Dactylysin

Dactylysin
Identifiers
EC no.	3.4.24.60
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

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

1. Carvalho KM, Joudiou C, Boussetta H, Leseney AM, Cohen P (January 1992). "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. Bibcode:1992PNAS...89...84C. doi: 10.1073/pnas.89.1.84 . PMC   48180 . PMID   1729723.
2. Delporte C, Carvalho KM, Leseney AM, Winand J, Christophe J, Cohen P (January 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". Biochemical and Biophysical Research Communications. 182 (1): 158–64. doi:10.1016/s0006-291x(05)80125-1. hdl: 2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/57451 . PMID   1531011. S2CID   34703070.
3. Joudiou C, Carvalho KM, Camarao G, Boussetta H, Cohen P (June 1993). "Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme". Biochemistry. 32 (23): 5959–66. doi:10.1021/bi00074a006. PMID   8507636.

External links

• Dactylysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)