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Literature summary for 3.4.24.15 extracted from

  • Dahms, P.; Mentlein, R.
    Purification of the main somatostatin-degrading proteases from rat and pig brains, their action on other neuropeptides, and their identification as endopeptidases 24.15 and 24.16 (1992), Eur. J. Biochem., 208, 145-154.
    View publication on PubMed
Search for more literature for 3.4.24.15

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
 Rattus norvegicus
1,10-phenanthroline
-
 Sus scrofa
Arg-Pro-Lys-Pro
-
 Sus scrofa
EDTA
-
 Rattus norvegicus
EDTA
-
 Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ 0.001 mM, stimulates Rattus norvegicus
Zn2+ 0.001 mM, stimulates Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000 70000 gel filtration Rattus norvegicus
66000 70000 gel filtration Sus scrofa
70000
-
 1 * 70000, SDS-PAGE Rattus norvegicus
70000
-
 1 * 70000, SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-
brain
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.006
-
-
 Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O i.e. somatostatin, cleavage sites: Asn5-Phe6, Phe6-Phe7 and Thr10-Phe11 Rattus norvegicus ?
-
 ?
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys + H2O i.e. somatostatin, cleavage sites: Asn5-Phe6, Phe6-Phe7 and Thr10-Phe11 Sus scrofa ?
-
 ?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O i.e. substance P, cleavage sites: Gln5-Gln6, Phe7-Phe8, Phe8-Gly9 Rattus norvegicus peptide fragments
-
 ?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met + H2O i.e. substance P, cleavage sites: Gln5-Gln6, Phe7-Phe8, Phe8-Gly9 Sus scrofa peptide fragments
-
 ?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O i.e. bradykinin, cleavage site: Phe5-Ser6 Rattus norvegicus Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
 ?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O i.e. bradykinin, cleavage site: Phe5-Ser6 Sus scrofa Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
-
 ?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O i.e. angiotensin II, cleavage site: Tyr4-Ile5 Rattus norvegicus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O i.e. angiotensin II, cleavage site: Tyr4-Ile5 Sus scrofa Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
cholecystokinin-8 sulfated Rattus norvegicus peptide fragments
-
 ?
cholecystokinin-8 sulfated Sus scrofa peptide fragments
-
 ?
corticotropin-like intermediate lobe peptide
-
 Rattus norvegicus peptide fragments
-
 ?
corticotropin-like intermediate lobe peptide
-
 Sus scrofa peptide fragments
-
 ?
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O i.e. luteinizing hormone-releasing hormone Rattus norvegicus pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
-
 ?
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 + H2O i.e. luteinizing hormone-releasing hormone Sus scrofa pGlu-His-Trp-Ser-Tyr + Gly-Leu-Arg-Pro-Gly-NH2
-
 ?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu i.e. neurotensin Rattus norvegicus pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg + Arg-Pro-Tyr-Ile-Leu
-
 ?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu i.e. neurotensin Sus scrofa pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg + Arg-Pro-Tyr-Ile-Leu
-
 ?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
-
 Rattus norvegicus Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
-
 ?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
-
 Sus scrofa Tyr-Gly-Gly-Phe-Leu + Arg-Arg-Ile
-
 ?
vasoactive intestinal peptide
-
 Rattus norvegicus peptide fragments
-
 ?
vasoactive intestinal peptide
-
 Sus scrofa peptide fragments
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 70000, SDS-PAGE Rattus norvegicus
monomer 1 * 70000, SDS-PAGE Sus scrofa