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Literature summary for 3.4.21.37 extracted from

  • Hajjar, E.; Broemstrup, T.; Kantari, C.; Witko-Sarsat, V.; Reuter, N.
    Structures of human proteinase 3 and neutrophil elastase - so similar yet so different (2010), FEBS J., 277, 2238-2254.
    View publication on PubMed
Search for more literature for 3.4.21.37

Inhibitors

Inhibitors Comment Organism Structure
MeO-Suc-Ala-Ala-Pro-Ala-CH2Cl
-
 Homo sapiens
MeO-Suc-Ala-Ala-Pro-Val-CH2Cl
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P08246
-
-

Source Tissue

Source Tissue Comment Organism Textmining
polymorphonuclear neutrophil
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid + H2O
-
 Homo sapiens ?
-
 ?
GW475151 + H2O
-
 Homo sapiens ?
-
 ?
additional information substrates with a hydrophobic side chain at P1 are efficiently cleaved and P1-valine is preferred over an alanine or a phenylalanine Homo sapiens ?
-
 ?
N-(4-(4-morpholinylcarbonyl)benzoyl)-Val-Pro-Ile + H2O
-
 Homo sapiens ?
-
 ?
OMTKY3a + H2O
-
 Homo sapiens ?
-
 ?
secretory leukocyte protease inhibitor + H2O
-
 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
HNE
-
 Homo sapiens
neutrophil elastase
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function human neutrophil elastase plays an important role in cell signaling and represents an regulator of the inflammatory response Homo sapiens