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Literature summary for 3.4.14.2 extracted from

  • Sentandreu, M.A.; Toldra, F.
    Evaluation of ACE inhibitory activity of dipeptides generated by the action of porcine muscle dipeptidyl peptidases (2007), Food Chem., 102, 511-515.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation and anion exchange chromatography Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Ala-p-nitroanilide + H2O 481% activity compared to Gly-Pro-7-amido-4-methylcoumarin Sus scrofa Ala-Ala + p-nitroaniline
-
?
Arg-Pro-p-nitroanilide + H2O 591% activity compared to Gly-Pro-7-amido-4-methylcoumarin Sus scrofa Arg-Pro + p-nitroaniline
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O 100% activity Sus scrofa Gly-Pro + 7-amino-4-methylcoumarin
-
?
Gly-Pro-p-nitroanilide + H2O 562% activity compared to Gly-Pro-7-amido-4-methylcoumarin Sus scrofa Gly-Pro + p-nitroaniline
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O 38% activity compared to Gly-Pro-7-amido-4-methylcoumarin Sus scrofa Lys-Ala + 7-amino-4-methylcoumarin
-
?
additional information no activity with Gly-Arg-7-amido-4-methylcoumarin, Arg-Arg-7-amido-4-methylcoumarin, and Ala-Arg-7-amido-4-methylcoumarin Sus scrofa ?
-
?

Synonyms

Synonyms Comment Organism
dipeptidyl peptidase
-
Sus scrofa
DPP
-
Sus scrofa