Leucolysin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.6 leucolysin
Dactylysin is a 100-kDa zinc metalloendopeptidase secreted from the skin of the amphibian Xenopus laevis; a similar endopeptidase occurs in human neuroblastoma cells. Like neprilysin it is insensitive to 1 microM captopril, but unlike neprilysin it is insensitive to thiorphan and cannot digest [Met5]enkephalin, [Leu5]enkephalin, oxytocin and substance P-(7-11). It hydrolyzes peptides of at least six residues with bulky hydrophobic residues at P1', preferring hydrophobic doublets such as -Phe-/-Phe- and -Phe-/-Leu- in somatostatin-(1-14) and dynorphin A-(1-6). In amphibian skin it processes antimicrobial peptides. It features an M13-family zinc catalytic fold.
Dactylysin is a 100-kDa zinc metalloendopeptidase secreted from the skin of the amphibian Xenopus laevis; a similar endopeptidase occurs in human neuroblastoma cells. Like neprilysin it is insensitive to 1 microM captopril, but unlike neprilysin it is insensitive to thiorphan and cannot digest [Met5]enkephalin, [Leu5]enkephalin, oxytocin and substance P-(7-11). It hydrolyzes peptides of at least six residues with bulky hydrophobic residues at P1', preferring hydrophobic doublets such as -Phe-/-Phe- and -Phe-/-Leu- in somatostatin-(1-14) and dynorphin A-(1-6). In amphibian skin it processes antimicrobial peptides. It features an M13-family zinc catalytic fold.
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