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3.4.24.60: dactylysin

This is an abbreviated version!
For detailed information about dactylysin, go to the full flat file.

Word Map on EC 3.4.24.60

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 =

Synonyms

Peptide hormone inactivating endopeptidase, peptide hormone inactivating enzyme, PHIE

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.60 dactylysin

Reference

Reference on EC 3.4.24.60 - dactylysin

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Delporte, C.; Carvalho, K.M.; Leseney, A.M.; Winand, J.; Christophe, J.; Cohen, P.
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
1992
Homo sapiens
Manually annotated by BRENDA team
Carvalho, K.M.; Joudiou, C.; Boussetta, H.; Leseney, A.M.; Cohen, P.
A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion
Proc. Natl. Acad. Sci. USA
89
84-88
1992
Xenopus laevis
Manually annotated by BRENDA team
Joudiou, C.; Carvalho, K.M.; Camarao, G.; Boussetta, H.; Cohen, P.
Characterization of the thermolysin-like cleavage of biologically active peptides by Xenopus laevis peptide hormone inactivating enzyme
Biochemistry
32
5959-5966
1993
Xenopus laevis
Manually annotated by BRENDA team
Clamagirand, C.; Joudiou, C.; Cohen, P.
Dactylysin
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
1042-1044
2004
Xenopus laevis
-
Manually annotated by BRENDA team