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Information on EC 3.4.21.71 - Pancreatic elastase II and Organism(s) Homo sapiens
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3.4.21.71 Pancreatic elastase IISpecify your search results
Word Map
- 3.4.21.71
- neutropenia
-
ii-forming
- chymostatin
- netherton
-
proelastase
-
kostmann
-
chymostatin-sensitive
- tetradecapeptide
-
1-protease
-
elastolytic
-
ii-generating
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
elastase 2, elastase-2, ela-2, pancreatic elastase ii, bovine pancreatic elastase, neutrophil elastase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Elastase 2
Elastase 2
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
75603-19-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is formed by activation of proelastase II from mammalian pancreas by trypsin, usually only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species
-
-
?
additional information
?
-
-
the enzyme is formed by activation of proelastase II from mammalian pancreas by trypsin, usually only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species
-
-
?
additional information
?
-
-
the enzyme is formed by activation of proelastase II from mammalian pancreas by trypsin, usually only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is formed by activation of proelastase II from mammalian pancreas by trypsin, usually only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species
-
-
?
additional information
?
-
-
the enzyme is formed by activation of proelastase II from mammalian pancreas by trypsin, usually only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species
-
-
?
additional information
?
-
-
the enzyme is formed by activation of proelastase II from mammalian pancreas by trypsin, usually only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kallikrein 5
-
kallikrein 5 leads to an elastolytic activity increase of 4times compared with the basal activity level of pro-elastase 2
-
additional information
-
the enzyme needs to be proteolytically activated e.g. by trypsin, proelastase 2 is not activated by cathepsin B
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000299
secretory leukoprotease inhibitor
-
pH and temperature not specified in the publication
-
0.0000143
skin-derived antileukoprotease
-
pH and temperature not specified in the publication
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
elastase 2 impairs skin barrier function in Netherton syndrome through filaggrin and lipid misprocessing. The enzyme is a major protease driving the pathogenesis of Netherton syndrome
physiological function
-
expression of ELA2 is associated with histone acetylation in leukemic cell lines. DNA methylation and transcript levels of ELA2 in chronic myeloid leukemia are not correlated
physiological function
-
the enzyme's biological functions include involvement in migration of neutrophils by means of focal proteolysis, killing of microorganisms, and degradation/activation of various proteins including cytokines, chemokines and ECM proteins
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CEL2A_HUMAN
269
0
28888
Swiss-Prot
Secretory Pathway (Reliability: 2)
CEL2B_HUMAN
269
0
28810
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
primary structure determined by sequence analysis of cloned mRNA
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the enzyme needs to be proteolytically activated e.g. by trypsin, proelastase 2 is not activated by cathepsin B
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
proelastase 2 from pancreatic juice by anion and cation exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
serum elastase 2 concentration was higher in patients affected by photoaging if compared with healthy controls compared with subjects receiving placebo 2 weeks after the end of treatment
-
serum neutrophil elastase 2 concentration is significantly decreased in patients treated with the dietary supplement
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fletcher, T.S.; Shen, W.F.; Largman, C.
Primary structure of human pancreatic elastase 2 determined by sequence analysis of the cloned mRNA
Biochemistry
26
7256-7261
1987
Homo sapiens
Shirasu, Y.; Yoshida, H.; Matsuki, S.; Takemura, K.; Ikeda, N.; Shimada, Y.; Ozawa, T.; Mikayama, T.; Iijima, H.; Ishida, A.; Sato, Y.; Tamai, Y.; Tanaka, J.; Ikenaga, H.
Molecular cloning and expression in Escherichia coli of a cDNA encoding human pancreatic elastase 2
J. Biochem.
102
1555-1563
1987
Homo sapiens
Davril, M.; Laine, A.; Hayem, A.
Studies on the interactions of human pancreatic elastase 2 with human alpha 1-proteinase inhibitor and alpha 1-antichymotrypsin
Biochem. J.
245
699-704
1987
Homo sapiens
Lindkvist, B.; Fajardo, I.; Pejler, G.; Borgstrom, A.
Cathepsin B activates human trypsinogen 1 but not proelastase 2 or procarboxypeptidase B
Pancreatology
6
224-231
2006
Homo sapiens
Bonnart, C.; Deraison, C.; Lacroix, M.; Uchida, Y.; Besson, C.; Robin, A.; Briot, A.; Gonthier, M.; Lamant, L.; Dubus, P.; Monsarrat, B.; Hovnanian, A.
Elastase 2 is expressed in human and mouse epidermis and impairs skin barrier function in Netherton syndrome through filaggrin and lipid misprocessing
J. Clin. Invest.
120
871-882
2010
Homo sapiens, Mus musculus
Rogers, S.L.; Zhao, Y.; Jiang, X.; Eaves, C.J.; Mager, D.L.; Rouhi, A.
Expression of the leukemic prognostic marker CD7 is linked to epigenetic modifications in chronic myeloid leukemia
Mol. Cancer
9
41
2010
Homo sapiens
Di Cerbo, A.; Laurino, C.; Palmieri, B.; Iannitti, T.
A dietary supplement improves facial photoaging and skin sebum, hydration and tonicity modulating serum fibronectin, neutrophil elastase 2, hyaluronic acid and carbonylated proteins
J. Photochem. Photobiol. B
144C
94-103
2015
Homo sapiens
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