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

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. & 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. PMC 48180. PMID 1729723.
  2. ↑ Delporte, C.; Carvalho, K.M.; Leseney, A.-M.; Winand, J.; Christophe, J. & 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. & 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.


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