| 词条 | Dactylysin |
| 释义 |
| Name = Dactylysin | EC_number = 3.4.24.60 | CAS_number = 139466-40-3 | IUBMB_EC_number = 3/4/24/60 | GO_code = | image = | width = | caption = }}Dactylysin ({{EC number|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. References1. ^{{cite journal | title = A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion |author = Carvalho, K.M. |author2 = Joudiou, C. |author3 = Boussetta, H. |author4 = Leseney, A.-M. |author5 = Cohen, P. |last-author-amp = yes |journal = Proc. Natl. Acad. Sci. USA |year = 1992 |volume = 89 |pages = 84–88 |pmid = 1729723 |doi=10.1073/pnas.89.1.84 |pmc=48180}} 2. ^{{cite journal | 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 |author = Delporte, C. |author2 = Carvalho, K.M. |author3 = Leseney, A.-M. |author4 = Winand, J. |author5 = Christophe, J. |author6 = Cohen, P. |last-author-amp = yes |journal = Biochem. Biophys. Res. Commun. |year = 1992 |volume = 182 |pages = 158–164 |pmid = 1531011 |doi=10.1016/s0006-291x(05)80125-1}} 3. ^{{cite journal | title = Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme |author = Joudiou, C. |author2 = Carvalho, K.M. |author3 = Camarao, G. |author4 = Boussetta, H. |author5 = Cohen, P. |last-author-amp = yes |journal = Biochemistry |year = 1993 |volume = 32 |pages = 5959–5966 |pmid = 8507636 |doi=10.1021/bi00074a006}} External links
1 : EC 3.4.24 |
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