Literature summary extracted from

Megias, C.; Yust, M.d.M.; Pedroche, J.; Lquari, H.; Giron-Calle, J.; Alaiz, M.; Millan, F.; Vioque, J.
Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates (2004), J. Agric. Food Chem., 52, 1928-1932.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
3.4.15.1	Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser	the peptide corresponds to a fragment of helianthinin, the 11S globulin from sunflower seeds, which is the main storage protein in sunflower. Sunflower seed proteins are a potential source of angiotensin-converting enzyme inhibitory peptides when hydrolyzed with pepsin and pancreatin	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	lung	-	Sus scrofa	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.4.15.1	hippuryl-His-Leu + H2O	-	Sus scrofa	hippuric acid + His-Leu	-	?

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Release 2023.1 (January 2023)