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Literature summary for 3.4.24.11 extracted from

  • Pope, D.; Madura, J.D.; Cascio, M.
    beta-Amyloid and neprilysin computational studies identify critical residues implicated in binding specificity (2014), J. Chem. Inf. Model., 54, 1157-1165.
    View publication on PubMed

Application

Application Comment Organism
medicine since accumulation of neurotoxic amyloid beta peptide aggregates in the brain appears to be a causative agent in the pathophysiology of Alzheimer's disease, increased clearance of amyloid beta peptide resulting from overexpression of the enzyme exhibits therapeutic potential for Alzheimer's disease Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc metalloprotease Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
amyloid beta peptide + H2O Homo sapiens degradation ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P08473
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amyloid beta peptide + H2O degradation Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
NEP
-
Homo sapiens

General Information

General Information Comment Organism
additional information protein-ligand docking calculations predict S2' subsite residues Arg102 and Arg110 of the enzyme to participate in specific interactions with amyloid beta peptide and are a target for modification of the enzyme for higher specificity against amyloid beta peptide Homo sapiens