR-1 and PAR-2 in the repair of 16HBE 14o(-) epithelial cell monolayers in vitro
Clin. Exp. Allergy
40
435-449
2010
Homo sapiens
Manually annotated by BRENDA team
Fischer, B.M.; Domowicz, D.A.; Zheng, S.; Carter, J.L.; McElvaney, N.G.; Taggart, C.; Lehmann, J.R.; Voynow, J.A.; Ghio, A.J.
Neutrophil elastase increases airway epithelial nonheme iron levels
Clin. Transl. Sci.
2
333-339
2009
Homo sapiens
Manually annotated by BRENDA team
Kawahara, Y.; Ninomiya, I.; Fujimura, T.; Funaki, H.; Nakagawara, H.; Takamura, H.; Oyama, K.; Tajima, H.; Fushida, S.; Inaba, H.; Kayahara, M.
Prospective randomized controlled study on the effects of perioperative administration of a neutrophil elastase inhibitor to patients undergoing video-assisted thoracoscopic surgery for thoracic esophageal cancer
Dis. Esophagus
23
329-339
2010
Homo sapiens
Manually annotated by BRENDA team
Kobayashi, M.; Irinoda, T.; Akiyama, Y.; Meguro, E.; Hayakawa, Y.; Funato, O.; Takagane, A.
Effect of a selective neutrophil elastase inhibitor on early recovery from body water imbalance after transthoracic esophagectomy
Dis. Esophagus
23
565-571
2010
Homo sapiens
Manually annotated by BRENDA team
Hsieh, P.W.; Yu, H.P.; Chang, Y.J.; Hwang, T.L.
Synthesis and evaluation of benzoxazinone derivatives on activity of human neutrophil elastase and on hemorrhagic shock-induced lung injury in rats
Eur. J. Med. Chem.
45
3111-3115
2010
Homo sapiens
Manually annotated by BRENDA team
Hajjar, E.; Broemstrup, T.; Kantari, C.; Witko-Sarsat, V.; Reuter, N.
Structures of human proteinase 3 and neutrophil elastase - so similar yet so different
FEBS J.
277
2238-2254
2010
Homo sapiens (P08246), Homo sapiens
Manually annotated by BRENDA team
Ikegame, Y.; Yamashita, K.; Hayashi, S.I.; Yoshimura, S.I.; Nakashima, S.; Iwama, T.
Neutrophil elastase inhibitor prevents ischemic brain damage via reduction of vasogenic edema
Hypertens. Res.
33
703-707
2010
Homo sapiens
Manually annotated by BRENDA team
Duvoix, A.; Mackay, R.M.; Henderson, N.; McGreal, E.; Postle, A.; Reid, K.; Clark, H.
Physiological concentration of calcium inhibits elastase-induced cleavage of a functional recombinant fragment of surfactant protein D
Immunobiology
216
72-79
2010
Homo sapiens, Pseudomonas aeruginosa
Manually annotated by BRENDA team
Fujii, M.; Miyagi, Y.; Bessho, R.; Nitta, T.; Ochi, M.; Shimizu, K.
Effect of a neutrophil elastase inhibitor on acute lung injury after cardiopulmonary bypass
Interact. Cardiovasc. Thorac. Surg.
10
859-862
2010
Homo sapiens
Manually annotated by BRENDA team
Abe, T.; Usui, A.; Oshima, H.; Akita, T.; Ueda, Y.
A pilot randomized study of the neutrophil elastase inhibitor, Sivelestat, in patients undergoing cardiac surgery
Interact. Cardiovasc. Thorac. Surg.
9
236-240
2009
Homo sapiens
Manually annotated by BRENDA team
Ho, S.C.; Lee, K.Y.; Chan, Y.F.; Kuo, L.W.; Ito, K.; Adcock, I.M.; Chen, B.C.; Sheu, J.R.; Lin, C.H.; Kuo, H.P.
Neutrophil elastase represses IL-8/CXCL8 synthesis in human airway smooth muscle cells through induction of NF-kappa B repressing factor
J. Immunol.
183
411-420
2009
Homo sapiens
Manually annotated by BRENDA team
Weldon, S.; McNally, P.; McElvaney, N.G.; Elborn, J.S.; McAuley, D.F.; Wartelle, J.; Belaaouaj, A.; Levine, R.L.; Taggart, C.C.
Decreased levels of secretory leucoprotease inhibitor in the Pseudomonas-infected cystic fibrosis lung are due to neutrophil elastase degradation
J. Immunol.
183
8148-8156
2009
Homo sapiens
Manually annotated by BRENDA team
Piper, M.G.; Massullo, P.R.; Loveland, M.; Druhan, L.J.; Kindwall-Keller, T.L.; Ai, J.; Copelan, A.; Avalos, B.R.
Neutrophil elastase downmodulates native G-CSFR expression and granulocyte-macrophage colony formation
J. Inflamm.
7
5
2010
Homo sapiens
Manually annotated by BRENDA team
Thongyoo, P.; Bonomelli, C.; Leatherbarrow, R.J.; Tate, E.W.
Potent inhibitors of beta-tryptase and human leukocyte elastase based on the MCoTI-II scaffold
J. Med. Chem.
52
6197-6200
2009
Homo sapiens
Manually annotated by BRENDA team
Mulchande, J.; Oliveira, R.; Carrasco, M.; Gouveia, L.; Guedes, R.C.; Iley, J.; Moreira, R.
4-Oxo-beta-lactams (azetidine-2,4-diones) are potent and selective inhibitors of human leukocyte elastase
J. Med. Chem.
53
241-253
2010
Homo sapiens
Manually annotated by BRENDA team
Kim, Y.H.; Ryoo, I.J.; Choo, S.J.; Xu, G.H.; Lee, S.; Seok, S.J.; Bae, K.; Yoo, I.D.
Clitocybin D, a novel human neutrophil elastase inhibitor from the culture broth of Clitocybe aurantiaca
J. Microbiol. Biotechnol.
19
1139-1141
2009
Homo sapiens
Manually annotated by BRENDA team
Hayashi, M.; Oya, A.; Miyake, H.; Nakai, A.; Takeshita, T.
Effect of urinary trypsin inhibitor on preterm labor with high granulocyte elastase concentration in cervical secretions
J. Nippon Med. Sch.
77
80-85
2010
Homo sapiens
Manually annotated by BRENDA team
Braun, B.C.; Meyer, H.A.; Reetz, A.; Fuhrmann, U.; Koehrle, J.
Effect of mutations of the human serpin protein corticosteroid-binding globulin on cortisol-binding, thermal and protease sensitivity
J. Steroid Biochem. Mol. Biol.
120
30-37
2010
Homo sapiens
Manually annotated by BRENDA team
Salipante, S.J.; Rojas, M.E.; Korkmaz, B.; Duan, Z.; Wechsler, J.; Benson, K.F.; Person, R.E.; Grimes, H.L.; Horwitz, M.S.
Contributions to neutropenia from PFAAP5 (N4BP2L2), a novel protein mediating transcriptional repressor cooperation between Gfi1 and neutrophil elastase
Mol. Cell. Biol.
29
4394-4405
2009
Homo sapiens
Manually annotated by BRENDA team
Jackson, P.L.; Xu, X.; Wilson, L.; Weathington, N.M.; Clancy, J.P.; Blalock, J.E.; Gaggar, A.
Human neutrophil elastase-mediated cleavage sites of MMP-9 and TIMP-1: implications to cystic fibrosis proteolytic dysfunction
Mol. Med.
16
159-166
2010
Homo sapiens
Manually annotated by BRENDA team
Zynek-Litwin, M.; Kuzniar, J.; Marchewka, Z.; Kopec, W.; Kusztal,M.; Patrzalek, D.; Biecek, P.; Klinger, M.
Plasma and urine leukocyte elastase-alpha1 protease inhibitor complex as a marker of early and long-term kidney graft function
Nephrol. Dial. Transplant.
25
2346-2351
2010
Homo sapiens
Manually annotated by BRENDA team
Topic, A.; Ljujic, M.; Nikolic, A.; Petrovic-Stanojevic, N.; Dopudja-Pantic, V.; Mitic-Milikic, M.; Radojkovic, D.
Alpha-1-antitrypsin phenotypes and neutrophil elastase gene promoter polymorphisms in lung cancer
Pathol. Oncol. Res.
17
75-80
2011
Homo sapiens
Manually annotated by BRENDA team
Sienczyk, M.; Winiarski, L.; Kasperkiewicz, P.; Psurski, M.; Wietrzyk, J.; Oleksyszyn, J.
Simple phosphonic inhibitors of human neutrophil elastase
Bioorg. Med. Chem. Lett.
21
1310-1314
2011
Homo sapiens
Manually annotated by BRENDA team
Dou, D.; He, G.; Kuang, R.; Fu, Q.; Venkataraman, R.; Groutas, W.C.
Effects of structure on inhibitory activity in a series of mechanism-based inhibitors of human neutrophil elastase
Bioorg. Med. Chem.
18
6646-6650
2010
Homo sapiens
Manually annotated by BRENDA team
Crocetti, L.; Giovannoni, M.P.; Schepetkin, I.A.; Quinn, M.T.; Khlebnikov, A.I.; Cilibrizzi, A.; Piaz, V.D.; Graziano, A.; Vergelli, C.
Design, synthesis and evaluation of N-benzoylindazole derivatives and analogues as inhibitors of human neutrophil elastase
Bioorg. Med. Chem.
19
4460-4472
2011
Homo sapiens
Manually annotated by BRENDA team
Ramachandran, R.; Mihara, K.; Chung, H.; Renaux, B.; Lau, C.S.; Muruve, D.A.; DeFea, K.A.; Bouvier, M.; Hollenberg, M.D.
Neutrophil elastase acts as a biased agonist for proteinase-activated receptor-2 (PAR2)
J. Biol. Chem.
286
24638-24648
2011
Homo sapiens
Manually annotated by BRENDA team
Papayannopoulos, V.; Metzler, K.D.; Hakkim, A.; Zychlinsky, A.
Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
J. Cell Biol.
191
677-691
2010
Homo sapiens
Manually annotated by BRENDA team
Estacio, S.G.; Moreira, R.; Guedes, R.C.
Characterizing the dynamics and ligand-specific interactions in the human leukocyte elastase through molecular dynamics simulations
J. Chem. Inf. Model.
51
1690-1702
2011
Homo sapiens
Manually annotated by BRENDA team
Hansen, G.; Gielen-Haertwig, H.; Reinemer, P.; Schomburg, D.; Harrenga, A.; Niefind, K.
Unexpected active-site flexibility in the structure of human neutrophil elastase in complex with a new dihydropyrimidone inhibitor
J. Mol. Biol.
409
681-691
2011
Homo sapiens (P08246), Homo sapiens
Manually annotated by BRENDA team
Nogami, K.; Ogiwara, K.; Matsumoto, T.; Nishiya, K.; Takeyama, M.; Shima, M.
Mechanisms of human neutrophil elastase-catalysed inactivation of factor VIII(a)
Thromb. Haemost.
105
968-980
2011
Homo sapiens
Manually annotated by BRENDA team
Madoiwa, S.; Tanaka, H.; Nagahama, Y.; Dokai, M.; Kashiwakura, Y.; Ishiwata, A.; Sakata, A.; Yasumoto, A.; Ohmori, T.; Mimuro, J.; Sakata, Y.
Degradation of cross-linked fibrin by leukocyte elastase as alternative pathway for plasmin-mediated fibrinolysis in sepsis-induced disseminated intravascular coagulation
Thromb. Res.
127
349-355
2011
Homo sapiens
Manually annotated by BRENDA team
Dokai, M.; Madoiwa, S.; Yasumoto, A.; Kashiwakura, Y.; Ishiwata, A.; Sakata, A.; Makino, N.; Ohmori, T.; Mimuro, J.; Sakata, Y.
Local regulation of neutrophil elastase activity by endogenous alpha1-antitrypsin in lipopolysaccharide-primed hematological cells
Thromb. Res.
128
283-292
2011
Homo sapiens
Manually annotated by BRENDA team
Collins, J.; Szardenings, M.; Maywald, F.; Blcker, H.; Frank, R.; Hecht, H.J.; Vasel, B.; Schomburg, D.; Fink, E.; Fritz, H.
Human leukocyte elastase inhibitors: designed variants of human pancreatic secretory trypsin inhibitor (hPSTI)
Biol. Chem. Hoppe-Seyler
371
29-36
1990
Homo sapiens
Manually annotated by BRENDA team
Ungurs, M.J.; Sinden, N.J.; Stockley, R.A.
Progranulin is a substrate for neutrophil-elastase and proteinase-3 in the airway and its concentration correlates with mediators of airway inflammation in COPD
Am. J. Physiol. Lung Cell Mol. Physiol.
306
L80-L87
2014
Homo sapiens
Manually annotated by BRENDA team
Popow-Stellmaszyk, J.; Wysocka, M.; Lesner, A.; Korkmaz, B.; Rolka, K.
A new proteinase 3 substrate with improved selectivity over human neutrophil elastase
Anal. Biochem.
442
75-82
2013
Homo sapiens
Manually annotated by BRENDA team
Lee, H.H.; Sung, M.H.
The neutrophil elastase mutant affects viability and differentiation of the human monocytic THP-1 cell
Cell Biochem. Funct.
31
305-311
2013
Homo sapiens
Manually annotated by BRENDA team
Schmelzer, C.E.; Jung, M.C.; Wohlrab, J.; Neubert, R.H.; Heinz, A.
Does human leukocyte elastase degrade intact skin elastin?
FEBS J.
279
4191-4200
2012
Homo sapiens
Manually annotated by BRENDA team
Lee, I.; Bae, K.; Kuk Yoo, J.; Ryoo, I.; Kim, B.; Seog Ahn, J.; Yoo, I.
Inhibition of human neutrophil elastase by ergosterol derivatives from the mycelium of Phellinus linteus
J. Antibiot.
65
437-440
2012
Homo sapiens
Manually annotated by BRENDA team
Gregory, A.D.; Kliment, C.R.; Metz, H.E.; Kim, K.H.; Kargl, J.; Agostini, B.A.; Crum, L.T.; Oczypok, E.A.; Oury, T.A.; Houghton, A.M.
Neutrophil elastase promotes myofibroblast differentiation in lung fibrosis
J. Leukoc. Biol.
98
143-152
2015
Homo sapiens
Manually annotated by BRENDA team
Pivetta, E.; Danussi, C.; Wassermann, B.; Modica, T.M.; Del Bel Belluz, L.; Canzonieri, V.; Colombatti, A.; Spessotto, P.
Neutrophil elastase-dependent cleavage compromises the tumor suppressor role of EMILIN1
Matrix Biol.
34
22-32
2014
Homo sapiens
Manually annotated by BRENDA team
Huang, G.; Feng, L.; Liu, B.; He, Y.; Li, Y.; Chen, Y.
Synthesis and biological evaluation of nigranoic acid esters as novel human neutrophil elastase inhibitors
Nat. Prod. Res.
29
1650-1656
2015
Homo sapiens
Manually annotated by BRENDA team
Avlonitis, N.; Debunne, M.; Aslam, T.; McDonald, N.; Haslett, C.; Dhaliwal, K.; Bradley, M.
Highly specific, multi-branched fluorescent reporters for analysis of human neutrophil elastase
Org. Biomol. Chem.
11
4414-4418
2013
Homo sapiens
Manually annotated by BRENDA team
Feng, L.; Liu, X.; Zhu, W.; Guo, F.; Wu, Y.; Wang, R.; Chen, K.; Huang, C.; Li, Y.
Inhibition of human neutrophil elastase by pentacyclic triterpenes
PLoS ONE
8
e82794
2013
Homo sapiens
Manually annotated by BRENDA team
Novovic, S.; Andersen, A.M.; Nord, M.; Astrand, M.; Ottosson, T.; Jorgensen, L.N.; Hansen, M.B.
Activity of neutrophil elastase reflects the progression of acute pancreatitis
Scand. J. Clin. Lab. Invest.
73
485-493
2013
Homo sapiens
Manually annotated by BRENDA team
Hochscherf, J.; Pietsch, M.; Tieu, W.; Kuan, K.; Abell, A.D.; Guetschow, M.; Niefind, K.
Crystal structure of highly glycosylated human leukocyte elastase in complex with an S2 site binding inhibitor
Acta Crystallogr. Sect. F
74
480-489
2018
Homo sapiens (P08246), Homo sapiens
Manually annotated by BRENDA team
Liu, S.Y.; Xiong, H.; Li, R.R.; Yang, W.C.; Yang, G.F.
Activity-based near-infrared fluorogenic probe for enabling in vitro and in vivo profiling of neutrophil elastase
Anal. Chem.
91
3877-3884
2019
Homo sapiens
Manually annotated by BRENDA team
Fu, Z.; Thorpe, M.; Akula, S.; Chahal, G.; Hellman, L.T.
Extended cleavage specificity of human neutrophil elastase, human proteinase 3, and their distant ortholog clawed frog PR3 - three elastases with similar primary but different extended specificities and stability
Front. Immunol.
9
2387
2018
Homo sapiens
Manually annotated by BRENDA team
Tan, X.F.; Kim, D.W.; Song, Y.H.; Kim, J.Y.; Yuk, H.J.; Wang, Y.; Curtis-Long, M.J.; Park, K.H.
Human neutrophil elastase inhibitory potential of flavonoids from Campylotropis hirtella and their kinetics
J. Enzyme Inhib. Med. Chem.
31
16-22
2016
Homo sapiens
Manually annotated by BRENDA team
Yang, R.; Zhong, L.; Yang, X.Q.; Jiang, K.L.; Li, L.; Song, H.; Liu, B.Z.
Neutrophil elastase enhances the proliferation and decreases apoptosis of leukemia cells via activation of PI3K/Akt signaling
Mol. Med. Rep.
13
4175-4182
2016
Homo sapiens
Manually annotated by BRENDA team
Wiesmeier, M.; Gautam, S.; Kirschnek, S.; Haecker, G.
Characterisation of neutropenia-associated neutrophil elastase mutations in a murine differentiation model in vitro and in vivo
PLoS ONE
11
e0168055
2016
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Macleod, T.; Doble, R.; McGonagle, D.; Wasson, C.W.; Alase, A.; Stacey, M.; Wittmann, M.
Neutrophil elastase-mediated proteolysis activates the anti-inflammatory cytokine IL-36 receptor antagonist
Sci. Rep.
6
24880
2016
Homo sapiens
Manually annotated by BRENDA team