Dactylysin Explained

Dactylysin (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.

Notes and References

1. Carvalho KM, Joudiou C, Boussetta H, Leseney AM, Cohen P . 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 . January 1992 . 1729723 . 48180 . 10.1073/pnas.89.1.84 . 1992PNAS...89...84C . free .
2. Delporte C, Carvalho KM, Leseney AM, Winand J, Christophe J, Cohen P . 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 . January 1992 . 1531011 . 10.1016/s0006-291x(05)80125-1 . 34703070 .
3. Joudiou C, Carvalho KM, Camarao G, Boussetta H, Cohen P . Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme . Biochemistry . 32 . 23 . 5959–66 . June 1993 . 8507636 . 10.1021/bi00074a006 .