KEGG   ENZYME: 3.4.24.60Help
Entry
EC 3.4.24.60                Enzyme                                 

Name
dactylysin;
peptide hormone inactivating endopeptidase;
PHIE
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
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
Comment
An endopeptidase of 100 kDa secreted from the skin of the amphibian, Xenopus laevis (Dactyletre du Cap). Resembles neprilysin in insensitivity to 1 muM captopril, but differs from it in being insensitive to thiorphan (1 muM) 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]
History
EC 3.4.24.60 created 1995
Reference
1  [PMID:1729723]
  Authors
Carvalho KM, Joudiou C, Boussetta H, Leseney AM, Cohen P.
  Title
A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 84-8.
Reference
2  [PMID:1531011]
  Authors
Delporte C, Carvalho KM, Leseney AM, Winand J, Christophe J, Cohen P.
  Title
A new metallo- endopeptidase from human neuroblastoma NB-OK-1 cells which inactivates atrial natriuretic peptide by selective cleavage at the Ser123-Phe124 bond.
  Journal
Biochem. Biophys. Res. Commun. 182 (1992) 158-64.
Reference
3  [PMID:8507636]
  Authors
Joudiou C, Carvalho KM, Camarao G, Boussetta H, Cohen P.
  Title
Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme.
  Journal
Biochemistry. 32 (1993) 5959-66.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
139466-40-3

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