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
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3.4.24.60
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metalloendopeptidase
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dibasic
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convertase
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n-arginine
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ectodomain
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factor-like
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adam17
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heparin-binding
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disintegrin
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hb-egf
- 3.4.24.60
- metalloendopeptidase
-
dibasic
-
convertase
-
n-arginine
-
ectodomain
-
factor-like
-
adam17
-
heparin-binding
-
disintegrin
-
hb-egf
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
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Reference
Reference on EC 3.4.24.60 - dactylysin
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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
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
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
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
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