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3.4.24.11: neprilysin

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

Word Map on EC 3.4.24.11

Reaction

preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1' =

Synonyms

Abeta-degrading enzyme, acute lymphoblastic leukemia antigen, antigen, CALLA (common acute lymphoblastic leukemia-associated), atriopeptidase, CALLA, CALLA (common acute lymphoblastic leukemia-associated) antigens, CALLA antigen, CALLA glycoproteins, CD10, CD10/neutral endopeptidase, CD10/neutral endopeptidase 24.11, common acute lymphoblastic leukemia antigen, common acute lymphoblastic leukemia-associated antigens, Common acute lymphocytic leukemia antigen, endopeptidase CD10, Endopeptidase-2, endopeptidase-24.11, enkephalinase, EP24.11, glycoprotein, CALLA, kidney-brush-border neutral endopeptidase, kidney-brush-border neutral peptidase, kidney-brush-border neutral proteinase, membrane metallo-endopeptidase, membrane metalloendopeptidase, MME, NEP, NEP 24.11, NEP, enkephalinase, neutrophil cluster-differentiation antigen 10, common acute lymphoblastic leukemia antigen, NEP-1, NEP/CD10, NEP2, NEP4A, NEP4B, neprilypsin, neprilysin, neprilysin 4, neutral endopeptidase, neutral endopeptidase 24.11, neutral endopeptidase 24.11/CD10, neutral metallendopeptidase, NL-1, peptidase, endo-, peptidase, membrane metalloendo-, SEP, skin fibroblast elastase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.11 neprilysin

Crystallization

Crystallization on EC 3.4.24.11 - neprilysin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3D-QSAR studies on mercaptodipeptide inhibitors, using CoMFA and CoMSIA techniques and based on data of PDB entry 1R1I
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crystal structures of the soluble extracellular domain of neprilysin (residues 52-749) complexed with various potent and competitive inhibitors. Vapour diffusion with 25% PEG 3350, 200 mM ammonium sulfate, 100 mM bis-tris, pH 7.5
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isolated extracellular catalytic domain of human neprilysin, 8 mg/ml protein in 25 mM Tris, 150 mM NaCl, and 2 mM MgCl2, pH 7.5, are mixed 1:1 with crystallisation buffer containing 0.2 M KNO3 and 20% w/v PEG 3350, 18°C, 1 month, X-ray diffracton structure determination and analysis at 1.9 A resolution
purified recombinant enzyme mutant G399V/G714K in complex with inhibitor phorphoramidon, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 25 mM Tris-HCl, pH 7.0, 150 mM NaCl and 2 mM MgCl2 with 2 mM phosphoramidon, 0.001 ml of reservoir solution containing 100 mM HEPES, pH 7.0, 22% w/v PEG3350 and 200 mM NaCl, at 20°C, 2 weeks, rod shaped crystals, improvement by streak seeding, X-ray diffraction structure determination and analysis at 2.15 A resolution, modeling
purified recombinant extracellular domain of human NEP (residues 54-749) in complex with LBQ657, hanging drop vapor diffusion method, mixing of 10 mg/ml protein in 20 mM Tris, pH 8.0, 125 mM NaCl, 2 mM MgCl2 and 1 mM in a 1:1 ratio with reservoir solution containing 25% w/v PEG 3350, 200 mM ammonium acetate, and 100 mM BisTris, pH 6.5, room temperature, overnight, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement