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Literature summary for 3.4.15.1 extracted from

  • Nakagomi, K.; Yamada, R.; Ebisu, H.; Sadakane, Y.; Akizawa, T.; Tanimura, T.
    Isolation of acein-2, a novel angiotensin-I-converting enzyme inhibitory peptide derived from a tryptic hydrolysate of human plasma (2000), FEBS Lett., 467, 235-238.
    View publication on PubMed

Application

Application Comment Organism
medicine acein-2 as well as acein-1 can be used as a starting material for anti-hypertensive drugs against ACE Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
Leu-Ile-Tyr i.e. acein-2, isolated from tryptic hydrolysate of human plasma, non-competitive inhibitor, IC50: 0.00082 mM. Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
lung
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hippuryl-His-Leu + H2O
-
Oryctolagus cuniculus hippuric acid + His-Leu
-
?

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00082
-
i.e. acein-2, isolated from tryptic hydrolysate of human plasma, non-competitive inhibitor, IC50: 0.00082 mM. Oryctolagus cuniculus Leu-Ile-Tyr