Information on EC 3.4.21.70 - Pancreatic endopeptidase E

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.70
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RECOMMENDED NAME
GeneOntology No.
Pancreatic endopeptidase E
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: Ala-/-. Does not hydrolyse elastin
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
68073-27-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-Ala-Ala-Ala-OMe + H2O
?
show the reaction diagram
Acetyl-tri-L-alanine methyl ester + H2O
Acetyl-tri-L-alanine + methanol
show the reaction diagram
Benzoyl-L-alanine methyl ester + H2O
Benzoyl-L-alanine + methanol
show the reaction diagram
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-
-
-
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Benzyloxycarbonylalanine 4-nitrophenyl ester + H2O
Benzyloxycarbonylalanine + 4-nitrophenol
show the reaction diagram
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-
-
-
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Carboxybenzoyl-L-alanine 4-nitrophenyl ester + H2O
Carboxybenzoyl-L-alanine + 4-nitrophenol
show the reaction diagram
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-
-
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casein + H2O
hydrolyzed casein
show the reaction diagram
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-
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Chymotrypsin + H2O
Hydrolyzed chymotrypsin
show the reaction diagram
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-
-
-
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Elastase + H2O
Hydrolyzd elastase
show the reaction diagram
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-
-
-
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Glucagon + H2O
?
show the reaction diagram
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carbonyl bond of Ala is the favoured cleavage site
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Hemoglobin + H2O
Hydrolyzed hemoglobin
show the reaction diagram
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-
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Insulin A-chain + H2O
Hydrolyzed insulin A-chain
show the reaction diagram
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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
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-
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Insulin B-chain + H2O
Hydrolyzed insulin B-chain
show the reaction diagram
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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
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Suc-Ala-Ala-Ala-4-nitrophenylamide + H2O
?
show the reaction diagram
Succinyl-tri-L-alanine 4-nitroanilide + H2O
Succinyl-tri-L-alanine + 4-nitroaniline
show the reaction diagram
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-
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Tert-Butyloxycarbonyl-L-alanine 4-nitrophenyl ester + H2O
Tert-Butyloxycarbonyl-L-alanine + 4-nitrophenol
show the reaction diagram
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-
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Trypsin + H2O
Hydrolyzed trypsin
show the reaction diagram
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-
-
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additional information
?
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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
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Acetyl-Ala-Ala-Ala-AlaCH2Cl
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Acetyl-Ala-Ala-AlaCH2Cl
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Acetyl-Ala-Ala-Phe-AlaCH2Cl
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Acetyl-Ala-Ala-Pro-AlaCH2Cl
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Carboxybenzoyl-Gly-Leu-AlaCH2Cl
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diisopropyl phosphofluoridate
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Human serum alpha1-antitrypsin
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no inhibition by other naturally occuring inhibitors tested
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phenylmethanesulfonyl fluoride
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plasma alpha1-proteinase inhibitor
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.86 - 4.4
Acetyl-tri-L-alanine methyl ester
24
Benzoyl-L-alanine methyl ester
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0.04706
Benzyloxycarbonylalanine 4-nitrophenyl ester
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0.95
Succinyl-tri-L-alanine 4-nitroanilide
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0.166
tert-butyloxycarbonyl-L-alanine 4-nitrophenyl ester
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
59
Acetyl-tri-L-alanine methyl ester
Sus scrofa
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6.3
Benzoyl-L-alanine methyl ester
Sus scrofa
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7.5
Succinyl-tri-L-alanine 4-nitroanilide
Sus scrofa
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additional information
additional information
Bos taurus
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7 - 9.5
8.4
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benzyloxycarbonylalanine 4-nitrophenyl ester
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
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cleavage of benzyloxycarbonylalanine 4-nitrophenyl ester
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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human, gel filtration
30500
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1 * 30500, human, SDS-PAGE
additional information
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primary structure determined by sequence analysis of cloned mRNA
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
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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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
subunit III, a truncated form of PEE
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a cleaved non-activatable form of porcine zymogen E
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subunit III, a truncated form of PEE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
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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
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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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
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loss of activity within 5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ at concentrations up to 0.4 M has no effect on stability
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Loses up to 20% of activity when subjected at 0.2 mg protein/ml to lyophilization or freezing and thawing
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Rapid autolysis at protein concentrations above 0.4 mg/ml, stable below
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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
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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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4°C, stable over months without loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE