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Dactylysin

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Dactylysin
Identifiers
EC no.3.4.24.60
CAS no.139466-40-3
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IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
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MetaCycmetabolic pathway
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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

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  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. 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.
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