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3.4.21.36: pancreatic elastase

This is an abbreviated version!
For detailed information about pancreatic elastase, go to the full flat file.

Word Map on EC 3.4.21.36

Reaction

Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-/- =

Synonyms

CELA1, CELA3A, CELA3B, chymotrypsin-like elastase, EC 3.4.21.11, EC 3.4.4.7, elastase, elastase 1, elastase-1, elaszym, ELT, FE1, pancreatic elastase, pancreatic elastase 3, pancreatic elastase 3B, pancreatic elastase I, pancreatic elastase-1, pancreatopeptidase E, PE 3B, PE-1, peptidase, pancreato-, E, PPE, PRT-201, serine elastase, type I pancreatic elastase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.36 pancreatic elastase

Crystallization

Crystallization on EC 3.4.21.36 - pancreatic elastase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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atomic resolution structure at 1.1 A
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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
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
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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
structure of a hybrid squash inhibitor, HEI-TOE I, in complex with porcine pancreatic elastase at 1.8 A resolution
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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
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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
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