Information on EC 3.4.21.71 - Pancreatic elastase II

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.71
-
RECOMMENDED NAME
GeneOntology No.
Pancreatic elastase II
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: Leu-/-, Met-/- and Phe-/-. Hydrolyses elastin
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
75603-19-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bovine
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
rat, male Wistar
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(pro)-filaggrin + H2O
?
show the reaction diagram
collagen fiber + H2O
?
show the reaction diagram
-
-
-
-
?
elastic fiber + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
Hydrolyzed elastin
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-Ile-Asp-Val-Gln-Ile-Tyr + H2O
Gly-Ile-Asp-Val-Gln + Ile-Tyr + ?
show the reaction diagram
-
sequence in phenylalanine oxidase
-
?
N-succinyl-Ala-ALa-Pro-Leu-P-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
SMS 201-995 + H2O
?
show the reaction diagram
-
-
-
?
Somatostatin-14 + H2O
?
show the reaction diagram
Suc-Ala-Ala-Pro-Met-p-nitroanilide + H2O
p-nitroaniline + Suc-Ala-Ala-Pro-Met
show the reaction diagram
-
-
-
?
Suc-Ala-Ala-Val-Ala-p-nitroanilide + H2O
p-nitroaniline + Suc-Ala-Ala-Val-Ala
show the reaction diagram
-
-
-
?
Suc-Tyr-Leu-Val-p-nitroanilide + H2O
p-nitroaniline + Suc-Tyr-Leu-Val
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(pro)-filaggrin + H2O
?
show the reaction diagram
collagen fiber + H2O
?
show the reaction diagram
-
-
-
-
?
elastic fiber + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Somatostatin-14 + H2O
?
show the reaction diagram
-
hydrolytic enzyme required for intestinal digestion of food stuff, natural substrates are proteins, protein fragments and peptides, greater affinity for natural substrates than for synthetics, specifically involved in the regulation of biological functions of somatostatin-14 in the gastrointestinal tract
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
-
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dichloroisocoumarin
-
causes total inhibition
alpha1-Antichymotrypsin
-
-
-
chymostatin
-
-
Cu2+
-
1 mM, 50% inhibition
diisopropyl fluorophosphate
-
causes total inhibition
Elastinal
-
-
Hg2+
-
1 mM, 50% inhibition
Human alpha1-proteinase inhibitor
-
-
-
leupeptin
-
-
N-alpha-tosyl-L-lysine-chloromethyl ketone
-
most potent inhibitor
NCDC
-
-
phenylmethylsulfonyl fluoride
secretory leukoprotease inhibitor
-
skin-derived antileukoprotease
-
Soybean trypsin inhibitor
-
most potent inhibitor
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
kallikrein 5
-
additional information
-
the enzyme needs to be proteolytically activated e.g. by trypsin, proelastase 2 is not activated by cathepsin B
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0083
Gly-Ile-Asp-Val-Gln-Ile-Tyr
-
pH 8.0, 25°C
0.089
Somatostatin-14
-
pH 8.0, 25°C
1.567
Suc-Ala-Ala-Pro-Met-p-nitroanilide
-
pH 8.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
Gly-Ile-Asp-Val-Gln-Ile-Tyr
Bos taurus
-
pH 8.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.76
-
-
additional information
-
specific activity 118.83, activity of the enzyme is determined by its ability to degrade 125I-S-14, ng degraded/mg protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
-
assay at
8 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 5.9
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
pancreatic juice
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
gel filtration
27260
-
predicted from cDNA clone
additional information
-
primary structure determined by sequence analysis of cloned mRNA
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
the enzyme needs to be proteolytically activated e.g. by trypsin, proelastase 2 is not activated by cathepsin B
additional information
-
no carbohydrate moiety detected in the structure
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 50
-
incubation of purified enzyme for 1 h causes a slight loss of activity, less than 10%
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proelastase 2 from pancreatic juice by anion and cation exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA clone isolated
-
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
-