Dactylysin

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
Dactylysin
Identifiers
EC number3.4.24.60
CAS number139466-40-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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

References
  1. Carvalho KM, Joudiou C, Boussetta H, Leseney AM, Cohen P (January 1992). "A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion". Proceedings of the National Academy of Sciences of the United States of America. 89 (1): 84–8. doi:10.1073/pnas.89.1.84. PMC 48180. PMID 1729723.
  2. Delporte C, Carvalho KM, Leseney AM, Winand J, Christophe J, Cohen P (January 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". Biochemical and Biophysical Research Communications. 182 (1): 158–64. doi:10.1016/s0006-291x(05)80125-1. PMID 1531011.
  3. Joudiou C, Carvalho KM, Camarao G, Boussetta H, Cohen P (June 1993). "Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme". Biochemistry. 32 (23): 5959–66. doi:10.1021/bi00074a006. PMID 8507636.


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