Biology:Dactylysin
From HandWiki
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
- ↑ "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. doi:10.1073/pnas.89.1.84. PMID 1729723. Bibcode: 1992PNAS...89...84C.
- ↑ "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. doi:10.1016/s0006-291x(05)80125-1. PMID 1531011. https://dipot.ulb.ac.be/dspace/bitstream/2013/57451/5/0f3326bd-1845-413d-9099-7f593c39e91a.txt.
- ↑ "Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme". Biochemistry 32 (23): 5959–66. June 1993. doi:10.1021/bi00074a006. PMID 8507636.
External links
- Dactylysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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