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Information on EC 3.4.21.70 - Pancreatic endopeptidase E
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3.4.21.70 Pancreatic endopeptidase ESpecify your search results
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The expected taxonomic range for this enzyme is: Tetrapoda
Synonyms
pancreatic protease e, pancreatic endopeptidase e, cholesterol-binding pancreatic proteinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CBPP
-
-
-
-
Cholesterol-binding pancreatic proteinase
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-
-
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Cholesterol-binding proteinase
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-
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Cholesterol-binding serine proteinase
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-
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pancreatic endopeptidase E
Pancreatic protease E
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-
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Pancreatic proteinase E
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-
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PEE
Proteinase, cholesterol-binding serine
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-
-
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Proteinase, E
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-
-
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Proteinase, pancreas E
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: Ala-/-. Does not hydrolyse elastin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
68073-27-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Benzyloxycarbonylalanine 4-nitrophenyl ester + H2O
Benzyloxycarbonylalanine + 4-nitrophenol
-
-
-
-
?
Carboxybenzoyl-L-alanine 4-nitrophenyl ester + H2O
Carboxybenzoyl-L-alanine + 4-nitrophenol
-
-
-
-
?
Insulin A-chain + H2O
Hydrolyzed insulin A-chain
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enzyme acts on the carbonyl bonds of Ala8, Val10 and Ser12, with less extensive action at Ile2 or Val3, Ser9, Leu13, Tyr14, Glu15, and Tyr19
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
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enzyme acts on the carbonyl bonds of Ser9, Val12, Ala14 and Val18 with less extensive action at Val2, Leu15, and Gly23, and minor cleavages at Leu6, Leu11, and Tyr16
-
-
?
Succinyl-tri-L-alanine 4-nitroanilide + H2O
Succinyl-tri-L-alanine + 4-nitroaniline
-
-
-
-
?
Tert-Butyloxycarbonyl-L-alanine 4-nitrophenyl ester + H2O
Tert-Butyloxycarbonyl-L-alanine + 4-nitrophenol
-
-
-
-
?
Acetyl-tri-L-alanine methyl ester + H2O
Acetyl-tri-L-alanine + methanol
-
-
-
-
?
additional information
?
-
-
general functional significance in the digestion of proteins
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-
?
additional information
?
-
-
no activity with: benzoyl-L-arginine ethyl ester, tosyl-L-arginine methyl ester
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-
?
additional information
?
-
-
may fulfill a function as an intestinal lipoprotein
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-
?
additional information
?
-
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pronounced selectivity for the carbonyl bonds of serine, threonine, alanine, and valine residues, with the latter most favoured
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-
?
additional information
?
-
-
the specificity is complementary to that of the chymotrypsins, this property may be physiologically significant
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
general functional significance in the digestion of proteins
-
-
?
additional information
?
-
-
may fulfill a function as an intestinal lipoprotein
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-
?
additional information
?
-
-
the specificity is complementary to that of the chymotrypsins, this property may be physiologically significant
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-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Human serum alpha1-antitrypsin
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no inhibition by other naturally occuring inhibitors tested
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additional information
-
a series of acyl-peptidyl chloromethanes with Ala in P1
-
additional information
-
a series of acyl-peptidyl chloromethanes with Ala in P1
-
additional information
-
a series of acyl-peptidyl chloromethanes with Ala in P1
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.7 - 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit III of the bovine ternary complex of procarboxypeptidase A-S6 (BSIII), a defective serine endopeptidase-like protein, is highly homologous to human protease E, possibly BSIII is a truncated protease site
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
truncated enzyme exists in pancreatic juice as a binary complex with procarboxypeptidase A
brenda
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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). CEL3A_HUMAN
270
0
29489
Swiss-Prot
Secretory Pathway (Reliability: 2)
CEL3B_HUMAN
270
0
29263
Swiss-Prot
Secretory Pathway (Reliability: 2)
CEL3B_MACMU
257
0
27687
Swiss-Prot
other Location (Reliability: 3)
CEL3B_MOUSE
269
0
28905
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q6AZF9_XENLA
269
0
28991
TrEMBL
Secretory Pathway (Reliability: 1)
Q5M925_XENTR
269
0
28965
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
35000
additional information
-
primary structure determined by sequence analysis of cloned mRNA
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
in the intestinal fluids the protein appears to be present in firm association with cholesterol, phospholipids, triacylglycerols and bile salts as macromolecular protein-lipid complex
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
24°C, dilute solution of protein concentration of less than 0.4 mg/ml, stable for 3 months, unstable below pH 4.0
29635
additional information
-
relatively resistant towards acid, the activity decreases by 20% by incubation in 50 mM acetic acid and by 60% in 50 mM HCl, complete inactivation by treatment with 50 mM NaOH
29641
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Loses up to 20% of activity when subjected at 0.2 mg protein/ml to lyophilization or freezing and thawing
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, slow inactivation over a period of a month to a limiting value of around 75% of maximal activity, this decrease is most rapid at pH 3 and slowest at pH 9
-
22°C, 50 mM Tris/100 mM NaCl, pH 7.9, 15 mM NaN3, with or without 10 mM CaCl2, loss of approximately 8% of its esterolytic activity per week
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24°C, dilute solution of protein concentration of less than 0.4 mg/ml, pH 4.0-8.0, stable for 3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mallory, P.A.; Travis, J.
Human pancreatic enzymes: purification and characterization of a nonelastolytic enzyme, protease E. resembling elastase
Biochemistry
14
722-730
1975
Homo sapiens
brenda
Shen, W.; Fletcher, T.S.; Largman, C.
Primary structure of human pancreatic protease E determined by sequence analysis of the cloned mRNA
Biochemistry
26
3447-3452
1987
Homo sapiens
brenda
Kobayashi, R.; Kobayashi, Y.; Hirs, C.H.W.
The specificity of porcine pancreatic protease E
J. Biol. Chem.
256
2460-2465
1981
Sus scrofa
brenda
Kobayashi, Y.; Kobayashi, R.; Hirs, C.H.W.
Identification of zymogen E in a complex with bovine procarboxypeptidase A
J. Biol. Chem.
256
2466-2470
1981
Bos taurus
brenda
Moulard, M.; Kerfelec, B.; Mallet, B.; Chapus, C.
Identification of a procarboxypeptidase A-truncated protease E binary complex in human pancreatic juice
FEBS Lett.
250
166-170
1989
Homo sapiens
brenda
Cambillau, C.; Kerfelec, B.; Sciaky, M.; Chapus, C.
Subunit III of ruminant procarboxypeptidase A-S6 complexes and pancreatic proteases E. A new family of pancreatic serine endopeptidases?
FEBS Lett.
232
91-95
1988
Bos taurus
brenda
Sziegoleit, A.
A novel proteinase from human pancreas
Biochem. J.
219
735-742
1984
Homo sapiens
brenda
Sziegoleit, A.
Purification and characterization of a cholesterol-binding protein from human pancreas
Biochem. J.
207
573-582
1982
Homo sapiens
brenda
Chapus, C.; Kerfelec, B.; Dimicoli, J.L.
Binding of terbium and of an elastase inhibitor to bovine pancreatic subunit III, an inactive protease E
J. Biol. Chem.
265
3726-3730
1990
Bos taurus
brenda
Pignol, D.; Granon, S.; Chapus, C.; Fontecilla-Camps, J.C.
Crystallographic study of a cleaved, non-activatable form of porcine zymogen E
J. Mol. Biol.
252
20-24
1995
Sus scrofa
brenda
Bieth, J.G.
Pancreatic endopeptidase E
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
2
1510-1511
2004
Bos taurus, Homo sapiens, Sus scrofa
-
brenda
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