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Dactylysin

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Template:Infobox enzyme 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 Edit

  1. Carvalho, K.M., Joudiou, C., Boussetta, H., Leseney, A.-M. and Cohen, P. (1992). A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion. Proc. Natl. Acad. Sci. USA 89: 84–88.
  2. Delporte, C., Carvalho, K.M., Leseney, A.-M., Winand, J., Christophe, J. and 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.
  3. Joudiou, C., Carvalho, K.M., Camarao, G., Boussetta, H. and Cohen, P. (1993). Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme. Biochemistry 32: 5959–5966.

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