ExplorEnz: EC 3.4.24.60

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3.4.24.60

Accepted name:

dactylysin

Reaction:

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

Other name(s):

peptide hormone inactivating endopeptidase; PHIE

Comments:

An endopeptidase of 100 kDa secreted from the skin of the amphibian, Xenopus laevis (Dactylêtre du Cap). Resembles neprilysin in insensitivity to 1 μM captopril, but differs from it in being insensitive to thiorphan (1 μM) 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]

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 139466-40-3

References:

1.	Carvalho, K.M., Joudiou, C., Boussetta, H., Leseney, A.-M. and Cohen, P. A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion. Proc. Natl. Acad. Sci. USA 89 (1992) 84–88. [DOI] [PMID: 1729723]
2.	Delporte, C., Carvalho, K.M., Leseney, A.-M., Winand, J., Christophe, J. and Cohen, P. A new metallo-endopeptidase from human neuroblastoma NB-OK-1 cells which inactivates atrial natriuretic peptide by selective cleavage at the Ser¹²³-Phe¹²⁴ bond. Biochem. Biophys. Res. Commun. 182 (1992) 158–164. [DOI] [PMID: 1531011]
3.	Joudiou, C., Carvalho, K.M., Camarao, G., Boussetta, H. and Cohen, P. Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme. Biochemistry 32 (1993) 5959–5966. [PMID: 8507636]

[EC 3.4.24.60 created 1995]