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Information on EC 3.4.21.36 - pancreatic elastase and Organism(s) Sus scrofa and UniProt Accession P00772
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3.4.21.36 pancreatic elastaseSpecify your search results
Word Map
- 3.4.21.36
- porcine
-
exocrine
- emphysema
-
fecal
- elastin
- pancreas
- leukocyte
- pulmonary
-
elastase-induced
- elastases
-
instil
-
intratracheal
- amylase
- abdominal
- alveolar
-
stool
- aortic
- aaa
-
elastolytic
- aneurysm
-
lavage
-
bronchoalveolar
- proteinases
-
emphysematous
-
airspace
- hne
-
intercept
- alpha-chymotrypsin
- steatorrhea
-
1-antitrypsin
-
2-macroglobulin
-
1-proteinase
-
elastase-treated
- analysis
-
elastase-mediated
- elastatinal
-
maldigestion
- isoamylase
-
cholangiopancreatography
-
alpha-1-proteinase
-
procarboxypeptidase
-
antiprotease
-
antielastase
-
intra-aortic
- medicine
- ovomucoid
-
non-pancreatic
-
pancreatoduodenectomy
-
carlsberg
- desmosine
-
3.4.21.1
-
elastase-like
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
pancreatic elastase, elastase 1, elastase-1, cela1, serine elastase, pancreatic elastase-1, cela3b, chymotrypsin-like elastase, prt-201, cela3a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
elastase
elaszym
-
-
-
-
pancreatic elastase I
-
-
-
-
pancreatopeptidase E
-
-
-
-
peptidase, pancreato-, E
-
-
-
-
serine elastase
-
-
-
-
elastase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
848900-32-3
-
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
succinyl-Ala-Ala-Ala-p-nitroanilide + H2O
succinyl-Ala-Ala-Ala + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Phe + 4-nitroaniline
-
-
?
succinyl-Ala-Ala-Pro-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Ala-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Ala + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-alpha-aminobutyric acid-4-nitroanilide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Ala-4-nitrophenol ester + H2O
t-butyloxycarbonyl-Ala + 4-nitrophenol
-
-
-
-
?
succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-([(S)-1-[((S)-2-[[(RS)-3,3,3-trifluoro-1-isopropyl-2-oxopropyl]aminocarbonyl]pyrrolidin-1-yl-)carbonyl]-2-methylpropyl]aminocarbonyl)benzoic acid
-
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
HEI-TOE I
hybrid inhibitor from Ecballium elaterium and the optimized binding loop of the third domain of turkey ovomucoid inhibitor
-
OMTKY3
third Kazal-type domain of ovomucoid inhibitor from turkey egg white
-
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
(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
-
-
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
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
HEI-TOE I
-
hybrid inhibitor from Ecballium elaterium and the optimized binding loop of the third domain of turkey ovomucoid inhibitor
-
N-(trifluoroacetyl)-alpha-aspartyl-N-[4-(trifluoromethyl)phenyl]alaninamide
-
reversible inhibitor
N-(trifluoroacetyl)leucyl-N-[4-(trifluoromethyl)phenyl]alaninamide
-
reversible inhibitor
N-(trifluoroacetyl)valyl-N-[4-(trifluoromethyl)phenyl]alaninamide
-
reversible inhibitor
N-benzyl-2-oxo-4-(phenylsulfonyl)azetidine-1-carboxamide
-
JM54, potent and irreversible inhibitor
N2-(trifluoroacetyl)lysyl-N-[4-(trifluoromethyl)phenyl]alaninamide
-
reversible inhibitor
Schistocerca gregaria proteinase inhibitor 2 variant E1
-
Tyr-Cys-Thr-Leu-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E10
-
Ala-Cys-Thr-Leu-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E11
-
Ala-Cys-Thr-Leu-Met-Tyr-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E12
-
Tyr-Cys-Thr-Leu-Met-Leu-Cys-Ala
-
Schistocerca gregaria proteinase inhibitor 2 variant E2
-
Tyr-Cys-Thr-Ile-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E3
-
Tyr-Cys-Thr-Val-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E4
-
Tyr-Cys-Thr-Met-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E5
-
Tyr-Cys-Thr-Ala-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E6
-
Tyr-Cys-Thr-Ser-Met-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E7
-
Tyr-Cys-Thr-Ile-Met-Glu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E8
-
Tyr-Cys-Thr-Leu-Arg-Leu-Cys-His
-
Schistocerca gregaria proteinase inhibitor 2 variant E9
-
Tyr-Cys-Thr-Leu-Met-Tyr-Cys-His
-
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
-
viral serpin crmA
-
pancreatic elastase is rapidly inhibited by wild-type crmA and reactive loop variant P1 Arg crmAs
-
additional information
-
not inhibited by dehydroepiandrosterone sulfate, pregnenolone sulfate, cholesterol, oleic acid, triolein, phosphatidylethanolamine, phosphatidylcholine, phosphatidylserine, sphingomyelin, GalCer, LacCer
-
additional information
-
the peptide RC-12 does not inhibit pancreatic elastase at concentrations up to 0.1 mM
-
additional information
-
an oligomeric fraction of procyanidins shows about 90% inhibition at 0.2 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
spermidine
-
spermidine serves as a partial stabilizer and an activator for the enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.555
succinyl-L-Ala-L-Ala-L-Pro-Gly-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
0.166
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
0.995
succinyl-L-Ala-L-Ala-L-Pro-L-Ile-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
0.785
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
0.54
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
2.311
succinyl-L-Ala-L-Ala-L-Pro-L-Ser-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
1.029
succinyl-L-Ala-L-Ala-L-Pro-L-Val-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
0.08229
4-nitrophenyl acetate
-
in the presence of 0.2 mM spermidine, at pH 8.5 and 37°C
0.09364
4-nitrophenyl acetate
-
in the presence of 0.3 mM spermidine, at pH 8.5 and 37°C
0.11568
4-nitrophenyl acetate
-
in the presence of 0.5 mM spermidine, at pH 8.5 and 37°C
2.09
succinyl-L-Ala-L-Ala-L-Ala-4-nitroanilide
-
in 0.1 M phosphate buffer, pH 7.0 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.86
succinyl-L-Ala-L-Ala-L-Pro-Gly-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
115
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
2.87
succinyl-L-Ala-L-Ala-L-Pro-L-Ile-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
57.8
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
0.7
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
5.62
succinyl-L-Ala-L-Ala-L-Pro-L-Ser-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
16.9
succinyl-L-Ala-L-Ala-L-Pro-L-Val-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
0.007
4-nitrophenyl acetate
-
in the presence of 0.2 mM spermidine, at pH 8.5 and 37°C
0.0092
4-nitrophenyl acetate
-
in the presence of 0.3 mM spermidine, at pH 8.5 and 37°C
0.0125
4-nitrophenyl acetate
-
in the presence of 0.5 mM spermidine, at pH 8.5 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
succinyl-L-Ala-L-Ala-L-Pro-Gly-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
690
succinyl-L-Ala-L-Ala-L-Pro-L-Ala-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
2.9
succinyl-L-Ala-L-Ala-L-Pro-L-Ile-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
74
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
1.3
succinyl-L-Ala-L-Ala-L-Pro-L-Met-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
2.4
succinyl-L-Ala-L-Ala-L-Pro-L-Ser-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
17
succinyl-L-Ala-L-Ala-L-Pro-L-Val-4-nitroanilide
-
isoform CELA1, at pH 8.0 and 22°C
0.085
4-nitrophenyl acetate
-
in the presence of 0.2 mM spermidine, at pH 8.5 and 37°C
0.097
4-nitrophenyl acetate
-
in the presence of 0.3 mM spermidine, at pH 8.5 and 37°C
0.107
4-nitrophenyl acetate
-
in the presence of 0.5 mM spermidine, at pH 8.5 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
Bovine pancreatic trypsin inhibitor
pH and temperature not specified in the publication
-
0.0000236
N-(trifluoroacetyl)leucyl-N-[4-(trifluoromethyl)phenyl]alaninamide
-
at pH 8.0 and 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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). CELA1_PIG
266
0
28821
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging drop vapour diffusion method, crystal structure of scyptolin A as bound to pancreatic elastase is solved at 2.8 A resolution
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 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
sitting drop vapour diffusion method with 0.3 M NaCl and 50 mM tris(hydroxymethyl)aminomethane-HCl at pH 7.0
apoenzyme and enzyme in complex with inhibitor JM102, hanging drop vapor diffusion method, using 200 mM sodium sulfate, 100 mM sodium acetate pH 5.1
-
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
hanging-drop vapour diffusion method. X-ray structure of a covalent serpin-proteinase complex, alpha1-proteinase inhibitor with pancreatic elastase
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
-
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
LITERATURE
analysis
elastase digests yield a large proportion of transmembrane peptides facilitating membrane protein identification
medicine
-
intratracheal administration of two doses of ELT induces a proinflammatory response in the lung that is characterized by significant infiltration of macrophages and an increased level of interleukin-1beta in lung homogenates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Powers, J.C.; Gupton, B.F.; Harley, A.D.; Nishino, N.; Whitley, R.J.
Specificity of porcine pancreatic elastase, human leukocyte elastase and cathepsin G. Inhibition with peptide chloromethyl ketones
Biochim. Biophys. Acta
485
156-166
1977
Sus scrofa
Katagiri, K.; Takeuchi, T.; Taniguchi, K.; Sasaki, M.
One step purification procedure of elastase from pancreatic powder by affinity chromatography
Anal. Biochem.
86
159-165
1978
Sus scrofa
Ardelt, W.
Partial purification and properties of porcine pancreatic elastase II
Biochim. Biophys. Acta
341
318-326
1974
Sus scrofa
Tsunemi, M.; Matsuura, Y.; Sakakibara, S.; Katsube, Y.
Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 A resolution
Biochemistry
35
11570-11576
1996
Sus scrofa (P00772), Sus scrofa
Tsunemi, M.; Matsuura, Y.; Sakakibara, S.; Katsube, Y.
Crystallization of a complex between an elastase-specific inhibitor elafin and porcine pancreatic elastase
J. Mol. Biol.
232
310-311
1993
Sus scrofa
Mattos, C.; Gianmmona, D.A.; Petsko, G.A.; Ringe, D.
Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors
Biochemistry
34
3193-3203
1995
Sus scrofa
Bode, W.; Meyer Jr., E.; Powers, J.C.
Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors
Biochemistry
28
1951-1963
1989
Sus scrofa
Plaskon, R.R.; Kam, C.M.; Burgess, E.M.; Powers, J.C.; Suddath, F.L.
Michaelis complexes of porcine pancreatic elastase with 7-[(alkylcarbamoyl)amino]-4-chloro-3-ethoxyisocoumarins: translational sampling of inhibitor position and kinetic measurements
Proteins
13
141-151
1992
Sus scrofa
Wurtele, M.; Hahn, M.; Hilpert, K.; Hohne, W.
Atomic resolution structure of native porcine pancreatic elastase at 1.1 A
Acta Crystallogr. Sect. D
56
520-523
2000
Sus scrofa
-
Hilpert, K.; Schneider-Mergener, J.; Ay, J.
Crystallization and preliminary X-ray analysis of the complex of porcine pancreatic elastase and a hybrid squash inhibitor
Acta Crystallogr. Sect. D
58
672-674
2002
Sus scrofa (P00772), Sus scrofa
Ay, J.; Hilpert, K.; Krauss, N.; Schneider-Mergener, J.; Hohne, W.
Structure of a hybrid squash inhibitor in complex with porcine pancreatic elastase at 1.8 A resolution
Acta Crystallogr. Sect. D
59
247-254
2003
Sus scrofa
Jaspard, E.
Role of protein-solvent interactions in refolding. Effects of cosolvent additives on the renaturation of porcine pancreatic elastase at various pHs
Arch. Biochem. Biophys.
375
220-228
2000
Sus scrofa
Wright, P.A.; Wilmouth, R.C.; Clifton, I.J.; Schofield, C.J.
'pH-jump' crystallographic analyses of gamma-lactam-porcine pancreatic elastase complexes
Biochem. J.
351
335-340
2000
Sus scrofa
-
Kinoshita, T.; Nakanishi, I.; Sato, A.; Tada, T.
True interaction mode of porcine pancreatic elastase with FR136706, a potent peptidyl inhibitor
Bioorg. Med. Chem. Lett.
13
21-24
2003
Sus scrofa (P00772), Sus scrofa
Matern, U.; Schleberger, C.; Jelakovic, S.; Weckesser, J.; Schulz, G.E.
Binding structure of elastase inhibitor scyptolin A
Chem. Biol.
10
997-1001
2003
Sus scrofa (P00772), Sus scrofa
Hilpert, K.; Wessner, H.; Schneider-Mergener, J.; Welfle, K.; Misselwitz, R.; Welfle, H.; Hocke, A.C.; Hippenstiel, S.; Hohne, W.
Design and characterization of a hybrid miniprotein that specifically inhibits porcine pancreatic elastase
J. Biol. Chem.
278
24986-24993
2003
Sus scrofa (P00772), Sus scrofa
Ito, N.; Iwamori, Y.; Hanaoka, K.; Iwamori, M.
Inhibition of pancreatic elastase by sulfated lipids in the intestinal mucosa
J. Biochem.
123
107-114
1998
Sus scrofa
Kinoshita, T.; Yamaguchi, A.; Tada, T.
Tris(hydroxymethyl)aminomethane induces conformational change and crystal-packing contraction of porcine pancreatic elastase
Acta Crystallogr. Sect. F
62
623-626
2006
Sus scrofa, Sus scrofa (P00772)
Dementiev, A.; Dobo, J.; Gettins, P.G.
Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase
J. Biol. Chem.
281
3452-3457
2006
Sus scrofa, Sus scrofa (P00772)
Hilpert, K.; Wessner, H.; Scholz, C.; Scheerer, P.; Volkmer-Engert, R.; Kraubeta, N.
Crystallization and preliminary X-ray analysis of complexes of porcine pancreatic elastase with two natural inhibitors
Protein Pept. Lett.
11
393-399
2004
Sus scrofa
Tesch, L.D.; Raghavendra, M.P.; Bedsted-Faarvang, T.; Gettins, P.G.; Olson, S.T.
Specificity and reactive loop length requirements for crmA inhibition of serine proteases
Protein Sci.
14
533-542
2005
Sus scrofa
Kinoshita, T.; Tamada, T.; Imai, K.; Kurihara, K.; Ohhara, T.; Tada, T.; Kuroki, R.
Crystallization of porcine pancreatic elastase and a preliminary neutron diffraction experiment
Acta Crystallogr. Sect. F
63
315-317
2007
Sus scrofa (P00772), Sus scrofa
Oliveira, T.F.; Mulchande, J.; Moreira, R.; Iley, J.; Archer, M.
Crystallization and preliminary diffraction studies of porcine pancreatic elastase in complex with a novel inhibitor
Protein Pept. Lett.
14
93-95
2007
Sus scrofa
Suzuki, M.; Betsuyaku, T.; Ito, Y.; Nagai, K.; Odajima, N.; Moriyama, C.; Nasuhara, Y.; Nishimura, M.
Curcumin attenuates elastase- and cigarette smoke-induced pulmonary emphysema in mice
Am. J. Physiol. Lung Cell Mol. Physiol.
296
L614-L623
2009
Sus scrofa
Conlon, J.M.; Raza, H.; Coquet, L.; Jouenne, T.; Leprince, J.; Vaudry, H.; King, J.D.
Purification of peptides with differential cytolytic activities from the skin secretions of the Central American frog, Lithobates vaillanti (Ranidae)
Comp. Biochem. Physiol. C
150
150-154
2009
Sus scrofa
Tamada, T.; Kinoshita, T.; Kurihara, K.; Adachi, M.; Ohhara, T.; Imai, K.; Kuroki, R.; Tada, T.
Combined high-resolution neutron and X-ray analysis of inhibited elastase confirms the active-site oxyanion hole but rules against a low-barrier hydrogen bond
J. Am. Chem. Soc.
131
11033-11040
2009
Sus scrofa (P00772), Sus scrofa
Inoue, K.; Koike, E.; Yanagisawa, R.; Takano, H.
Extensive analysis of elastase-induced pulmonary emphysema in rats: ALP in the lung, a new biomarker for disease progression?
J. Clin. Biochem. Nutr.
46
168-176
2010
Sus scrofa
Kwan, J.C.; Taori, K.; Paul, V.J.; Luesch, H.
Lyngbyastatins 8-10, elastase inhibitors with cyclic depsipeptide scaffolds isolated from the marine cyanobacterium Lyngbya semiplena
Mar. Drugs
7
528-538
2009
Sus scrofa
Rietschel, B.; Arrey, T.; Meyer, B.; Bornemann, S.; Schuerken, M.; Karas, M.; Poetsch, A.
Elastase digests: New ammunition for shotgun membrane proteomics
Mol. Cell. Proteomics
8
1029-1043
2009
Sus scrofa (P00772), Sus scrofa
Matthew, S.; Paul, V.J.; Luesch, H.
Tiglicamides A-C, cyclodepsipeptides from the marine cyanobacterium Lyngbya confervoides
Phytochemistry
70
2058-2063
2009
Sus scrofa
Bras, N.F.; Goncalves, R.; Fernandes, P.A.; Mateus, N.; Ramos, M.J.; de Freitas, V.
Understanding the binding of procyanidins to pancreatic elastase by experimental and computational methods
Biochemistry
49
5097-5108
2010
Sus scrofa
Bras, N.F.; Goncalves, R.; Mateus, N.; Fernandes, P.A.; Ramos, M.J.; de Freitas, V.
Inhibition of pancreatic elastase by polyphenolic compounds
J. Agric. Food Chem.
58
10668-10676
2010
Sus scrofa
Qasim, M.A.; Wang, L.; Qasim, S.; Lu, S.; Lu, W.; Wynn, R.; Yi, Z.P.; Laskowski, M.
Additivity-based design of the strongest possible turkey ovomucoid third domain inhibitors for porcine pancreatic elastase (PPE) and Streptomyces griseus protease B (SGPB)
FEBS Lett.
587
3021-3026
2013
Sus scrofa
Hofbauer, S.; Brito, J.A.; Mulchande, J.; Nogly, P.; Pessanha, M.; Moreira, R.; Archer, M.
Stabilization of porcine pancreatic elastase crystals by glutaraldehyde cross-linking
Acta Crystallogr. Sect. F
71
1346-1351
2015
Sus scrofa
Sadeghi-Kaji, S.; Shareghi, B.; Saboury, A.A.; Farhadian, S.
Spectroscopic and molecular docking studies on the interaction between spermidine and pancreatic elastase
Int. J. Biol. Macromol.
131
473-483
2019
Sus scrofa
Boros, E.; Szabo, A.; Zboray, K.; Heja, D.; Pal, G.; Sahin-Toth, M.
Overlapping specificity of duplicated human pancreatic elastase 3 isoforms and archetypal porcine elastase 1 provides clues to evolution of digestive enzymes
J. Biol. Chem.
292
2690-2702
2017
Homo sapiens, Sus scrofa
Stergiou, P.Y.; Foukis, A.; Gkini, O.A.; Bieth, J.G.; Papamichael, E.M.
Kinetic and computational analysis of the reversible inhibition of porcine pancreatic elastase a structural and mechanistic approach
J. Enzyme Inhib. Med. Chem.
31
131-139
2016
Sus scrofa
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