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3.4.24.56: insulysin

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

Word Map on EC 3.4.24.56

Reaction

Degradation of insulin, glucagon and other polypeptides. No action on proteins =

Synonyms

ADE, amyloid degrading enzyme, cgd6_5510, EC 3.4.22.11, EC 3.4.99.10, EC 3.4.99.45, gamma-endorphin-generating enzyme, IDE, INS20-19, insulin degrading enzyme, Insulin protease, Insulin proteinase, Insulin-degrading enzyme, Insulin-degrading neutral proteinase, Insulin-glucagon protease, Insulin-specific protease, Insulinase, Insulysin, Metalloinsulinase, More, pitrilysin metallopeptidase 1, Pitrm1

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.56 insulysin

Crystallization

Crystallization on EC 3.4.24.56 - insulysin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the crystal structure of IDE active site, overview
hanging drop vapor diffusion method, using 0.1 M sodium cacodylate (pH 6.5), 0.2 M MgCl2, and 10% (w/v) PEG-3000 at 18°C
hanging drop vapor diffusion method, X-ray co-crystal structures, including an insulin-degrading enzyme-ligand-glucagon ternary complex, reveal substrate-dependent interactions that enable these inhibitors to potently block insulin binding while allowing glucagon cleavage, even at saturating inhibitor concentrations
IDE in closed conformation
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in complex with bradykinin, to 1.9 A resolution. Bradykinin binds to the exosite. Residue C819 is located inside the catalytic chamber pointing toward an extended hydrophobic pocket. Specific activity similar to wild-type using substrate 7-methoxycoumarin-4-ylacetyl-NPPGFSAFK-2,4-dinitrophenyl
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mutant E111Q in complex with substrates insulin B-chain, amyloid beta-protein, amylin and glucagon. Enzyme forms an enclosed cage just large enough to encapsulate insulin. enclosed substrate undergoes conformational changes to form beta-sheets with two discrete regions of enzyme for degradation
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mutant E111Q, in complex with inhibitors, hanging drop vapor-diffusion method, using 10-13% (w/v) PEG MME 5000, 100 mM HEPES pH 7.0, 4-14% (w/v) tacsimate, 10% (v/v) dioxane
purified recombinant mutant E110Q with bound insulin, hanging drop vapor diffusion method, 0.001 ml of 16-20 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 50 mM NaCl, is mixed with 0.001 ml of reservoir solution containing, 10-13% PEG MME 5000, 100 mM HEPES, pH 7.0, 4-14% tacsimate, and 10% dioxane, equilibration over 0.5 ml of reservoir solution, 18°C, 3-5 days, X-ray diffraction structure determination and analysis at 2.6-2.8 A resolution, molecular replacement
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purified recombinant mutant E11Q in complex with peptide substrate, and substrate-free mutant Y831F, hanging drop vapour diffusion method, 0.001 ml of 15-20 mg/ml protein and 0.001 ml of crystallization solution, containing 10-13% PEGMME 5000, 100 mM HEPES, pH 7.0, 4-14% Tacsimate, and 10% dioxane, are mixed and equilibrated with 0.5 ml of well solution at 18 °C, 3-5 days, cryoprotection by 15-30% glycerol, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution, modeling
X-ray diffraction structure determination and analysis of enzyme-substrate complexes IDE-IGF-II and IDE-TGF-alpha at 2.3 A resolution and IDE-amylin at 2.9 A resolution
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