Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
Reaction(IUBMB)
Hydrolysis of peptides of at least six residues, with bulky hydrophobic residues in the P1' position. Shows a preference for hydrophobic doublets such as -Phe!Phe- and -Phe!Leu- in somatostatin-(1-14)-peptide and dynorphin A-(1-6)-peptide, respectively
Comment
An endopeptidase of 100 kDa secreted from the skin of the amphibian, Xenopus laevis (Dactyletre du Cap). Resembles neprilysin in insensitivity to 1 muM captopril, but differs from it in being insensitive to thiorphan (1 muM) and unable to digest [Met5]enkephalin, [Leu5]enkephalin, oxytocin, and substance P-(7-11)-peptide. A similar endopeptidase is found in human neuroblastoma cells [2]
Delporte C, Carvalho KM, Leseney AM, Winand J, Christophe J, Cohen P.
Title
A new metallo- endopeptidase from human neuroblastoma NB-OK-1 cells which inactivates atrial natriuretic peptide by selective cleavage at the Ser123-Phe124 bond.
