|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Undetermined; a substrate lacks a chemical formula
Enzyme Commission Primary Name: dactylysin
Enzyme Commission Synonyms: peptide hormone inactivating endopeptidase, PHIE
Enzyme Commission Summary:
This enzyme catalyzes 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.
An endopeptidase of 100 kDa secreted from the skin of the amphibian, Xenopus laevis (DactylÍtre du Cap). Resembles neprilysin in insensitivity to 1 M captopril, but differs from it in being insensitive to thiorphan (1 M) and unable to digest [Met5]enkephalin, [Leu5]enkephalin, oxytocin, and substance P-(7-11)-peptide. A similar endopeptidase is found in human neuroblastoma cells [Delporte92].
Carvalho92: Carvalho KM, Joudiou C, Boussetta H, Leseney AM, Cohen P (1992). "A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion." Proc Natl Acad Sci U S A 89(1);84-8. PMID: 1729723
Delporte92: Delporte C, Carvalho KM, Leseney AM, 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(1);158-64. PMID: 1531011
Joudiou93: Joudiou C, Carvalho KM, 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(23);5959-66. PMID: 8507636
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