The Enzyme Database

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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
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 created 1995]

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