Information on EC 3.4.21.36 - pancreatic elastase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.36
-
RECOMMENDED NAME
GeneOntology No.
pancreatic elastase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-/-
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
848900-32-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
cod myofibrillar protein + H2O
?
show the reaction diagram
-
-
-
-
?
Elastin + H2O
?
show the reaction diagram
elastin orcein + H2O
?
show the reaction diagram
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
orcein-elastin + H2O
?
show the reaction diagram
-
-
-
-
?
somatostatin 14 + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Ala + 4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Ala + 4-nitroaniline
show the reaction diagram
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
?
show the reaction diagram
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala-Ala + p-nitroaniline
show the reaction diagram
succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-Pro-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Ala-p-nitroanilide + H2O
?
show the reaction diagram
succinyl-Ala-Ala-Pro-Ile-p-nitroanilide + H2O
?
show the reaction diagram
succinyl-Ala-Ala-Pro-Leu-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Met-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
?
show the reaction diagram
succinyl-Ala-Ala-Pro-Val-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Ala-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Ala-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-alpha-aminobutyric acid-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Ile-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Ala-4-nitrophenol ester + H2O
t-butyloxycarbonyl-Ala + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Ala-p-nitrophenylester + H2O
?
show the reaction diagram
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
Elastin + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
slightly activates
Mg2+
-
slightly activates
NaCl
-
elastase 1: slight inhibition above 150 mM, elastase 2: 25-250 mM, activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R,2'R,2''R,2'''R,3S,3'S,3''S,3'''S,4S,4'S,4''R)-2,2',2'''-tris(3,4-dihydroxyphenyl)-2''-(4-hydroxyphenyl)-3,3',3'',3''',4,4',4'',4'''-octahydro-2H,2'H,2''H,2'''H-4,8':4',8'':4'',8'''-quaterchromene-3,3',3'',3''',5,5',5'',5''',7,7',7'',7'''-dodecol
-
-
(2R,2'R,2''R,3S,3'S,3''S,4S,4'R)-2,2',2''-tris(3,4-dihydroxyphenyl)-3,3',3'',4,4',4''-hexahydro-2H,2'H,2''H-4,8':4',8''-terchromene-3,3',3'',5,5',5'',7,7',7''-nonol
-
-
(trifluoroacetyl)-Phe-Ala-p-(trifluoromethanal)anilide
-
-
-
(trifluoroacetyl)-Val-Ala-p-(trifluoromethanal)anilide
-
-
-
1-O-(3-O-sulfo-beta-D-galactopyranosyl)-ceramide
-
0.001 mg elastase in 0.01 ml of 50 mM HEPES buffer at pH 7.5 with 0.01 mg inhibitor in 0.01 ml DMSO at 37° for 30 min
-
3,4-dichloroisocoumarin
-
-
3-Phenylpropionic acid
-
-
4-([(S)-1-[((S)-2-[[(RS)-3,3,3-trifluoro-1-isopropyl-2-oxopropyl]aminocarbonyl]pyrrolidin-1-yl-)carbonyl]-2-methylpropyl]aminocarbonyl)benzoic acid
-
-
Alpha1-antitrypsin
-
-
-
Alpha1-proteinase inhibitor
-
-
-
alpha2-Macroglobulin
-
-
-
Cholesterol sulfate
-
0.001 mg elastase in 0.09 ml of 50 mM HEPES buffer at pH 7.5 with 0.01 mg inhibitor in 0.01 ml DMSO at 37° for 30 min
diisopropyl fluorophosphate
EETI II
-
trypsin-specific squash inhibitor from Ecballium elaterium
-
elafin
-
Elastinal
FR130180
-
i.e. 4-([(S)-1-[((S)-2-[[(RS)-3,3,3-trifluoro-1-isopropyl-2-oxopropyl]-aminocarbonyl]pyrrolidin-1yl)carbonyl]-2-methylpropyl]aminocarbonyl) benzoic acid
FR136706
-
potent inhibitor
HEI-TOE I
-
hybrid inhibitor from Ecballium elaterium and the optimized binding loop of the third domain of turkey ovomucoid inhibitor
-
HEI-TOE II
-
-
-
HEI-TOE III
-
-
-
largamide A
-
-
largamide A methyl ester
-
low-micromolar inhibitory activity
largamide B
-
-
largamide B methyl ester
-
low-micromolar inhibitory activity
largamide C
-
-
largamide C methyl ester
-
low-micromolar inhibitory activity
lyngbyastatin 10
-
-
lyngbyastatin 7
-
-
lyngbyastatin 8
-
-
lyngbyastatin 9
-
-
MCEI III
-
-
-
N-benzyl-2-oxo-4-(phenylsulfonyl)azetidine-1-carboxamide
-
JM54, potent and irreversible inhibitor
NaCl
-
elastase 1: slight inhibition above 150 mM, elastase 2: 25-250 mM, activation
OMTKY3
-
third Kazal-type domain of ovomucoid inhibitor from turkey egg white
-
PACTLEYRC
-
-
Pancreatic trypsin inhibitor
-
-
-
phenylmethanesulfonyl fluoride
PMTLEYR
-
-
scyptolin A
-
the inhibitor occupies the most prominent subsites S1 through S4 of the elastase and prevents a hydrolytic attack by covering the active center with its rigid ring structure
SDS
-
0.001 mg elastase in 0.09 ml of 50 mM HEPES buffer at pH 7.5 with 0.01 mg inhibitor in 0.01 ml DMSO at 37° for 30 min
serpin
-
active site distortion is sufficient for proteinase inhibition by serpins
-
Soybean trypsin inhibitor
-
tiglicamide A
-
moderate inhibition of porcine pancreatic elastase in vitro
tiglicamide B
-
moderate inhibition of porcine pancreatic elastase in vitro
tiglicamide C
-
moderate inhibition of porcine pancreatic elastase in vitro
tosyl-L-phenylalanyl chloromethylketone
-
-
trappin-2
-
-
-
viral serpin crmA
-
pancreatic elastase is rapidly inhibited by wild-type crmA and reactive loop variant P1 Arg crmAs
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.68 - 1.47
succinyl-Ala-Ala-Ala-p-nitroanilide
0.83
succinyl-Ala-Ala-Pro-Ala-p-nitroanilide
-
-
0.15 - 0.91
succinyl-Ala-Ala-Pro-Ile-p-nitroanilide
1.34
succinyl-Ala-Ala-Pro-Leu-p-nitroanilide
-
-
1.42
succinyl-Ala-Ala-Pro-Met-p-nitroanilide
-
-
1.21
succinyl-Ala-Ala-Pro-Phe-p-nitroanilide
-
-
0.82
succinyl-Ala-Ala-Pro-Val-p-nitroanilide
-
-
2.09
succinyl-L-Ala-L-Ala-L-Ala-4-nitroanilide
-
in 0.1 M phosphate buffer, pH 7.0 and 37°C
0.513
tert-butyloxycarbonyl-Ala-p-nitrophenylester
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.59
succinyl-Ala-Ala-Ala-p-nitroanilide
Rattus norvegicus
-
-
4.88
succinyl-Ala-Ala-Pro-Ala-p-nitroanilide
Rattus norvegicus
-
-
0.12
succinyl-Ala-Ala-Pro-Met-p-nitroanilide
Rattus norvegicus
-
-
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.082 - 0.82
EETI II
-
0.00000075
elafin
-
panreatic elastase
-
0.000098 - 0.00038
HEI-TOE I
-
0.00007
HEI-TOE II
-
pH 8.5, 25°C
-
0.000056 - 0.00031
HEI-TOE III
-
0.000013
MCEI III
-
pH 8.5, 25°C
-
0.000000024
OMTKY3
-
0.017 - 0.17
PACTLEYRC
0.000049 - 0.0013
PMTLEYR
0.00000032
trappin-2
-
pancreatic elastase
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00141
largamide A
Sus scrofa
-
-
0.00294
largamide A methyl ester
Sus scrofa
-
-
0.00053
largamide B
Sus scrofa
-
-
0.00223
largamide B methyl ester
Sus scrofa
-
-
0.00115
largamide C
Sus scrofa
-
-
0.00216
largamide C methyl ester
Sus scrofa
-
-
0.00012
lyngbyastatin 10
Sus scrofa
-
in Tris-HCl (pH 8.0)
0.0000473
lyngbyastatin 7
Sus scrofa
-
in Tris-HCl (pH 8.0)
0.000123
lyngbyastatin 8
Sus scrofa
-
in Tris-HCl (pH 8.0)
0.00021
lyngbyastatin 9
Sus scrofa
-
in Tris-HCl (pH 8.0)
0.00214
tiglicamide A
Sus scrofa
-
-
0.00699
tiglicamide B
Sus scrofa
-
-
0.00728
tiglicamide C
Sus scrofa
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.31
-
-
7.21 - 8.74
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.4
-
-
8 - 9.5
-
-
8.5
-
-
8.6
Thunnus albacora
-
-
8.7
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
-
-
6.8 - 10.5
-
pH 6.8: about 45% of maximal activity, pH 10.5: about 45% of maximal activity, succinyl-Ala-Ala-Ala-4-nitroanilide
7.3 - 9.2
-
50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 40
-
assay at
45 - 55
Thunnus albacora
-
-
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21900
-
gel filtration
25000
-
gel filtration
26300
-
x * 26300, SDS-PAGE
26500
-
x * 26500, SDS-PAGE
27000
-
x * 27000, SDS-PAGE
28000
-
x * 28000, SDS-PAGE
29000
-
gel filtration
30000
-
gel filtration
30790
-
amino acid analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
side-chain modification
-
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
atomic resolution structure at 1.1 A
-
crystal structure of the enzyme complexed with the inhibitor FR136706, solved at 2.2 A resolution
-
crystallization of the complex of the porcine pancreatic elastase and the hybrid inhibitor HEI-TOE I, hanging-drop vapour diffusion method
-
crystallization under sulfate-free conditions containing 0.3 M NaCl and 50 mM tris(hydroxymethyl)aminomethane-HCl at pH 7.0. Crystal structure determined at 1.5 A resolution has a unique conformation in four regions which contains loop portions; sitting drop vapour diffusion method with 0.3 M NaCl and 50 mM tris(hydroxymethyl)aminomethane-HCl at pH 7.0
-
hanging drop vapour diffusion method, crystal structure of scyptolin A as bound to pancreatic elastase is solved at 2.8 A resolution
-
hanging-drop vapour diffusion method. X-ray structure of a covalent serpin-proteinase complex, alpha1-proteinase inhibitor with pancreatic elastase; in complex with alpha1-proteinase inhibitor, hanging drop vapour diffusion method with 0.2 M bicine buffer, pH 8.1, 60 mM sodium citrate, and 16-18% polyethyleneglycol 3350
-
in complex with inhibitor N-benzyl-2-oxo-4-(phenylsulfonyl)azetidine-1-carboxamide, sitting drop vapour diffusion method, in 200 mM sodium sulfate and 100 mM sodium acetate at pH 5.1
-
in complex with the inhibitor 4-([(S)-1-[((S)-2-[[(RS)-3,3,3-trifluoro-1-isopropyl-2-oxopropyl]aminocarbonyl]pyrrolidin-1-yl-)carbonyl]-2-methylpropyl]aminocarbonyl)benzoic acid, sitting drop vapour diffusion method using 50 mM D-substituted sodium acetate and 0.2-0.3 M sodium sulfate
-
PPE in complex with peptidic inhibitor FR130180 to 1.65 A resolution by neutron crystallography and 1.20 A resolution by X-ray crystallography at ambient temperature
-
structure of a hybrid squash inhibitor, HEI-TOE I, in complex with porcine pancreatic elastase at 1.8 A resolution
-
the pH-jump crystallographuic analyses demonstrates that the side chain of His57 can flip between two conformations, the oxxupancy of which depends upon the pH
-
the squash inhibitor MCE III and the third domain of turkey ovomucoid inhibitor OMTKY3 are crystallized in complexes with porcine pancreatic elastase. Crystals of the complex between MCEI III and pancreatic elastase are grown in citrate buffer with and without ammonium acetate. X-ray diffraction data are collected to 1.9 A resolution at room temperature using synchrotron radiation. The crystals belong to space group P21, with unit-cell parameters a = 49.17 A, beta = 44.59 A, c = 67.08 A, beta = 110-97°. Crystals of the OMTKY3/pancreatic elastase complex are obtained in the presence of ammonium sulfate, MES buffer and polyethylene glycol monomethylether. The crystrals of this complex diffract to 2.1 A resolution and belong to space group I222, with unit-cell parameters a = 84.58, b = 84.61, c = 89.92 A
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
-
-
29635
4 - 10
-
-
36568
4 - 11
-
-
36569
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, 24 hours
Thunnus albacora
-
dialysis, unstable
-
dilute solutions, stable
-
freezing and thawing inactivates
-
when the native structure is achieved, cosolvents increase the stability of the enzyme to the same extent as does the acylation of the active center residue Ser195. Dimethylsulfoxide, glycerol and methanol enhance the stability of the intermediates able to refold into the native form, contrary to acetonitrile
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, pH 6.5, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and ion exchange chromatography
-
chromatofocusing and Superdex-75 gel filtration
-
two forms: EI and EII
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
fecal elastase-1 concentrations correlates negatively with age and are significantly lower among subjects over 70 years old compared to controls
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
renatured by dilution in the solution of substrate at various pHs under agitation. A lag period is observed before reaching the steady state of the hydrolysis of an amide substrate, and the lag period measured with the refolding enzyme is longer than that measured with the native elastase
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
elastase digests yield a large proportion of transmembrane peptides facilitating membrane protein identification
medicine