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Literature summary for 3.4.21.117 extracted from

  • Shropshire, T.D.; Reifert, J.; Rajagopalan, S.; Baker, D.; Feinstein, S.C.; Daugherty, P.S.
    Amyloid ? peptide cleavage by kallikrein 7 attenuates fibril growth and rescues neurons from Abeta-mediated toxicity in vitro (2014), Biol. Chem., 395, 109-118.
    View publication on PubMed
Search for more literature for 3.4.21.117

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-amyloid peptide + H2O Rattus norvegicus degradation, the enzyme cleaves after both Phe residues within the core of Abeta42 in vitro, thereby inhibiting A? fibril formation and promoting the degradation of preformed fibrils ?
-
 ?
additional information Rattus norvegicus the enzyme shows a unique extended chymotrypsin-like specificity and beta-amyloid peptide-degrading capacity ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-amyloid peptide + H2O degradation Rattus norvegicus ?
-
 ?
beta-amyloid peptide + H2O degradation, the enzyme cleaves after both Phe residues within the core of Abeta42 in vitro, thereby inhibiting A? fibril formation and promoting the degradation of preformed fibrils Rattus norvegicus ?
-
 ?
additional information the enzyme shows a unique extended chymotrypsin-like specificity and beta-amyloid peptide-degrading capacity Rattus norvegicus ?
-
 ?
additional information the enzyme's consensus motif is RX0(Y/F)-/-(Y/F)-/-(S/A/G/T) or RX0(Y/F)-/-(S/T/A) (0 = hydrophobic) Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
kallikrein 7
-
 Rattus norvegicus
KLK7
-
 Rattus norvegicus

General Information

General Information Comment Organism
physiological function the treatment of beta-amyloid oligomer preparations with the enzyme, but not the inactive proform, significantly reduces Abeta42-mediated toxicity to rat hippocampal neurons to the same extent as the known Abeta-degrading protease insulin-degrading enzyme Rattus norvegicus