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Information on EC 3.4.24.60 - dactylysin
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3.4.24.60 dactylysinSpecify your search results
Word Map
- 3.4.24.60
- metalloendopeptidase
-
dibasic
-
convertase
-
n-arginine
-
ectodomain
-
factor-like
-
adam17
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heparin-binding
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disintegrin
-
hb-egf
The expected taxonomic range for this enzyme is: Tetrapoda
Reaction Schemes
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
dactylysin, peptide hormone inactivating endopeptidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Peptide hormone inactivating endopeptidase
-
-
-
-
PHIE
PHIE
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
139466-40-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(19-28)ANF peptide + H2O
?
-
i.e. atrial natriuretic factor derived peptide, cleavage site: Gly20-Leu21
-
-
?
(20-28)ANF peptide + H2O
?
-
i.e. atrial natriuretic factor derived peptide
-
-
?
(21-28)ANF octapeptide + H2O
?
-
i.e. atrial natriuretic factor derived peptide
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-
?
(22-28)ANF heptapeptide + H2O
?
-
i.e. atrial natriuretic factor derived peptide
-
-
?
(23-28)ANF hexapeptide + H2O
?
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i.e. atrial natriuretic factor derived peptide
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-
?
(5-11)Substance P heptapeptide + H2O
?
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i.e. Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2, cleavage site: Gly9-Leu10
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-
?
(6-11)Substance P hexapeptide + H2O
?
-
i.e. Gln-Phe-Phe-Gly-Leu-Met-NH2, cleavage site: Gly9-Leu10
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-
?
ANP-(103-126) + H2O
ANP-(103-123) + Phe124-Arg125-Tyr126
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i.e. atrial natriuretic peptide, cleavage sites: Xaa-Phe, Xaa-Leu or Xaa-Ile bonds
-
?
Asp-Ala-Asp-Thr-Cys-[D-Arg8]-kermit + H2O
?
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model substrate, derivative of kermit, cleavage site: Ser12-Phe13
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-
?
atrial natriuretic factor + H2O
LGCNS + Phe-Arg-Tyr
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cleavage of Ser-Phe
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-
?
Neuromedin B + H2O
?
-
i.e. Gly-Asn-Leu-Trp-Ala-Thr-Gly-His-Phe-Met-NH2, major cleavage site: His8-Phe9, minor site: Gly7-His8
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-
?
peptide PglA + H2O
?
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antimicrobial peptide of Xenopus laevis skin secretion predominantly cleaved at the Lys12-Ile13 bond
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-
?
substance P + H2O
RPKQQF + Phe-Gly + Leu-Met-NH2
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cleavage of Gly9-Leu10
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-
?
[Arg0,Leu5,Arg6]enkephalin + H2O
?
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heptapeptide Arg-Tyr-Gly-Gly-Phe-Leu-Arg, cleavage site: Phe5-Leu6
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-
?
[Arg0,Leu5]enkephalin + H2O
?
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hexapeptide Arg-Tyr-Gly-Gly-Phe-Leu, cleavage site: Phe4-Leu5
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-
?
[D-Arg8]-kermit + H2O
?
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model substrate, derivative of kermit i.e. Asp-Val-Asp-Glu-Arg-Asp-Val-Arg-Gly-Phe-Ala-Ser-Phe-Leu-NH2, cleavage site: Ser12-Phe13
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-
?
[Leu5,Arg6]enkephalin + H2O
?
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hexapeptide Tyr-Gly-Gly-Phe-Leu-Arg, cleavage site: Phe4-Leu5
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-
?
[Leu5,Ile6]enkephalin + H2O
?
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hexapeptide Tyr-Gly-Gly-Phe-Leu-Ile, cleavage site: Phe4-Leu5
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-
?
[Leu5,Lys6]enkephalin + H2O
?
-
hexapeptide Tyr-Gly-Gly-Phe-Leu-Lys, cleavage site: Phe4-Leu5
-
-
?
(5-28)ANF + H2O
ANF(5-25) + Phe26-Arg27-Tyr28
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i.e. atrial natriuretic factor, cleavage site: exclusively Ser25-Phe26
-
?
angiotensin II + H2O
?
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe, cleavage site: Tyr4-Ile5
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-
?
angiotensin II + H2O
?
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe, cleavage site: Tyr4-Ile5
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-
?
Antibacterial peptide PGLa + H2O
?
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i.e. Gly-Met-Ala-Ser-Lys-Ala-Gly-Ala-Ile-Ala-Gly-Lys-Ile-Ala-Lys-Val-Ala-Leu-Lys-Ala-Leu-NH2, a peptide of Xenopus laevis skin secretion, cleavage site: Lys12-Ile13
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-
?
bradykinin + H2O
?
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, major cleavage site: Gly4-Phe5, minor site: Pro7-Pro8
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-
?
bradykinin + H2O
?
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i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, major cleavage site: Gly4-Phe5, minor site: Pro7-Pro8
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-
?
Neurokinin A + H2O
?
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i.e. substance K or neuromedin L, His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2, cleavage site: Gly8-Leu9, not Ser5-Phe6
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-
?
Neuromedin C + H2O
?
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Gly-Asn-His-Trp-Ala-Val-Gly-His-Leu-Met-NH2, major cleavage site: His8-Leu9, minor site: Gly7-His8
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-
?
Neuromedin C + H2O
?
-
Gly-Asn-His-Trp-Ala-Val-Gly-His-Leu-Met-NH2, major cleavage site: His8-Leu9, minor site: Gly7-His8
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-
?
Somatostatin-14 + H2O
?
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i.e. Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys, cleavage site: Phe6-Phe7 within disulfide bridged segment yielding one single product
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-
?
Somatostatin-14 + H2O
?
-
i.e. Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys, cleavage site: Phe6-Phe7 within disulfide bridged segment yielding one single product
-
-
?
Somatostatin-14 + H2O
?
-
cleavage of Phe-Phe in the intersulfide bridge motif
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-
?
Substance P + H2O
?
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major cleavage site: Gly9-Leu10, minor site: Phe7-Phe8
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-
?
Substance P + H2O
?
-
i.e. Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2
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-
?
Substance P + H2O
?
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major cleavage site: Gly9-Leu10, minor site: Phe7-Phe8
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-
?
additional information
?
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no cleavage of analogous bonds in [Leu5]-enkephalin, oxytocin, vasopressin
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?
additional information
?
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minimal peptide chain length required: 6 amino acids
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?
additional information
?
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exhibits preference for cleavage on amino-terminal side of Phe, Leu or Ile in Xaa-Leu, Xaa-Phe or Xaa-Ile dipeptide
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-
?
additional information
?
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no cleavage of analogous bonds in [Leu5]-enkephalin, oxytocin, vasopressin
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?
additional information
?
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substance P-(7-11)-peptide, [Val26]-(21-28)ANF-peptide or [Ala26]-(21-28)ANF-peptide
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-
?
additional information
?
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hydrolyzes bonds on amino-terminus of hydrophobic amino acids, thermolysin-like cleavage
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?
additional information
?
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might be involved in inactivation of a great number of peptide hormones
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-
?
additional information
?
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might be involved in inactivation of a great number of peptide hormones
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-
?
additional information
?
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no cleavage of (Leu5)-enkephalin and (Met5)-enkephalin
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
might be involved in inactivation of a great number of peptide hormones
-
-
?
additional information
?
-
-
might be involved in inactivation of a great number of peptide hormones
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(24-28)ANF pentapeptide
-
i.e. Asn-Ser-Phe-Arg-Tyr, weak, substance P as substrate, inhibits cleavage of Gly9-Leu10 and Phe7-Phe8 bonds
(25-28)ANF tetrapeptide
-
i.e. Ser-Phe-Arg-Tyr, weak, substance P as substrate, inhibits cleavage of Gly9-Leu10 and Phe7-Phe8 bonds
CP-96345
-
non-peptide agonist of substance P, substance P as substrate, inhibits cleavage of Gly9-Leu10 bond
Pentapeptides reproducing or mimicking the COOH-terminal sequence of ANF
-
24-28 ANF as substrate
-
RP 67580
-
non-peptide agonist of substance P, substance P as substrate, inhibits cleavage of Gly9-Leu10 bond
1,10-phenanthroline
-
0.01 or 0.05 mM Zn2+, Ca2+ or Mn2+ fully restores; metalloendopeptidase character
thiorphan
-
i.e. 3-mercapto-2-benzyl-propanoylglycine, only at high concentrations, above 0.001 mM
additional information
-
no inhibition by N-tosyl-L-Phe chloromethyl ketone (i.e. TPCK); pepstatin, guanidylethylmercaptosuccinic acid (i.e. GEMSA), captopril, aprotinin, soybean trypsin inhibitor (i.e. STI), PMSF, IAA
-
additional information
-
pepstatin, guanidylethylmercaptosuccinic acid (i.e. GEMSA), captopril, aprotinin, soybean trypsin inhibitor (i.e. STI), PMSF, IAA; retrothiorphan
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
about half-maximal activity at pH 6 and about 75% of maximal activity at pH 8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, in 10 mM potassium phosphate buffer, pH 7.5, 0.05% Nonidet P-40, at least 3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2000fold purified by a four-step fractionation including successively ion-exchange column, hydrophobic chromatographies and gel filtration
-
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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
brenda
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
brenda
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
brenda
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
-
brenda
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