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Literature summary extracted from

  • Mallikarjun Gouda, K.G.; Gowda, L.R.; Rao, A.G.; Prakash, V.
    Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max) (2006), J. Agric. Food Chem., 54, 4568-4573.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.15.1 medicine the peptide Val-Leu-Ile-Val-Pro is resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.15.1 glycinin hydrolysate
-
 Sus scrofa
3.4.15.1 Val-Leu-Ile-Val-Pro IC50: 0.00169 mM. The peptide is resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.4.15.1 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.15.1 kidney
-
 Sus scrofa
-
3.4.15.1 lung
-
 Sus scrofa
-

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.15.1 0.0045
-
 Val-Leu-Ile-Val-Pro
-
 Sus scrofa

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.4.15.1 0.00169
-
 IC50: 0.00169 mM. The peptide is resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods Sus scrofa Val-Leu-Ile-Val-Pro