Dactylysin

Dactylysin
Identifiers
EC number	3.4.24.60
CAS number	139466-40-3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Dactylysin (EC 3.4.24.60, peptide hormone inactivating endopeptidase, PHIE) is an enzyme.^[1][2][3] This enzyme catalyses the following chemical 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

This endopeptidase in the skin of the amphibian, Xenopus laevis.

References

1. Carvalho, K.M., Joudiou, C., Boussetta, H., Leseney, A.-M. and Cohen, P. (1992). "A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion". Proc. Natl. Acad. Sci. USA 89: 84–88. doi:10.1073/pnas.89.1.84. PMID 1729723.
2. Delporte, C., Carvalho, K.M., Leseney, A.-M., Winand, J., Christophe, J. and Cohen, P. (1992). "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: 158–164. doi:10.1016/s0006-291x(05)80125-1. PMID 1531011.
3. Joudiou, C., Carvalho, K.M., Camarao, G., Boussetta, H. and Cohen, P. (1993). "Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme". Biochemistry 32: 5959–5966. doi:10.1021/bi00074a006. PMID 8507636.

External links

• Dactylysin at the US National Library of Medicine Medical Subject Headings (MeSH)