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Literature summary for 3.4.24.16 extracted from

  • Yoshikawa, S.; Tashiro, T.; Takahashi, K.
    Specificity of action on neuropeptides of an endopeptidase from the synaptosomal membranes of guinea pig brain (1988), J. Biochem., 104, 1007-1010.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane synaptosomal Cavia porcellus 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Cavia porcellus possible implication of the enzyme in the specific degradation of neurotensin and other peptide neurotransmitters in the synaptic cleft ?
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?

Organism

Organism UniProt Comment Textmining
Cavia porcellus
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-
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Purification (Commentary)

Purification (Comment) Organism
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Cavia porcellus

Source Tissue

Source Tissue Comment Organism Textmining
brain
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Cavia porcellus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O i.e. substance P, cleavage sites: Pro4-Gln5, Gln5-Gln6, Gln6-Phe7 Cavia porcellus Arg-Pro-Lys-Pro-Gln + Gln-Phe-Phe-Gly-Leu-Met-NH2 + Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly-Leu-Met-NH2 + Arg-Pro-Lys-Pro
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?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O i.e. bradykinin, cleavage site: Phe5-Ser6 Cavia porcellus Arg-Pro-Pro-Gly-Phe + Ser-Pro-Phe-Arg
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?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O i.e. angiotensin I, cleavage site: Pro7-Phe8 Cavia porcellus Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
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?
additional information marked specificity towards Pro-X bonds present in the interior parts of various neuropeptides and related peptides. No cleavage is observed at the first and second peptide bonds from the NH2-terimini or from the COOH-terminal extension of the peptides examined, suggesting that the enzyme requires both NH2- and COOH-terminal extensions of at least 3 residues from the scissile bond for its action. Not strictly specific for Pro-X bonds Cavia porcellus ?
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?
additional information possible implication of the enzyme in the specific degradation of neurotensin and other peptide neurotransmitters in the synaptic cleft Cavia porcellus ?
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?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O i.e. neurotensin Cavia porcellus pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
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?
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu + H2O specific hydrolysis of the Pro10-Tyr11 bond Cavia porcellus pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro + Tyr-Ile-Leu
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?
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro + H2O i.e. beta-neoendorphin, cleavage sites: Leu5-Arg6, Arg6-Lys7 Cavia porcellus Tyr-Gly-Gly-Phe-Leu + Arg-Lys-Tyr-Pro + Tyr-Gly-Gly-Phe-Leu-Arg + Lys-Tyr-Pro
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?
Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-Gly-Arg-Pro-Glu + H2O i.e. BAM-12P, cleavage sites: Phe4-Met5, Arg6-Arg7, Gly9-Arg10 Cavia porcellus Tyr-Gly-Gly-Phe + Met-Arg-Arg-Val-Gly + Arg-Pro-Glu + Tyr-Gly-Gly-Phe-Met-Arg + -Arg-Val-Gly
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?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O i.e. beta-casomorphin, cleavage site: Pro4-Gly5 Cavia porcellus Tyr-Pro-Phe-Pro + Gly-Pro-Ile
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?