Dactylysin
| Dactylysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.60 | ||||||||
| CAS number | 139466-40-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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
- ↑ Carvalho, K.M.; Joudiou, C.; Boussetta, H.; Leseney, A.-M. & Cohen, P. (1992). "A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion". Proc. Natl. Acad. Sci. USA. 89: 84–88. doi:10.1073/pnas.89.1.84. PMID 1729723.
- ↑ Delporte, C.; Carvalho, K.M.; Leseney, A.-M.; 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: 158–164. doi:10.1016/s0006-291x(05)80125-1. PMID 1531011.
- ↑ Joudiou, C.; Carvalho, K.M.; 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: 5959–5966. doi:10.1021/bi00074a006. PMID 8507636.
External links
- Dactylysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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